Q8WWQ8 · STAB2_HUMAN
- ProteinStabilin-2
- GeneSTAB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2551 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalization as well as HA and CS.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endocytic vesicle membrane | |
Cellular Component | external side of plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | hyaluronic acid binding | |
Molecular Function | low-density lipoprotein particle binding | |
Molecular Function | low-density lipoprotein particle receptor activity | |
Molecular Function | protein-disulfide reductase activity | |
Molecular Function | scavenger receptor activity | |
Biological Process | angiogenesis | |
Biological Process | cell adhesion | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | endocytosis | |
Biological Process | hyaluronan catabolic process | |
Biological Process | receptor-mediated endocytosis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStabilin-2
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WWQ8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Only a small amount appears to be present at the cell surface (PubMed:17145755).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-2458 | Extracellular | ||||
Sequence: SPAETTGQARRCDRKSLLTIRTECRSCALNLGVKCPDGYTMITSGSVGVRDCRYTFEVRTYSLSLPGCRHICRKDYLQPRCCPGRWGPDCIECPGGAGSPCNGRGSCAEGMEGNGTCSCQEGFGGTACETCADDNLFGPSCSSVCNCVHGVCNSGLDGDGTCECYSAYTGPKCDKPIPECAALLCPENSRCSPSTEDENKLECKCLPNYRGDGKYCDPINPCLRKICHPHAHCTYLGPNRHSCTCQEGYRGDGQVCLPVDPCQINFGNCPTKSTVCKYDGPGQSHCECKEHYQNFVPGVGCSMTDICKSDNPCHRNANCTTVAPGRTECICQKGYVGDGLTCYGNIMERLRELNTEPRGKWQGRLTSFISLLDKAYAWPLSKLGPFTVLLPTDKGLKGFNVNELLVDNKAAQYFVKLHIIAGQMNIEYMNNTDMFYTLTGKSGEIFNSDKDNQIKLKLHGGKKKVKIIQGDIIASNGLLHILDRAMDKLEPTFESNNEQTIMTMLQPRYSKFRSLLEETNLGHALDEDGVGGPYTIFVPNNEALNNMKDGTLDYLLSPEGSRKLLELVRYHIVPFTQLEVATLISTPHIRSMANQLIQFNTTDNGQILANDVAMEEIEITAKNGRIYTLTGVLIPPSIVPILPHRCDETKREMKLGTCVSCSLVYWSRCPANSEPTALFTHRCVYSGRFGSLKSGCARYCNATVKIPKCCKGFYGPDCNQCPGGFSNPCSGNGQCADSLGGNGTCICEEGFQGSQCQFCSDPNKYGPRCNKKCLCVHGTCNNRIDSDGACLTGTCRDGSAGRLCDKQTSACGPYVQFCHIHATCEYSNGTASCICKAGYEGDGTLCSEMDPCTGLTPGGCSRNAECIKTGTGTHTCVCQQGWTGNGRDCSEINNCLLPSAGGCHDNASCLYVGPGQNECECKKGFRGNGIDCEPITSCLEQTGKCHPLASCQSTSSGVWSCVCQEGYEGDGFLCYGNAAVELSFLSEAAIFNRWINNASLQPTLSATSNLTVLVPSQQATEDMDQDEKSFWLSQSNIPALIKYHMLLGTYRVADLQTLSSSDMLATSLQGNFLHLAKVDGNITIEGASIVDGDNAATNGVIHIINKVLVPQRRLTGSLPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVLEIQKNRCDNNDTTIIRGRCRTCSSELTCPFGTKSLGNEKRRCIYTSYFMGRRTLFIGCQPKCVRTVITRECCAGFFGPQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQGPLGDGSCDCDVGWRGVHCDNATTEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICTAINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCLEINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCTLINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFTCRGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLLSPKNLLITPKDNSGRILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLLIDPTLGGRCDTFTTFDASGECGSCVNTPSCPRWSKPKGVKQKCLYNLPFKRNLEGCRERCSLVIQIPRCCKGYFGRDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDDGITGSGQCLCETGWTGPSCDTQAVLPAVCTPPCSAHATCKENNTCECNLDYEGDGITCTVVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCTEIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCEPEQLPIDRCLQDNGQCHADAKCVDLHFQDTTVGVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYRMKDVNCTCKVGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPLKAPPAPVTLTHT | ||||||
Transmembrane | 2459-2479 | Helical | ||||
Sequence: GLGAGIFFAIILVTGAVALAA | ||||||
Topological domain | 2480-2551 | Cytoplasmic | ||||
Sequence: YSYFRINRRTIGFQHFESEEDINVAALGKQQPENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048995 | 110 | in dbSNP:rs17034186 | |||
Sequence: I → V | ||||||
Natural variant | VAR_048996 | 306 | in dbSNP:rs12319476 | |||
Sequence: E → K | ||||||
Natural variant | VAR_019541 | 510 | in dbSNP:rs1609860 | |||
Sequence: P → H | ||||||
Natural variant | VAR_048997 | 787 | in dbSNP:rs17034336 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_048998 | 881 | in dbSNP:rs7973658 | |||
Sequence: R → H | ||||||
Natural variant | VAR_048999 | 1736 | in dbSNP:rs17034433 | |||
Sequence: N → T | ||||||
Natural variant | VAR_049000 | 2039 | in dbSNP:rs7306642 | |||
Sequence: P → T | ||||||
Natural variant | VAR_049001 | 2401 | in dbSNP:rs2271637 | |||
Sequence: L → V | ||||||
Natural variant | VAR_049002 | 2519 | in dbSNP:rs3751197 | |||
Sequence: Y → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,166 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-19 | UniProt | |||||
Sequence: MMLQHLVIFCLGLVVQNFC | |||||||
Chain | PRO_0000007712 | 20-2551 | UniProt | Stabilin-2 | |||
Sequence: SPAETTGQARRCDRKSLLTIRTECRSCALNLGVKCPDGYTMITSGSVGVRDCRYTFEVRTYSLSLPGCRHICRKDYLQPRCCPGRWGPDCIECPGGAGSPCNGRGSCAEGMEGNGTCSCQEGFGGTACETCADDNLFGPSCSSVCNCVHGVCNSGLDGDGTCECYSAYTGPKCDKPIPECAALLCPENSRCSPSTEDENKLECKCLPNYRGDGKYCDPINPCLRKICHPHAHCTYLGPNRHSCTCQEGYRGDGQVCLPVDPCQINFGNCPTKSTVCKYDGPGQSHCECKEHYQNFVPGVGCSMTDICKSDNPCHRNANCTTVAPGRTECICQKGYVGDGLTCYGNIMERLRELNTEPRGKWQGRLTSFISLLDKAYAWPLSKLGPFTVLLPTDKGLKGFNVNELLVDNKAAQYFVKLHIIAGQMNIEYMNNTDMFYTLTGKSGEIFNSDKDNQIKLKLHGGKKKVKIIQGDIIASNGLLHILDRAMDKLEPTFESNNEQTIMTMLQPRYSKFRSLLEETNLGHALDEDGVGGPYTIFVPNNEALNNMKDGTLDYLLSPEGSRKLLELVRYHIVPFTQLEVATLISTPHIRSMANQLIQFNTTDNGQILANDVAMEEIEITAKNGRIYTLTGVLIPPSIVPILPHRCDETKREMKLGTCVSCSLVYWSRCPANSEPTALFTHRCVYSGRFGSLKSGCARYCNATVKIPKCCKGFYGPDCNQCPGGFSNPCSGNGQCADSLGGNGTCICEEGFQGSQCQFCSDPNKYGPRCNKKCLCVHGTCNNRIDSDGACLTGTCRDGSAGRLCDKQTSACGPYVQFCHIHATCEYSNGTASCICKAGYEGDGTLCSEMDPCTGLTPGGCSRNAECIKTGTGTHTCVCQQGWTGNGRDCSEINNCLLPSAGGCHDNASCLYVGPGQNECECKKGFRGNGIDCEPITSCLEQTGKCHPLASCQSTSSGVWSCVCQEGYEGDGFLCYGNAAVELSFLSEAAIFNRWINNASLQPTLSATSNLTVLVPSQQATEDMDQDEKSFWLSQSNIPALIKYHMLLGTYRVADLQTLSSSDMLATSLQGNFLHLAKVDGNITIEGASIVDGDNAATNGVIHIINKVLVPQRRLTGSLPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVLEIQKNRCDNNDTTIIRGRCRTCSSELTCPFGTKSLGNEKRRCIYTSYFMGRRTLFIGCQPKCVRTVITRECCAGFFGPQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQGPLGDGSCDCDVGWRGVHCDNATTEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICTAINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCLEINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCTLINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFTCRGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLLSPKNLLITPKDNSGRILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLLIDPTLGGRCDTFTTFDASGECGSCVNTPSCPRWSKPKGVKQKCLYNLPFKRNLEGCRERCSLVIQIPRCCKGYFGRDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDDGITGSGQCLCETGWTGPSCDTQAVLPAVCTPPCSAHATCKENNTCECNLDYEGDGITCTVVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCTEIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCEPEQLPIDRCLQDNGQCHADAKCVDLHFQDTTVGVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYRMKDVNCTCKVGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPLKAPPAPVTLTHTGLGAGIFFAIILVTGAVALAAYSYFRINRRTIGFQHFESEEDINVAALGKQQPENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL | |||||||
Disulfide bond | 112↔126 | UniProt | |||||
Sequence: CPGGAGSPCNGRGSC | |||||||
Disulfide bond | 120↔136 | UniProt | |||||
Sequence: CNGRGSCAEGMEGNGTC | |||||||
Glycosylation | 133 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 138↔147 | UniProt | |||||
Sequence: CQEGFGGTAC | |||||||
Disulfide bond | 160↔171 | UniProt | |||||
Sequence: CSSVCNCVHGVC | |||||||
Disulfide bond | 164↔181 | UniProt | |||||
Sequence: CNCVHGVCNSGLDGDGTC | |||||||
Disulfide bond | 183↔192 | UniProt | |||||
Sequence: CYSAYTGPKC | |||||||
Disulfide bond | 199↔210 | UniProt | |||||
Sequence: CAALLCPENSRC | |||||||
Disulfide bond | 204↔222 | UniProt | |||||
Sequence: CPENSRCSPSTEDENKLEC | |||||||
Disulfide bond | 224↔235 | UniProt | |||||
Sequence: CLPNYRGDGKYC | |||||||
Disulfide bond | 241↔252 | UniProt | |||||
Sequence: CLRKICHPHAHC | |||||||
Disulfide bond | 246↔262 | UniProt | |||||
Sequence: CHPHAHCTYLGPNRHSC | |||||||
Disulfide bond | 264↔275 | UniProt | |||||
Sequence: CQEGYRGDGQVC | |||||||
Disulfide bond | 326↔338 | UniProt | |||||
Sequence: CKSDNPCHRNANC | |||||||
Disulfide bond | 332↔348 | UniProt | |||||
Sequence: CHRNANCTTVAPGRTEC | |||||||
Glycosylation | 337 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 350↔361 | UniProt | |||||
Sequence: CQKGYVGDGLTC | |||||||
Glycosylation | 449 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 619 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 720 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 740↔754 | UniProt | |||||
Sequence: CPGGFSNPCSGNGQC | |||||||
Disulfide bond | 748↔764 | UniProt | |||||
Sequence: CSGNGQCADSLGGNGTC | |||||||
Glycosylation | 761 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 766↔775 | UniProt | |||||
Sequence: CEEGFQGSQC | |||||||
Disulfide bond | 830↔843 | UniProt | |||||
Sequence: CGPYVQFCHIHATC | |||||||
Disulfide bond | 837↔852 | UniProt | |||||
Sequence: CHIHATCEYSNGTASC | |||||||
Glycosylation | 847 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 854↔865 | UniProt | |||||
Sequence: CKAGYEGDGTLC | |||||||
Disulfide bond | 871↔885 | UniProt | |||||
Sequence: CTGLTPGGCSRNAEC | |||||||
Disulfide bond | 879↔895 | UniProt | |||||
Sequence: CSRNAECIKTGTGTHTC | |||||||
Disulfide bond | 897↔908 | UniProt | |||||
Sequence: CQQGWTGNGRDC | |||||||
Disulfide bond | 914↔928 | UniProt | |||||
Sequence: CLLPSAGGCHDNASC | |||||||
Disulfide bond | 922↔938 | UniProt | |||||
Sequence: CHDNASCLYVGPGQNEC | |||||||
Glycosylation | 925 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 940↔951 | UniProt | |||||
Sequence: CKKGFRGNGIDC | |||||||
Disulfide bond | 957↔970 | UniProt | |||||
Sequence: CLEQTGKCHPLASC | |||||||
Disulfide bond | 964↔980 | UniProt | |||||
Sequence: CHPLASCQSTSSGVWSC | |||||||
Glycosylation | 1016 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1028 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1100 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Chain | PRO_0000007713 | 1136-2551 | UniProt | 190 kDa form stabilin-2 | |||
Sequence: SLPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVLEIQKNRCDNNDTTIIRGRCRTCSSELTCPFGTKSLGNEKRRCIYTSYFMGRRTLFIGCQPKCVRTVITRECCAGFFGPQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQGPLGDGSCDCDVGWRGVHCDNATTEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICTAINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCLEINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCTLINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFTCRGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLLSPKNLLITPKDNSGRILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLLIDPTLGGRCDTFTTFDASGECGSCVNTPSCPRWSKPKGVKQKCLYNLPFKRNLEGCRERCSLVIQIPRCCKGYFGRDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDDGITGSGQCLCETGWTGPSCDTQAVLPAVCTPPCSAHATCKENNTCECNLDYEGDGITCTVVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCTEIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCEPEQLPIDRCLQDNGQCHADAKCVDLHFQDTTVGVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYRMKDVNCTCKVGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPLKAPPAPVTLTHTGLGAGIFFAIILVTGAVALAAYSYFRINRRTIGFQHFESEEDINVAALGKQQPENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL | |||||||
Glycosylation | 1247 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1275 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1348↔1362 | UniProt | |||||
Sequence: CPGNAQNVCFGNGIC | |||||||
Disulfide bond | 1356↔1372 | UniProt | |||||
Sequence: CFGNGICLDGVNGTGVC | |||||||
Glycosylation | 1367 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1374↔1383 | UniProt | |||||
Sequence: CGEGFSGTAC | |||||||
Disulfide bond | 1395↔1406 | UniProt | |||||
Sequence: CDQACSCVHGRC | |||||||
Disulfide bond | 1399↔1416 | UniProt | |||||
Sequence: CSCVHGRCNQGPLGDGSC | |||||||
Disulfide bond | 1418↔1427 | UniProt | |||||
Sequence: CDVGWRGVHC | |||||||
Glycosylation | 1429 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1436↔1446 | UniProt | |||||
Sequence: CNGTCHTSANC | |||||||
Glycosylation | 1437 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1440↔1456 | UniProt | |||||
Sequence: CHTSANCLTNSDGTASC | |||||||
Disulfide bond | 1458↔1469 | UniProt | |||||
Sequence: CAAGFQGNGTIC | |||||||
Glycosylation | 1465 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1475↔1488 | UniProt | |||||
Sequence: CEISNGGCSAKADC | |||||||
Disulfide bond | 1482↔1498 | UniProt | |||||
Sequence: CSAKADCKRTTPGRRVC | |||||||
Disulfide bond | 1500↔1511 | UniProt | |||||
Sequence: CKAGYTGDGIVC | |||||||
Disulfide bond | 1517↔1530 | UniProt | |||||
Sequence: CLENHGGCDKNAEC | |||||||
Disulfide bond | 1524↔1540 | UniProt | |||||
Sequence: CDKNAECTQTGPNQAAC | |||||||
Disulfide bond | 1542↔1553 | UniProt | |||||
Sequence: CLPAYTGDGKVC | |||||||
Disulfide bond | 1559↔1572 | UniProt | |||||
Sequence: CLTKNGGCSEFAIC | |||||||
Disulfide bond | 1566↔1582 | UniProt | |||||
Sequence: CSEFAICNHTGQVERTC | |||||||
Glycosylation | 1573 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1679 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1743 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1962↔1976 | UniProt | |||||
Sequence: CPGGPDAPCNNRGVC | |||||||
Disulfide bond | 1970↔1986 | UniProt | |||||
Sequence: CNNRGVCLDQYSATGEC | |||||||
Disulfide bond | 1988↔1997 | UniProt | |||||
Sequence: CNTGFNGTAC | |||||||
Glycosylation | 1993 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2009↔2020 | UniProt | |||||
Sequence: CLPCGCSDHGQC | |||||||
Disulfide bond | 2014↔2030 | UniProt | |||||
Sequence: CSDHGQCDDGITGSGQC | |||||||
Disulfide bond | 2032↔2041 | UniProt | |||||
Sequence: CETGWTGPSC | |||||||
Disulfide bond | 2051↔2061 | UniProt | |||||
Sequence: CTPPCSAHATC | |||||||
Disulfide bond | 2055↔2067 | UniProt | |||||
Sequence: CSAHATCKENNTC | |||||||
Glycosylation | 2064 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 2069↔2080 | UniProt | |||||
Sequence: CNLDYEGDGITC | |||||||
Disulfide bond | 2086↔2099 | UniProt | |||||
Sequence: CKQDNGGCAKVARC | |||||||
Disulfide bond | 2093↔2108 | UniProt | |||||
Sequence: CAKVARCSQKGTKVSC | |||||||
Disulfide bond | 2110↔2121 | UniProt | |||||
Sequence: CQKGYKGDGHSC | |||||||
Disulfide bond | 2127↔2141 | UniProt | |||||
Sequence: CADGLNGGCHEHATC | |||||||
Disulfide bond | 2135↔2151 | UniProt | |||||
Sequence: CHEHATCKMTGPGKHKC | |||||||
Disulfide bond | 2153↔2164 | UniProt | |||||
Sequence: CKSHYVGDGLNC | |||||||
Disulfide bond | 2220↔2289 | UniProt | |||||
Sequence: CANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFC | |||||||
Disulfide bond | 2244↔2265 | UniProt | |||||
Sequence: CSAGWLETGRVAYPTAFASQNC | |||||||
Glycosylation | 2280 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2296 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2336 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 2352 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 2368 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2382 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 2393 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 2497 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Glycosylated.
Proteolytically processed to yield a 190 kDa protein.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in sinusoidal endothelial cells of liver, spleen and lymph nodes. Also expressed in non SEC-cells such as HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type 1-associated myelopathy), and several macrophage cell line.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GULP1 and heparin. Also interacts with alpha-M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or TMSB4Y).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q8WWQ8 | Tmsb4x P20065 | 3 | EBI-7945957, EBI-7946048 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 108-148 | EGF-like 1 | ||||
Sequence: DCIECPGGAGSPCNGRGSCAEGMEGNGTCSCQEGFGGTACE | ||||||
Domain | 156-193 | EGF-like 2 | ||||
Sequence: FGPSCSSVCNCVHGVCNSGLDGDGTCECYSAYTGPKCD | ||||||
Domain | 195-236 | EGF-like 3 | ||||
Sequence: PIPECAALLCPENSRCSPSTEDENKLECKCLPNYRGDGKYCD | ||||||
Domain | 237-276 | EGF-like 4 | ||||
Sequence: PINPCLRKICHPHAHCTYLGPNRHSCTCQEGYRGDGQVCL | ||||||
Domain | 322-362 | EGF-like 5 | ||||
Sequence: MTDICKSDNPCHRNANCTTVAPGRTECICQKGYVGDGLTCY | ||||||
Domain | 371-505 | FAS1 1 | ||||
Sequence: ELNTEPRGKWQGRLTSFISLLDKAYAWPLSKLGPFTVLLPTDKGLKGFNVNELLVDNKAAQYFVKLHIIAGQMNIEYMNNTDMFYTLTGKSGEIFNSDKDNQIKLKLHGGKKKVKIIQGDIIASNGLLHILDRAM | ||||||
Domain | 515-652 | FAS1 2 | ||||
Sequence: NNEQTIMTMLQPRYSKFRSLLEETNLGHALDEDGVGGPYTIFVPNNEALNNMKDGTLDYLLSPEGSRKLLELVRYHIVPFTQLEVATLISTPHIRSMANQLIQFNTTDNGQILANDVAMEEIEITAKNGRIYTLTGVL | ||||||
Domain | 736-776 | EGF-like 6 | ||||
Sequence: DCNQCPGGFSNPCSGNGQCADSLGGNGTCICEEGFQGSQCQ | ||||||
Domain | 826-866 | EGF-like 7 | ||||
Sequence: QTSACGPYVQFCHIHATCEYSNGTASCICKAGYEGDGTLCS | ||||||
Domain | 867-909 | EGF-like 8 | ||||
Sequence: EMDPCTGLTPGGCSRNAECIKTGTGTHTCVCQQGWTGNGRDCS | ||||||
Domain | 910-952 | EGF-like 9 | ||||
Sequence: EINNCLLPSAGGCHDNASCLYVGPGQNECECKKGFRGNGIDCE | ||||||
Domain | 953-992 | EGF-like 10 | ||||
Sequence: PITSCLEQTGKCHPLASCQSTSSGVWSCVCQEGYEGDGFL | ||||||
Domain | 994-1127 | FAS1 3 | ||||
Sequence: YGNAAVELSFLSEAAIFNRWINNASLQPTLSATSNLTVLVPSQQATEDMDQDEKSFWLSQSNIPALIKYHMLLGTYRVADLQTLSSSDMLATSLQGNFLHLAKVDGNITIEGASIVDGDNAATNGVIHIINKVL | ||||||
Domain | 1137-1265 | FAS1 4 | ||||
Sequence: LPNLLMRLEQMPDYSIFRGYIIQYNLANAIEAADAYTVFAPNNNAIENYIREKKVLSLEEDVLRYHVVLEEKLLKNDLHNGMHRETMLGFSYFLSFFLHNDQLYVNEAPINYTNVATDKGVIHGLGKVL | ||||||
Domain | 1343-1408 | Laminin EGF-like 1 | ||||
Sequence: PQCQPCPGNAQNVCFGNGICLDGVNGTGVCECGEGFSGTACETCTEGKYGIHCDQACSCVHGRCNQ | ||||||
Domain | 1432-1470 | EGF-like 11 | ||||
Sequence: TEDNCNGTCHTSANCLTNSDGTASCKCAAGFQGNGTICT | ||||||
Domain | 1471-1512 | EGF-like 12 | ||||
Sequence: AINACEISNGGCSAKADCKRTTPGRRVCTCKAGYTGDGIVCL | ||||||
Domain | 1513-1554 | EGF-like 13 | ||||
Sequence: EINPCLENHGGCDKNAECTQTGPNQAACNCLPAYTGDGKVCT | ||||||
Domain | 1555-1594 | EGF-like 14 | ||||
Sequence: LINVCLTKNGGCSEFAICNHTGQVERTCTCKPNYIGDGFT | ||||||
Domain | 1596-1724 | FAS1 5 | ||||
Sequence: RGSIYQELPKNPKTSQYFFQLQEHFVKDLVGPGPFTVFAPLSAAFDEEARVKDWDKYGLMPQVLRYHVVACHQLLLENLKLISNATSLQGEPIVISVSQSTVYINNKAKIISSDIISTNGIVHIIDKLL | ||||||
Domain | 1740-1881 | FAS1 6 | ||||
Sequence: ILQNLTTLATNNGYIKFSNLIQDSGLLSVITDPIHTPVTLFWPTDQALHALPAEQQDFLFNQDNKDKLKEYLKFHVIRDAKVLAVDLPTSTAWKTLQGSELSVKCGAGRDIGDLFLNGQTCRIVQRELLFDLGVAYGIDCLL | ||||||
Domain | 1957-2022 | Laminin EGF-like 2 | ||||
Sequence: RDCQACPGGPDAPCNNRGVCLDQYSATGECKCNTGFNGTACEMCWPGRFGPDCLPCGCSDHGQCDD | ||||||
Domain | 2047-2081 | EGF-like 15 | ||||
Sequence: LPAVCTPPCSAHATCKENNTCECNLDYEGDGITCT | ||||||
Domain | 2082-2122 | EGF-like 16 | ||||
Sequence: VVDFCKQDNGGCAKVARCSQKGTKVSCSCQKGYKGDGHSCT | ||||||
Domain | 2123-2165 | EGF-like 17 | ||||
Sequence: EIDPCADGLNGGCHEHATCKMTGPGKHKCECKSHYVGDGLNCE | ||||||
Domain | 2198-2291 | Link | ||||
Sequence: GVFHLRSPLGQYKLTFDKAREACANEAATMATYNQLSYAQKAKYHLCSAGWLETGRVAYPTAFASQNCGSGVVGIVDYGPRPNKSEMWDVFCYR | ||||||
Domain | 2311-2446 | FAS1 7 | ||||
Sequence: SGNLLQVLMSFPSLTNFLTEVLAYSNSSARGRAFLEHLTDLSIRGTLFVPQNSGLGENETLSGRDIEHHLANVSMFFYNDLVNGTTLQTRLGSKLLITASQDPLQPTETRFVDGRAILQWDIFASNGIIHVISRPL | ||||||
Region | 2504-2514 | Interaction with TMSB4X | ||||
Sequence: AALGKQQPENI | ||||||
Compositional bias | 2512-2530 | Polar residues | ||||
Sequence: ENISNPLYESTTSAPPEPS | ||||||
Region | 2512-2551 | Disordered | ||||
Sequence: ENISNPLYESTTSAPPEPSYDPFTDSEERQLEGNDPLRTL | ||||||
Compositional bias | 2533-2551 | Basic and acidic residues | ||||
Sequence: PFTDSEERQLEGNDPLRTL |
Domain
Recognizes phosphatidyl serine via its epidermal growth factor-like domains.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,551
- Mass (Da)276,988
- Last updated2007-04-17 v3
- Checksum3ACB6A6C3CB80044
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 67 | in Ref. 5; BAD18723 | ||||
Sequence: G → R | ||||||
Sequence conflict | 152 | in Ref. 5; BAD18723 | ||||
Sequence: D → A | ||||||
Sequence conflict | 887 | in Ref. 5; BAD18723 | ||||
Sequence: K → N | ||||||
Sequence conflict | 1136 | in Ref. 8; AA sequence | ||||
Sequence: S → L | ||||||
Sequence conflict | 1151 | in Ref. 1; CAC82105 | ||||
Sequence: S → P | ||||||
Sequence conflict | 1276 | in Ref. 1; CAC82105 | ||||
Sequence: D → A | ||||||
Sequence conflict | 1522 | in Ref. 5; BAD18723 | ||||
Sequence: G → C | ||||||
Sequence conflict | 1557 | in Ref. 6; AAO39681 | ||||
Sequence: N → Y | ||||||
Sequence conflict | 1599-1600 | in Ref. 7; AAF82398 | ||||
Sequence: IY → HE | ||||||
Sequence conflict | 1854 | in Ref. 5; BAD18723 | ||||
Sequence: F → S | ||||||
Sequence conflict | 2249 | in Ref. 5; BAD18723 | ||||
Sequence: L → V | ||||||
Sequence conflict | 2253 | in Ref. 5; BAD18723 | ||||
Sequence: R → G | ||||||
Compositional bias | 2512-2530 | Polar residues | ||||
Sequence: ENISNPLYESTTSAPPEPS | ||||||
Compositional bias | 2533-2551 | Basic and acidic residues | ||||
Sequence: PFTDSEERQLEGNDPLRTL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ295695 EMBL· GenBank· DDBJ | CAC82105.1 EMBL· GenBank· DDBJ | mRNA | ||
AB052958 EMBL· GenBank· DDBJ | BAC15608.1 EMBL· GenBank· DDBJ | mRNA | ||
AY311388 EMBL· GenBank· DDBJ | AAP74958.1 EMBL· GenBank· DDBJ | mRNA | ||
AK024503 EMBL· GenBank· DDBJ | BAB15793.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074051 EMBL· GenBank· DDBJ | BAB84877.1 EMBL· GenBank· DDBJ | mRNA | ||
AK160380 EMBL· GenBank· DDBJ | BAD18723.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY227444 EMBL· GenBank· DDBJ | AAO39681.1 EMBL· GenBank· DDBJ | mRNA | ||
AF160476 EMBL· GenBank· DDBJ | AAF82398.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |