Q8IU80 · TMPS6_HUMAN
- ProteinTransmembrane protease serine 6
- GeneTMPRSS6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids811 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Through the cleavage of cell surface HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis (PubMed:18408718, PubMed:18976966, PubMed:25156943).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 617 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 668 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 762 | Charge relay system | ||||
Sequence: S |
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 | extracellular space | |
Cellular Component | plasma membrane | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | BMP signaling pathway | |
Biological Process | collagen catabolic process | |
Biological Process | extracellular matrix disassembly | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | membrane protein proteolysis | |
Biological Process | multicellular organismal-level iron ion homeostasis | |
Biological Process | negative regulation of BMP signaling pathway | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | self proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTransmembrane protease serine 6
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IU80
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-55 | Cytoplasmic | ||||
Sequence: MLLLFHSKRMPVAEAPQVAGGQGDGGDGEEAEPEGMFKACEDSKRKARGYLRLVP | ||||||
Transmembrane | 56-76 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LFVLLALLVLASAGVLLWYFL | ||||||
Topological domain | 77-811 | Extracellular | ||||
Sequence: GYKAEVMVSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASVKDIAALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGEFLCSVNGLCVPACDGVKDCPNGLDERNCVCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCDCGLQGPSSRIVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Iron-refractory iron deficiency anemia (IRIDA)
- Note
- DescriptionKey features include congenital hypochromic microcytic anemia, very low mean corpuscular erythrocyte volume, low transferrin saturation, abnormal iron absorption characterized by no hematologic improvement following treatment with oral iron, and abnormal iron utilization characterized by a sluggish, incomplete response to parenteral iron.
- See alsoMIM:206200
Natural variants in IRIDA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_068665 | 114 | E>K | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474803 | |
VAR_068666 | 118 | A>D | in IRIDA; results in reduced inhibition of HAMP promoter; dbSNP:rs267607121 | |
VAR_064075 | 141 | Y>C | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; does not undergo proteolytic processing; impaired localization to the cell membrane; able to interact with HJV; dbSNP:rs1430692214 | |
VAR_064076 | 212 | I>T | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; no effect on catalytic activity; dbSNP:rs776877803 | |
VAR_068668 | 235 | L>P | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474802 | |
VAR_072901 | 247 | W>C | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |
VAR_064077 | 271 | R>Q | in IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on localization to the cell membrane; no effect on catalytic activity; HJV processing is not affected; dbSNP:rs776180387 | |
VAR_072902 | 287 | T>N | in IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on catalytic activity; autoproteolytic and HJV processing are not affected; dbSNP:rs1449962575 | |
VAR_064078 | 304 | S>L | in IRIDA; dbSNP:rs1373272804 | |
VAR_072903 | 335 | C>F | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |
VAR_068669 | 418 | Y>C | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474804 | |
VAR_044435 | 442 | G>R | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; altered catalytic activity; autoproteolytic processing is reduced but it retains the ability to process HJV; able to interact with HJV; dbSNP:rs137853119 | |
VAR_072904 | 510 | C>R | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |
VAR_064079 | 510 | C>S | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; loss of catalytic activity; no ability to process HJV | |
VAR_072905 | 521 | D>G | in IRIDA | |
VAR_044436 | 521 | D>N | in IRIDA; reduced expression at the cell surface; partially retained in the Golgi apparatus; does not undergo proteolytic processing; able to interact with HJV; results in reduced inhibition of HAMP promoter; dbSNP:rs137853120 | |
VAR_068671 | 522 | E>K | in IRIDA; reduced expression at the cell surface; partially retained in the Golgi apparatus; does not undergo proteolytic processing; able to interact with HJV; results in reduced inhibition of HAMP promoter; dbSNP:rs387907018 | |
VAR_072906 | 590 | W>R | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired; dbSNP:rs770897887 | |
VAR_072907 | 597 | R>W | in IRIDA; slightly reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are significantly reduced; dbSNP:rs773272073 | |
VAR_068672 | 603 | G>R | in IRIDA; dbSNP:rs769083817 | |
VAR_072908 | 605 | A>G | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |
VAR_072909 | 606 | L>R | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |
VAR_072910 | 623 | S>T | in IRIDA | |
VAR_068674 | 765 | P>A | in IRIDA; severely reduced proteolytic processing; loss of activity; dbSNP:rs199474805 | |
VAR_044437 | 774 | R>C | in IRIDA; reduced proteolytic processing; reduced expression to plasma membrane; does not affect binding to HJV; dbSNP:rs776069764 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_068665 | 114 | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474803 | |||
Sequence: E → K | ||||||
Natural variant | VAR_068666 | 118 | in IRIDA; results in reduced inhibition of HAMP promoter; dbSNP:rs267607121 | |||
Sequence: A → D | ||||||
Natural variant | VAR_064075 | 141 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; does not undergo proteolytic processing; impaired localization to the cell membrane; able to interact with HJV; dbSNP:rs1430692214 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_064076 | 212 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; no effect on catalytic activity; dbSNP:rs776877803 | |||
Sequence: I → T | ||||||
Natural variant | VAR_036296 | 223 | in a breast cancer sample; somatic mutation; dbSNP:rs749106338 | |||
Sequence: R → H | ||||||
Natural variant | VAR_068667 | 228 | in dbSNP:rs754848810 | |||
Sequence: G → D | ||||||
Natural variant | VAR_036297 | 234 | in a breast cancer sample; somatic mutation | |||
Sequence: R → S | ||||||
Natural variant | VAR_068668 | 235 | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474802 | |||
Sequence: L → P | ||||||
Natural variant | VAR_072901 | 247 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |||
Sequence: W → C | ||||||
Natural variant | VAR_051841 | 253 | in dbSNP:rs2235324 | |||
Sequence: K → E | ||||||
Natural variant | VAR_044434 | 262 | in dbSNP:rs2235324 | |||
Sequence: E → K | ||||||
Natural variant | VAR_064077 | 271 | in IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on localization to the cell membrane; no effect on catalytic activity; HJV processing is not affected; dbSNP:rs776180387 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_072902 | 287 | in IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on catalytic activity; autoproteolytic and HJV processing are not affected; dbSNP:rs1449962575 | |||
Sequence: T → N | ||||||
Natural variant | VAR_051842 | 288 | in dbSNP:rs5995378 | |||
Sequence: S → L | ||||||
Natural variant | VAR_064078 | 304 | in IRIDA; dbSNP:rs1373272804 | |||
Sequence: S → L | ||||||
Natural variant | VAR_072903 | 335 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |||
Sequence: C → F | ||||||
Natural variant | VAR_068669 | 418 | in IRIDA; does not undergo proteolytic processing; loss of activity; dbSNP:rs199474804 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_044435 | 442 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; altered catalytic activity; autoproteolytic processing is reduced but it retains the ability to process HJV; able to interact with HJV; dbSNP:rs137853119 | |||
Sequence: G → R | ||||||
Natural variant | VAR_068670 | 446 | in dbSNP:rs117576908 | |||
Sequence: R → W | ||||||
Natural variant | VAR_072904 | 510 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |||
Sequence: C → R | ||||||
Natural variant | VAR_064079 | 510 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; loss of catalytic activity; no ability to process HJV | |||
Sequence: C → S | ||||||
Natural variant | VAR_072905 | 521 | in IRIDA | |||
Sequence: D → G | ||||||
Natural variant | VAR_044436 | 521 | in IRIDA; reduced expression at the cell surface; partially retained in the Golgi apparatus; does not undergo proteolytic processing; able to interact with HJV; results in reduced inhibition of HAMP promoter; dbSNP:rs137853120 | |||
Sequence: D → N | ||||||
Natural variant | VAR_068671 | 522 | in IRIDA; reduced expression at the cell surface; partially retained in the Golgi apparatus; does not undergo proteolytic processing; able to interact with HJV; results in reduced inhibition of HAMP promoter; dbSNP:rs387907018 | |||
Sequence: E → K | ||||||
Mutagenesis | 576 | Does not undergo proteolytic processing. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_072906 | 590 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired; dbSNP:rs770897887 | |||
Sequence: W → R | ||||||
Natural variant | VAR_072907 | 597 | in IRIDA; slightly reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are significantly reduced; dbSNP:rs773272073 | |||
Sequence: R → W | ||||||
Natural variant | VAR_068672 | 603 | in IRIDA; dbSNP:rs769083817 | |||
Sequence: G → R | ||||||
Natural variant | VAR_072908 | 605 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |||
Sequence: A → G | ||||||
Natural variant | VAR_072909 | 606 | in IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired | |||
Sequence: L → R | ||||||
Natural variant | VAR_072910 | 623 | in IRIDA | |||
Sequence: S → T | ||||||
Natural variant | VAR_068673 | 674 | ||||
Sequence: L → F | ||||||
Natural variant | VAR_051843 | 736 | in dbSNP:rs855791 | |||
Sequence: V → A | ||||||
Mutagenesis | 762 | Does not undergo proteolytic processing. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_051844 | 763 | in dbSNP:rs11703011 | |||
Sequence: G → D | ||||||
Natural variant | VAR_068674 | 765 | in IRIDA; severely reduced proteolytic processing; loss of activity; dbSNP:rs199474805 | |||
Sequence: P → A | ||||||
Natural variant | VAR_044437 | 774 | in IRIDA; reduced proteolytic processing; reduced expression to plasma membrane; does not affect binding to HJV; dbSNP:rs776069764 | |||
Sequence: R → C | ||||||
Natural variant | VAR_068675 | 795 | in dbSNP:rs139105452 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000088696 | 1-811 | Transmembrane protease serine 6 | |||
Sequence: MLLLFHSKRMPVAEAPQVAGGQGDGGDGEEAEPEGMFKACEDSKRKARGYLRLVPLFVLLALLVLASAGVLLWYFLGYKAEVMVSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASVKDIAALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGEFLCSVNGLCVPACDGVKDCPNGLDERNCVCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCDCGLQGPSSRIVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT | ||||||
Glycosylation | 136 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 216 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 335↔366 | |||||
Sequence: CEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHC | ||||||
Glycosylation | 338 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 433 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 453 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 458↔470 | |||||
Sequence: CPGEFLCSVNGLC | ||||||
Disulfide bond | 464↔480 | |||||
Sequence: CSVNGLCVPACDGVKDC | ||||||
Disulfide bond | 474↔489 | |||||
Sequence: CDGVKDCPNGLDERNC | ||||||
Disulfide bond | 491↔503 | |||||
Sequence: CRATFQCKEDSTC | ||||||
Disulfide bond | 497↔516 | |||||
Sequence: CKEDSTCISLPKVCDGQPDC | ||||||
Disulfide bond | 510↔525 | |||||
Sequence: CDGQPDCLNGSDEEQC | ||||||
Glycosylation | 518 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 531↔543 | |||||
Sequence: CGTFTFQCEDRSC | ||||||
Disulfide bond | 538↔557 | |||||
Sequence: CEDRSCVKKPNPQCDGRPDC | ||||||
Disulfide bond | 551↔566 | |||||
Sequence: CDGRPDCRDGSDEEHC | ||||||
Disulfide bond | 602↔618 | |||||
Sequence: CGGALIADRWVITAAHC | ||||||
Disulfide bond | 702↔768 | |||||
Sequence: CWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVC | ||||||
Disulfide bond | 733↔747 | |||||
Sequence: CSEVYRYQVTPRMLC | ||||||
Disulfide bond | 758↔787 | |||||
Sequence: CQGDSGGPLVCKALSGRWFLAGLVSWGLGC |
Post-translational modification
This results in TMPRSS6 shedding from the cell surface and conversion into an activated two-chains form which is released extracellularly (PubMed:18976966, PubMed:20518742, PubMed:25156943).
The process involves a trans-activation mechanism that requires TMPRSS6 oligomerization (PubMed:20518742, PubMed:25156943).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IU80-2 | ATN1 Q86V38 | 3 | EBI-25839648, EBI-11954292 | |
BINARY | Q8IU80-2 | CRYAA P02489 | 3 | EBI-25839648, EBI-6875961 | |
BINARY | Q8IU80-2 | DYNC1H1 Q14204 | 3 | EBI-25839648, EBI-356015 | |
BINARY | Q8IU80-2 | KLK6 Q92876 | 3 | EBI-25839648, EBI-2432309 | |
BINARY | Q8IU80-4 | HJV Q6ZVN8 | 3 | EBI-11686560, EBI-10900704 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 84-209 | SEA | ||||
Sequence: VSQVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELITSTRLGTYYNSSSVYSFGEGPLTCFFWFILQIPEHRRLMLSPEVVQALLVEELLSTVNSSAAVPYRAEYEVDPEGLVILEASV | ||||||
Domain | 213-336 | CUB 1 | ||||
Sequence: AALNSTLGCYRYSYVGQGQVLRLKGPDHLASSCLWHLQGPKDLMLKLRLEWTLAECRDRLAMYDVAGPLEKRLITSVYGCSRQEPVVEVLASGAIMAVVWKKGLHSYYDPFVLSVQPVVFQACE | ||||||
Domain | 335-452 | CUB 2 | ||||
Sequence: CEVNLTLDNRLDSQGVLSTPYFPSYYSPQTHCSWHLTVPSLDYGLALWFDAYALRRQKYDLPCTQGQWTIQNRRLCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLY | ||||||
Domain | 457-489 | LDL-receptor class A 1 | ||||
Sequence: PCPGEFLCSVNGLCVPACDGVKDCPNGLDERNC | ||||||
Domain | 490-526 | LDL-receptor class A 2 | ||||
Sequence: VCRATFQCKEDSTCISLPKVCDGQPDCLNGSDEEQCQ | ||||||
Domain | 530-567 | LDL-receptor class A 3 | ||||
Sequence: PCGTFTFQCEDRSCVKKPNPQCDGRPDCRDGSDEEHCD | ||||||
Domain | 577-811 | Peptidase S1 | ||||
Sequence: IVGGAVSSEGEWPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASTVLWTVFLGKVWQNSRWPGEVSFKVSRLLLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPISNALQKVDVQLIPQDLCSEVYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVCKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVISWIQQVVT |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8IU80-4
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length811
- Mass (Da)90,000
- Last updated2008-10-14 v3
- Checksum7EEF193F655DDE9D
Q8IU80-1
- Name2
- Differences from canonical
- 1-9: Missing
Q8IU80-2
- Name3
Q8IU80-5
- Name4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035562 | 1-9 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008379 | 409-461 | in isoform 3 | |||
Sequence: LCGLRILQPYAERIPVVATAGITINFTSQISLTGPGVRVHYGLYNQSDPCPGE → YHFLSSLWLPFLPPPPSLPSSTVTPSLEAQVPNLRGAARGASRGWGWCQACCP | ||||||
Sequence conflict | 430 | In isoform Q8IU80-2; in Ref. 4; CAQ07364 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_008380 | 462-811 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035563 | 714 | in isoform 4 | |||
Sequence: G → ALRADAVALFYGWRNQGSETCCC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY055383 EMBL· GenBank· DDBJ | AAL16413.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY055384 EMBL· GenBank· DDBJ | AAL16414.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358398 EMBL· GenBank· DDBJ | AAQ88764.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456446 EMBL· GenBank· DDBJ | CAG30332.1 EMBL· GenBank· DDBJ | mRNA | ||
AL022314 EMBL· GenBank· DDBJ | CAQ07360.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL022314 EMBL· GenBank· DDBJ | CAQ07361.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL022314 EMBL· GenBank· DDBJ | CAQ07363.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL022314 EMBL· GenBank· DDBJ | CAQ07364.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ319876 EMBL· GenBank· DDBJ | CAC85953.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039082 EMBL· GenBank· DDBJ | AAH39082.1 EMBL· GenBank· DDBJ | mRNA |