Q7TN88 · PK1L2_MOUSE
- ProteinPolycystin-1-like protein 2
- GenePkd1l2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2461 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
May function as an ion-channel regulator. May function as a G-protein-coupled receptor (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 1316-1317 | Cleavage; by autolysis | ||||
Sequence: LT |
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 | membrane | |
Molecular Function | calcium channel activity | |
Molecular Function | calcium ion binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | G-protein alpha-subunit binding | |
Biological Process | detection of mechanical stimulus |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended namePolycystin-1-like protein 2
- Short namesPolycystin-1L2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TN88
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1346-1366 | Helical | ||||
Sequence: PVVVTTVGCLCMLYVLVLIWA | ||||||
Transmembrane | 1554-1574 | Helical | ||||
Sequence: VSCCFSMLLCTMLTSIMFWGV | ||||||
Transmembrane | 1596-1616 | Helical | ||||
Sequence: MIGLESSILMFPINLLIVQIF | ||||||
Transmembrane | 1816-1836 | Helical | ||||
Sequence: WWCVLVGWLLVATTSGVAAFF | ||||||
Transmembrane | 1863-1883 | Helical | ||||
Sequence: SVFITQPLKVLGFAAFFALVL | ||||||
Transmembrane | 1940-1960 | Helical | ||||
Sequence: AFALIREILAYLAFLWMLLLV | ||||||
Transmembrane | 2186-2206 | Helical | ||||
Sequence: HPFVVAAELTYFLFLFYYMVV | ||||||
Transmembrane | 2222-2242 | Helical | ||||
Sequence: KWNLLEVAIILASWSALVVFV | ||||||
Transmembrane | 2273-2293 | Helical | ||||
Sequence: ALGYIIAFLVLLSTVKLWHLL | ||||||
Transmembrane | 2315-2335 | Helical | ||||
Sequence: GFVAVILIMLLAYSFASNLVF | ||||||
Transmembrane | 2380-2400 | Helical | ||||
Sequence: CIVFMTFVVLNLFISVILVAF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MAGLVFLGLALSSGATVA | ||||||
Chain | PRO_0000322577 | 19-2461 | Polycystin-1-like protein 2 | |||
Sequence: KSEGGSLCSRSQVFFRDACYEFVPLEHTFPGAQGWCEGHGGHLAFIPDEDTQQFLQRHITQDREWWIGLTGGSGHNGTVGGSGTWLDTSNVNYSNWQEGQATPAPGSCGYIGSGPSSQWAALEDCTQTFAFVCEFGVGRSLACEGHNATMHCDSGEVILVQDAFYGHQTPYLCTRGIWPPSDLEGECGWVSVKDEVAGQCQGLQACQVAVDGTYFGDPCPTRGSYLWVQYQCLEGLRLVVPNGSFIFDNVTISLMWLLSPYTGNLSCVLSMGDGYTFDPYNPPSVSSNVTHQFSSPGEFTVFAECTTSEWHVTAQKQVILCEKVETPRITGCTGLAGAGVGLLCQAVFGEPLWVQVDLDGGAGATYAVLSHNRTLAEFTAQRGSQLYNLTLDRDIQEMLGPGRHHLKIQAVSNEGTGTASAPSGNFTVYFVEPLSGLRASWASDRVELGWDLVVNVSVARGTLEELTFEVAGLNANFSQEEESVGQSSGNYHVAVPAEGTFLVTVHVRNAFSELSLDIGNITVTASSSLQELSGINAEAKSGHKQDMKVFTEPELYVDPFTEVTLGWPDDDPGLNFHWSCGRCWAQWNACVGRQLLHTDQRLLVLHTFCLPPLNSAVTLHLAILRGQELEKETEQCLYVSAPLNLGPQISCEKNCRPVKADQDVLLTVTVGDETSVAVFSWYLDDTVPEEVEPLPAACRLRGFWPRSLTLLHSNSSVLLLNSSFLQTWGPVIPIRVTALTSHAYGEDTYMISMLPRPEVPACTIDPEEGSVLTSFTVSCSTPATLGPVEYCFCLPSGFCLHCGPEPALPAVYLPLGEEKDGFVLPVVISVTNRAGDIEQTQVAVKVGHSYTGVEDVTFQEMVSERIATALHQESGREQLLLFAKAVSSELNSEVQSPGSGQLGMDIKRKVRELMLRSLSVVTTGLQNMQRVQALAEVLREVTQRAEELTPAAQWEASCALQRATEALLVASTKVRPEDQRRQEATRAMFEAVGSVLEASLSHRSEEPMEANSSQVAYIVAQLLRVIDHFQSALLLGTLPGGLPAILVTPSISVYTDRIQPRSWQGSSVHTAAADSVTFTLPAATFLCPMEDSQEPVDIRMMSFSQNPFPSRSQFDVSGTVGGLRLTSSSGHPIPVKNLSQNIEILLPRISAHIEPKMLSLASREALSVNVTAGDTALGIQLHWGPGVPLILSLGYGYHPNETSYDAQTHLPPVAATGDLPTWILHPEDLPFGEGVYYLRVVPEADLESSSGRNLTVGITTFLAHCVFWDETQETWDDSGCQVGPRTTPSQTHCLCNHLTFFGSSFLVMPNAIDVRQTAELFATFEDNPVVVTTVGCLCMLYVLVLIWARRKDIQDQAKVKVVVLEDNDPFAQYHYLVTVYTGHRRGAATSSKVTLTLYGSDGESEPHHLSDPDAAVFERGGVDVFLLSTLFPLGELQSLRLWHDNSGDRPSWYVSRVLVYDSVVDRKWYFLCNSWLSVDVGDCVLDKVFPVATEQDRKQFSHLFFTKTSTGFQDGHIWYSVFCSATRSSFTRVQRVSCCFSMLLCTMLTSIMFWGVPKDPAEQKMDLGKIEFTWQEVMIGLESSILMFPINLLIVQIFRNTRPRLPMGKDGRQKQGPPNLTPSAQPTEEGLLTPETGIQSLISSLFKALKVQPPASGWDSMNPVDINYLLTLMEDIICPESTEGPGFWEEAKGREDPITSTRGSVKPKENTWHPKPELAVRGLWKDSVYRRCLYLQLEHVERELQLLGPQGFLHHHSHAQALRQLHVLKGHLWGQPGTPALAYPSTSRVSKSPRGLPWWCVLVGWLLVATTSGVAAFFTMLYGLHYGRVSSLKWLISMAVSFVESVFITQPLKVLGFAAFFALVLKREDDEETLPLFPGHLSSPGPGVLFRSRRHSSERAYQPPPMAAIEKMKTTRLKEQKAFALIREILAYLAFLWMLLLVAYGQRDPNAYHFHRHLERSFSQGFSPVLGFRGFFEWANTTLVKNLYGHHPGFVTDGNSKLVGSAHIRQVRVRESSCAVAQQLQDSLDGCHGPYSLGIEDLVDYGEGWNASAYNNSNGFPQAWRYQSQSQRRGYPMWGKLTLYGGGGYVVPLGTDHQSASRILQYLFDNSWLDALTRAVFVEFTVYNANVNLFCTVTLTLETSGLGTFFSHVTLQSLRLYPFTDGWHPFVVAAELTYFLFLFYYMVVQGKLMRKQKWGYFCSKWNLLEVAIILASWSALVVFVKRTILADRDLQRYREHREGISFSETAAADAALGYIIAFLVLLSTVKLWHLLRLNPKMNMITSALRRAWGDISGFVAVILIMLLAYSFASNLVFGWKLRSYKTLFDAAETMVSLQLGIFNYEEVLDYSPILGSLLIGSCIVFMTFVVLNLFISVILVAFSEEQKSDQLSEEGEIADLLLVKILSFLGIRCKREETWSSSEQPELPPQALAPQPAQALSRV | ||||||
Disulfide bond | 54↔151 | |||||
Sequence: CEGHGGHLAFIPDEDTQQFLQRHITQDREWWIGLTGGSGHNGTVGGSGTWLDTSNVNYSNWQEGQATPAPGSCGYIGSGPSSQWAALEDCTQTFAFVC | ||||||
Glycosylation | 94 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 110 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 126↔143 | |||||
Sequence: CGYIGSGPSSQWAALEDC | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 267 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 306 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 390 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 406 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 443 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 473 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 494 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1283↔1311 | |||||
Sequence: CVFWDETQETWDDSGCQVGPRTTPSQTHC | ||||||
Disulfide bond | 1298↔1313 | |||||
Sequence: CQVGPRTTPSQTHCLC |
Post-translational modification
Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-152 | C-type lectin | ||||
Sequence: FRDACYEFVPLEHTFPGAQGWCEGHGGHLAFIPDEDTQQFLQRHITQDREWWIGLTGGSGHNGTVGGSGTWLDTSNVNYSNWQEGQATPAPGSCGYIGSGPSSQWAALEDCTQTFAFVCE | ||||||
Domain | 160-251 | SUEL-type lectin | ||||
Sequence: ACEGHNATMHCDSGEVILVQDAFYGHQTPYLCTRGIWPPSDLEGECGWVSVKDEVAGQCQGLQACQVAVDGTYFGDPCPTRGSYLWVQYQCL | ||||||
Domain | 255-346 | PKD | ||||
Sequence: RLVVPNGSFIFDNVTISLMWLLSPYTGNLSCVLSMGDGYTFDPYNPPSVSSNVTHQFSSPGEFTVFAECTTSEWHVTAQKQVILCEKVETPR | ||||||
Domain | 424-1125 | REJ | ||||
Sequence: LKIQAVSNEGTGTASAPSGNFTVYFVEPLSGLRASWASDRVELGWDLVVNVSVARGTLEELTFEVAGLNANFSQEEESVGQSSGNYHVAVPAEGTFLVTVHVRNAFSELSLDIGNITVTASSSLQELSGINAEAKSGHKQDMKVFTEPELYVDPFTEVTLGWPDDDPGLNFHWSCGRCWAQWNACVGRQLLHTDQRLLVLHTFCLPPLNSAVTLHLAILRGQELEKETEQCLYVSAPLNLGPQISCEKNCRPVKADQDVLLTVTVGDETSVAVFSWYLDDTVPEEVEPLPAACRLRGFWPRSLTLLHSNSSVLLLNSSFLQTWGPVIPIRVTALTSHAYGEDTYMISMLPRPEVPACTIDPEEGSVLTSFTVSCSTPATLGPVEYCFCLPSGFCLHCGPEPALPAVYLPLGEEKDGFVLPVVISVTNRAGDIEQTQVAVKVGHSYTGVEDVTFQEMVSERIATALHQESGREQLLLFAKAVSSELNSEVQSPGSGQLGMDIKRKVRELMLRSLSVVTTGLQNMQRVQALAEVLREVTQRAEELTPAAQWEASCALQRATEALLVASTKVRPEDQRRQEATRAMFEAVGSVLEASLSHRSEEPMEANSSQVAYIVAQLLRVIDHFQSALLLGTLPGGLPAILVTPSISVYTDRIQPRSWQGSSVHTAAADSVTFTLPAATFLCPMEDSQEPVDIRMMSFSQNP | ||||||
Domain | 1174-1332 | GAIN-B | ||||
Sequence: KMLSLASREALSVNVTAGDTALGIQLHWGPGVPLILSLGYGYHPNETSYDAQTHLPPVAATGDLPTWILHPEDLPFGEGVYYLRVVPEADLESSSGRNLTVGITTFLAHCVFWDETQETWDDSGCQVGPRTTPSQTHCLCNHLTFFGSSFLVMPNAIDV | ||||||
Region | 1283-1332 | GPS | ||||
Sequence: CVFWDETQETWDDSGCQVGPRTTPSQTHCLCNHLTFFGSSFLVMPNAIDV | ||||||
Domain | 1391-1508 | PLAT | ||||
Sequence: YHYLVTVYTGHRRGAATSSKVTLTLYGSDGESEPHHLSDPDAAVFERGGVDVFLLSTLFPLGELQSLRLWHDNSGDRPSWYVSRVLVYDSVVDRKWYFLCNSWLSVDVGDCVLDKVFP | ||||||
Region | 1623-1648 | Disordered | ||||
Sequence: LPMGKDGRQKQGPPNLTPSAQPTEEG | ||||||
Compositional bias | 1634-1648 | Polar residues | ||||
Sequence: GPPNLTPSAQPTEEG | ||||||
Region | 1702-1729 | Disordered | ||||
Sequence: GPGFWEEAKGREDPITSTRGSVKPKENT | ||||||
Compositional bias | 1705-1729 | Basic and acidic residues | ||||
Sequence: FWEEAKGREDPITSTRGSVKPKENT | ||||||
Region | 2381-2461 | Interaction with GNAS and GNAI1 | ||||
Sequence: IVFMTFVVLNLFISVILVAFSEEQKSDQLSEEGEIADLLLVKILSFLGIRCKREETWSSSEQPELPPQALAPQPAQALSRV | ||||||
Region | 2438-2461 | Disordered | ||||
Sequence: SSSEQPELPPQALAPQPAQALSRV |
Sequence similarities
Belongs to the polycystin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,461
- Mass (Da)271,977
- Last updated2003-10-01 v1
- Checksum5F837EBA57D54BF3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9QPG2 | E9QPG2_MOUSE | Pkd1l2 | 2461 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1634-1648 | Polar residues | ||||
Sequence: GPPNLTPSAQPTEEG | ||||||
Compositional bias | 1705-1729 | Basic and acidic residues | ||||
Sequence: FWEEAKGREDPITSTRGSVKPKENT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY164484 EMBL· GenBank· DDBJ | AAO32797.1 EMBL· GenBank· DDBJ | mRNA |