Q7TN88 · PK1L2_MOUSE

  • Protein
    Polycystin-1-like protein 2
  • Gene
    Pkd1l2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

May function as an ion-channel regulator. May function as a G-protein-coupled receptor (By similarity).

Features

Showing features for site.

124612004006008001,0001,2001,4001,6001,8002,0002,2002,400
TypeIDPosition(s)Description
Site1316-1317Cleavage; by autolysis

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmembrane
Molecular Functioncalcium channel activity
Molecular Functioncalcium ion binding
Molecular Functioncarbohydrate binding
Molecular FunctionG-protein alpha-subunit binding
Biological Processdetection of mechanical stimulus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Polycystin-1-like protein 2
  • Short names
    Polycystin-1L2
  • Alternative names
    • PC1-like 2 protein
    • Polycystic kidney disease protein 1-like 2

Gene names

    • Name
      Pkd1l2

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q7TN88

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane1346-1366Helical
Transmembrane1554-1574Helical
Transmembrane1596-1616Helical
Transmembrane1816-1836Helical
Transmembrane1863-1883Helical
Transmembrane1940-1960Helical
Transmembrane2186-2206Helical
Transmembrane2222-2242Helical
Transmembrane2273-2293Helical
Transmembrane2315-2335Helical
Transmembrane2380-2400Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000032257719-2461Polycystin-1-like protein 2
Disulfide bond54↔151
Glycosylation94N-linked (GlcNAc...) asparagine
Glycosylation110N-linked (GlcNAc...) asparagine
Disulfide bond126↔143
Glycosylation165N-linked (GlcNAc...) asparagine
Glycosylation267N-linked (GlcNAc...) asparagine
Glycosylation306N-linked (GlcNAc...) asparagine
Glycosylation390N-linked (GlcNAc...) asparagine
Glycosylation406N-linked (GlcNAc...) asparagine
Glycosylation443N-linked (GlcNAc...) asparagine
Glycosylation473N-linked (GlcNAc...) asparagine
Glycosylation494N-linked (GlcNAc...) asparagine
Glycosylation1187N-linked (GlcNAc...) asparagine
Disulfide bond1283↔1311
Disulfide bond1298↔1313

Post-translational modification

Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

May interact via its C-terminus with GNAS and GNAI1.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain33-152C-type lectin
Domain160-251SUEL-type lectin
Domain255-346PKD
Domain424-1125REJ
Domain1174-1332GAIN-B
Region1283-1332GPS
Domain1391-1508PLAT
Region1623-1648Disordered
Compositional bias1634-1648Polar residues
Region1702-1729Disordered
Compositional bias1705-1729Basic and acidic residues
Region2381-2461Interaction with GNAS and GNAI1
Region2438-2461Disordered

Sequence similarities

Belongs to the polycystin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    2,461
  • Mass (Da)
    271,977
  • Last updated
    2003-10-01 v1
  • Checksum
    5F837EBA57D54BF3
MAGLVFLGLALSSGATVAKSEGGSLCSRSQVFFRDACYEFVPLEHTFPGAQGWCEGHGGHLAFIPDEDTQQFLQRHITQDREWWIGLTGGSGHNGTVGGSGTWLDTSNVNYSNWQEGQATPAPGSCGYIGSGPSSQWAALEDCTQTFAFVCEFGVGRSLACEGHNATMHCDSGEVILVQDAFYGHQTPYLCTRGIWPPSDLEGECGWVSVKDEVAGQCQGLQACQVAVDGTYFGDPCPTRGSYLWVQYQCLEGLRLVVPNGSFIFDNVTISLMWLLSPYTGNLSCVLSMGDGYTFDPYNPPSVSSNVTHQFSSPGEFTVFAECTTSEWHVTAQKQVILCEKVETPRITGCTGLAGAGVGLLCQAVFGEPLWVQVDLDGGAGATYAVLSHNRTLAEFTAQRGSQLYNLTLDRDIQEMLGPGRHHLKIQAVSNEGTGTASAPSGNFTVYFVEPLSGLRASWASDRVELGWDLVVNVSVARGTLEELTFEVAGLNANFSQEEESVGQSSGNYHVAVPAEGTFLVTVHVRNAFSELSLDIGNITVTASSSLQELSGINAEAKSGHKQDMKVFTEPELYVDPFTEVTLGWPDDDPGLNFHWSCGRCWAQWNACVGRQLLHTDQRLLVLHTFCLPPLNSAVTLHLAILRGQELEKETEQCLYVSAPLNLGPQISCEKNCRPVKADQDVLLTVTVGDETSVAVFSWYLDDTVPEEVEPLPAACRLRGFWPRSLTLLHSNSSVLLLNSSFLQTWGPVIPIRVTALTSHAYGEDTYMISMLPRPEVPACTIDPEEGSVLTSFTVSCSTPATLGPVEYCFCLPSGFCLHCGPEPALPAVYLPLGEEKDGFVLPVVISVTNRAGDIEQTQVAVKVGHSYTGVEDVTFQEMVSERIATALHQESGREQLLLFAKAVSSELNSEVQSPGSGQLGMDIKRKVRELMLRSLSVVTTGLQNMQRVQALAEVLREVTQRAEELTPAAQWEASCALQRATEALLVASTKVRPEDQRRQEATRAMFEAVGSVLEASLSHRSEEPMEANSSQVAYIVAQLLRVIDHFQSALLLGTLPGGLPAILVTPSISVYTDRIQPRSWQGSSVHTAAADSVTFTLPAATFLCPMEDSQEPVDIRMMSFSQNPFPSRSQFDVSGTVGGLRLTSSSGHPIPVKNLSQNIEILLPRISAHIEPKMLSLASREALSVNVTAGDTALGIQLHWGPGVPLILSLGYGYHPNETSYDAQTHLPPVAATGDLPTWILHPEDLPFGEGVYYLRVVPEADLESSSGRNLTVGITTFLAHCVFWDETQETWDDSGCQVGPRTTPSQTHCLCNHLTFFGSSFLVMPNAIDVRQTAELFATFEDNPVVVTTVGCLCMLYVLVLIWARRKDIQDQAKVKVVVLEDNDPFAQYHYLVTVYTGHRRGAATSSKVTLTLYGSDGESEPHHLSDPDAAVFERGGVDVFLLSTLFPLGELQSLRLWHDNSGDRPSWYVSRVLVYDSVVDRKWYFLCNSWLSVDVGDCVLDKVFPVATEQDRKQFSHLFFTKTSTGFQDGHIWYSVFCSATRSSFTRVQRVSCCFSMLLCTMLTSIMFWGVPKDPAEQKMDLGKIEFTWQEVMIGLESSILMFPINLLIVQIFRNTRPRLPMGKDGRQKQGPPNLTPSAQPTEEGLLTPETGIQSLISSLFKALKVQPPASGWDSMNPVDINYLLTLMEDIICPESTEGPGFWEEAKGREDPITSTRGSVKPKENTWHPKPELAVRGLWKDSVYRRCLYLQLEHVERELQLLGPQGFLHHHSHAQALRQLHVLKGHLWGQPGTPALAYPSTSRVSKSPRGLPWWCVLVGWLLVATTSGVAAFFTMLYGLHYGRVSSLKWLISMAVSFVESVFITQPLKVLGFAAFFALVLKREDDEETLPLFPGHLSSPGPGVLFRSRRHSSERAYQPPPMAAIEKMKTTRLKEQKAFALIREILAYLAFLWMLLLVAYGQRDPNAYHFHRHLERSFSQGFSPVLGFRGFFEWANTTLVKNLYGHHPGFVTDGNSKLVGSAHIRQVRVRESSCAVAQQLQDSLDGCHGPYSLGIEDLVDYGEGWNASAYNNSNGFPQAWRYQSQSQRRGYPMWGKLTLYGGGGYVVPLGTDHQSASRILQYLFDNSWLDALTRAVFVEFTVYNANVNLFCTVTLTLETSGLGTFFSHVTLQSLRLYPFTDGWHPFVVAAELTYFLFLFYYMVVQGKLMRKQKWGYFCSKWNLLEVAIILASWSALVVFVKRTILADRDLQRYREHREGISFSETAAADAALGYIIAFLVLLSTVKLWHLLRLNPKMNMITSALRRAWGDISGFVAVILIMLLAYSFASNLVFGWKLRSYKTLFDAAETMVSLQLGIFNYEEVLDYSPILGSLLIGSCIVFMTFVVLNLFISVILVAFSEEQKSDQLSEEGEIADLLLVKILSFLGIRCKREETWSSSEQPELPPQALAPQPAQALSRV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E9QPG2E9QPG2_MOUSEPkd1l22461

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1634-1648Polar residues
Compositional bias1705-1729Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY164484
EMBL· GenBank· DDBJ
AAO32797.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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