AGRV1_HUMAN
ID AGRV1_HUMAN Reviewed; 6306 AA.
AC Q8WXG9; O75171; Q8TF58; Q9H0X5; Q9UL61;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Adhesion G-protein coupled receptor V1 {ECO:0000305};
DE Short=ADGRV1 {ECO:0000305};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8VHN7};
DE AltName: Full=G-protein coupled receptor 98;
DE AltName: Full=Monogenic audiogenic seizure susceptibility protein 1 homolog;
DE AltName: Full=Usher syndrome type-2C protein;
DE AltName: Full=Very large G-protein coupled receptor 1;
DE Contains:
DE RecName: Full=ADGRV1 subunit alpha {ECO:0000250|UniProtKB:Q8VHN7};
DE Contains:
DE RecName: Full=ADGRV1 subunit beta {ECO:0000250|UniProtKB:Q8VHN7};
DE Flags: Precursor;
GN Name=ADGRV1 {ECO:0000312|HGNC:HGNC:17416};
GN Synonyms=GPR98, KIAA0686, KIAA1943, MASS1,
GN VLGR1 {ECO:0000303|PubMed:11606593};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-5344, AND TISSUE
RP SPECIFICITY.
RX PubMed=10976914; DOI=10.1210/mend.14.9.0511;
RA Nikkila H., McMillan D.R., Nunez B.S., Pascoe L., Curnow K.M., White P.C.;
RT "Sequence similarities between a novel putative G protein-coupled receptor
RT and Na+/Ca2+ exchangers define a cation binding domain.";
RL Mol. Endocrinol. 14:1351-1364(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT GLY-5344,
RP DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=11606593; DOI=10.1074/jbc.m108929200;
RA McMillan D.R., Kayes-Wandover K.M., Richardson J.A., White P.C.;
RT "Very large G protein-coupled receptor-1, the largest known cell surface
RT protein, is highly expressed in the developing central nervous system.";
RL J. Biol. Chem. 277:785-792(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-6306 (ISOFORM 4), AND VARIANT
RP PHE-1093.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2436-4042 (ISOFORM 1), AND
RP VARIANTS SER-2584 AND LYS-3471.
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5107-6306 (ISOFORMS 1/2), AND
RP VARIANT GLY-5344.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP INTERACTION WITH WHRN.
RX PubMed=16434480; DOI=10.1093/hmg/ddi490;
RA van Wijk E., van der Zwaag B., Peters T., Zimmermann U., Te Brinke H.,
RA Kersten F.F.J., Maerker T., Aller E., Hoefsloot L.H., Cremers C.W.R.J.,
RA Cremers F.P.M., Wolfrum U., Knipper M., Roepman R., Kremer H.;
RT "The DFNB31 gene product whirlin connects to the Usher protein network in
RT the cochlea and retina by direct association with USH2A and VLGR1.";
RL Hum. Mol. Genet. 15:751-765(2006).
RN [9]
RP INTERACTION WITH PDZD7.
RX PubMed=20440071; DOI=10.1172/jci39715;
RA Ebermann I., Phillips J.B., Liebau M.C., Koenekoop R.K., Schermer B.,
RA Lopez I., Schafer E., Roux A.F., Dafinger C., Bernd A., Zrenner E.,
RA Claustres M., Blanco B., Nurnberg G., Nurnberg P., Ruland R.,
RA Westerfield M., Benzing T., Bolz H.J.;
RT "PDZD7 is a modifier of retinal disease and a contributor to digenic Usher
RT syndrome.";
RL J. Clin. Invest. 120:1812-1823(2010).
RN [10]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP POSSIBLE INVOLVEMENT IN FAMILIAL FEBRILE CONVULSIONS 4.
RX PubMed=12402266; DOI=10.1002/ana.10347;
RA Nakayama J., Fu Y.H., Clark A.M., Nakahara S., Hamano K., Iwasaki N.,
RA Matsui A., Arinami T., Ptacek L.J.;
RT "A nonsense mutation of the MASS1 gene in a family with febrile and
RT afebrile seizures.";
RL Ann. Neurol. 52:654-657(2002).
RN [13]
RP INVOLVEMENT IN USH2C, AND VARIANTS ARG-127; LYS-249; PHE-1093; MET-1927;
RP ILE-1951; ASP-1985; LEU-1987; PHE-2004; CYS-2232; SER-2345; ALA-2379;
RP SER-2584; LEU-2764; THR-2803; VAL-3217; ASP-3248; LYS-3471 AND GLY-5344.
RX PubMed=14740321; DOI=10.1086/381685;
RA Weston M.D., Luijendijk M.W.J., Humphrey K.D., Moeller C., Kimberling W.J.;
RT "Mutations in the VLGR1 gene implicate G-protein signaling in the
RT pathogenesis of Usher syndrome type II.";
RL Am. J. Hum. Genet. 74:357-366(2004).
RN [14]
RP VARIANTS USH2C TRP-4789 AND ARG-5978.
RX PubMed=22147658; DOI=10.1002/humu.22004;
RA Besnard T., Vache C., Baux D., Larrieu L., Abadie C., Blanchet C.,
RA Odent S., Blanchet P., Calvas P., Hamel C., Dollfus H., Lina-Granade G.,
RA Lespinasse J., David A., Isidor B., Morin G., Malcolm S.,
RA Tuffery-Giraud S., Claustres M., Roux A.F.;
RT "Non-USH2A mutations in USH2 patients.";
RL Hum. Mutat. 33:504-510(2012).
CC -!- FUNCTION: G-protein coupled receptor which has an essential role in the
CC development of hearing and vision. Couples to G-alpha(i)-proteins,
CC GNAI1/2/3, G-alpha(q)-proteins, GNAQ, as well as G-alpha(s)-proteins,
CC GNAS, inhibiting adenylate cyclase (AC) activity and cAMP production.
CC Required for the hair bundle ankle formation, which connects growing
CC stereocilia in developing cochlear hair cells of the inner ear. In
CC response to extracellular calcium, activates kinases PKA and PKC to
CC regulate myelination by inhibiting the ubiquitination of MAG, thus
CC enhancing the stability of this protein in myelin-forming cells of the
CC auditory pathway. In retina photoreceptors, the USH2 complex is
CC required for the maintenance of periciliary membrane complex that seems
CC to play a role in regulating intracellular protein transport. Involved
CC in the regulation of bone metabolism. {ECO:0000250|UniProtKB:Q8VHN7}.
CC -!- FUNCTION: [ADGRV1 subunit beta]: Cleaved ADGRV1 beta-subunit couples
CC with G-alpha(i)-proteins, GNAI1/2/3, and constitutively inhibits
CC adenylate cyclase (AC) activity with a stronger effect than full
CC ADGRV1. {ECO:0000250|UniProtKB:Q8VHN7}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (alpha subunit) non-covalently linked to a seven-transmembrane
CC moiety (beta subunit) (By similarity). Component of USH2 complex,
CC composed of ADGRV1, PDZD7, USH2A and WHRN. Interacts with USH2A and
CC WHRN (PubMed:16434480). Interacts (via the cytoplasmic region) with
CC PDZD7 (PubMed:20440071). Interacts (via the cytoplasmic region) with
CC MYO7A (via MyTH4-FERM domains) (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHN7, ECO:0000269|PubMed:16434480,
CC ECO:0000269|PubMed:20440071}.
CC -!- INTERACTION:
CC Q8WXG9; Q9H5P4: PDZD7; NbExp=3; IntAct=EBI-7851128, EBI-20859318;
CC Q8WXG9-1; Q9Y6N9-4: USH1C; NbExp=3; IntAct=EBI-11621707, EBI-11523636;
CC Q8WXG9-1; Q9ES64-3: Ush1c; Xeno; NbExp=2; IntAct=EBI-11621707, EBI-7418919;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VHN7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VHN7}. Cell
CC projection, stereocilium membrane {ECO:0000250|UniProtKB:Q8VHN7}.
CC Photoreceptor inner segment {ECO:0000250|UniProtKB:Q8VHN7}.
CC Note=Localizes at the ankle region of the stereocilia. In
CC photoreceptors, localizes at a plasma membrane microdomain in the
CC apical inner segment that surrounds the connecting cilia called
CC periciliary membrane complex. {ECO:0000250|UniProtKB:Q8VHN7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=VLGR1b;
CC IsoId=Q8WXG9-1; Sequence=Displayed;
CC Name=2; Synonyms=VLGR1a;
CC IsoId=Q8WXG9-2; Sequence=VSP_017947, VSP_017950;
CC Name=3; Synonyms=VLGR1c;
CC IsoId=Q8WXG9-3; Sequence=VSP_017948, VSP_017949;
CC Name=4;
CC IsoId=Q8WXG9-4; Sequence=VSP_035313, VSP_035314;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in adult tissues.
CC {ECO:0000269|PubMed:10976914}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is 4 times more abundant than isoform 2
CC in most tissues tested, despite wide variations in absolute levels of
CC expression. Isoform 3 is expressed at about 1.5 times isoform 1 levels
CC in most tissues examined. In fetal testis, isoform 3 is expressed
CC almost exclusively. {ECO:0000269|PubMed:11606593}.
CC -!- DOMAIN: The 7 transmembrane domain is required in hair cells for the
CC hair bundle ankle formation. {ECO:0000250|UniProtKB:Q8VHN7}.
CC -!- PTM: Autoproteolytically cleaved into 2 subunits, an extracellular
CC alpha subunit and a seven-transmembrane subunit.
CC {ECO:0000250|UniProtKB:Q8VHN7}.
CC -!- DISEASE: Usher syndrome 2C (USH2C) [MIM:605472]: USH is a genetically
CC heterogeneous condition characterized by the association of retinitis
CC pigmentosa with sensorineural deafness. Age at onset and differences in
CC auditory and vestibular function distinguish Usher syndrome type 1
CC (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3).
CC USH2 is characterized by congenital mild hearing impairment with normal
CC vestibular responses. {ECO:0000269|PubMed:14740321,
CC ECO:0000269|PubMed:22147658}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Febrile seizures, familial, 4 (FEB4) [MIM:604352]: Seizures
CC associated with febrile episodes in childhood without any evidence of
CC intracranial infection or defined pathologic or traumatic cause. It is
CC a common condition, affecting 2-5% of children aged 3 months to 5
CC years. The majority are simple febrile seizures (generally defined as
CC generalized onset, single seizures with a duration of less than 30
CC minutes). Complex febrile seizures are characterized by focal onset,
CC duration greater than 30 minutes, and/or more than one seizure in a 24
CC hour period. The likelihood of developing epilepsy following simple
CC febrile seizures is low. Complex febrile seizures are associated with a
CC moderately increased incidence of epilepsy. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: By far is the largest known cell surface protein.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305|PubMed:11606593}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL30811.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB66476.2; Type=Erroneous translation; Note=Wrong genetic code use for translating the sequence.; Evidence={ECO:0000305};
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DR EMBL; AF055084; AAD55586.1; -; mRNA.
DR EMBL; AF435925; AAL30811.1; ALT_FRAME; mRNA.
DR EMBL; AC027323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC094109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB075823; BAB85529.1; -; mRNA.
DR EMBL; AL136541; CAB66476.2; ALT_SEQ; mRNA.
DR EMBL; AB014586; BAA31661.2; -; mRNA.
DR CCDS; CCDS47246.1; -. [Q8WXG9-1]
DR RefSeq; NP_115495.3; NM_032119.3. [Q8WXG9-1]
DR BioGRID; 123854; 56.
DR ComplexPortal; CPX-2821; USH2 complex.
DR CORUM; Q8WXG9; -.
DR IntAct; Q8WXG9; 22.
DR MINT; Q8WXG9; -.
DR STRING; 9606.ENSP00000384582; -.
DR TCDB; 9.A.14.6.11; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 1289; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8WXG9; 4 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (2 sites).
DR iPTMnet; Q8WXG9; -.
DR PhosphoSitePlus; Q8WXG9; -.
DR BioMuta; ADGRV1; -.
DR DMDM; 327478512; -.
DR EPD; Q8WXG9; -.
DR jPOST; Q8WXG9; -.
DR MassIVE; Q8WXG9; -.
DR PaxDb; Q8WXG9; -.
DR PeptideAtlas; Q8WXG9; -.
DR PRIDE; Q8WXG9; -.
DR ProteomicsDB; 75040; -. [Q8WXG9-1]
DR ProteomicsDB; 75041; -. [Q8WXG9-2]
DR ProteomicsDB; 75042; -. [Q8WXG9-3]
DR ProteomicsDB; 75043; -. [Q8WXG9-4]
DR Antibodypedia; 6556; 130 antibodies from 24 providers.
DR DNASU; 84059; -.
DR Ensembl; ENST00000405460.9; ENSP00000384582.2; ENSG00000164199.18. [Q8WXG9-1]
DR GeneID; 84059; -.
DR KEGG; hsa:84059; -.
DR MANE-Select; ENST00000405460.9; ENSP00000384582.2; NM_032119.4; NP_115495.3.
DR UCSC; uc003kju.4; human. [Q8WXG9-1]
DR CTD; 84059; -.
DR DisGeNET; 84059; -.
DR GeneCards; ADGRV1; -.
DR GeneReviews; ADGRV1; -.
DR HGNC; HGNC:17416; ADGRV1.
DR HPA; ENSG00000164199; Tissue enriched (adrenal).
DR MalaCards; ADGRV1; -.
DR MIM; 602851; gene.
DR MIM; 604352; phenotype.
DR MIM; 605472; phenotype.
DR neXtProt; NX_Q8WXG9; -.
DR OpenTargets; ENSG00000164199; -.
DR Orphanet; 36387; Generalized epilepsy with febrile seizures-plus.
DR Orphanet; 231178; Usher syndrome type 2.
DR VEuPathDB; HostDB:ENSG00000164199; -.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000154880; -.
DR HOGENOM; CLU_223063_0_0_1; -.
DR InParanoid; Q8WXG9; -.
DR OMA; QWKAGYP; -.
DR OrthoDB; 5733at2759; -.
DR PhylomeDB; Q8WXG9; -.
DR TreeFam; TF331149; -.
DR PathwayCommons; Q8WXG9; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; Q8WXG9; -.
DR BioGRID-ORCS; 84059; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; ADGRV1; human.
DR GeneWiki; GPR98; -.
DR GenomeRNAi; 84059; -.
DR Pharos; Q8WXG9; Tbio.
DR PRO; PR:Q8WXG9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WXG9; protein.
DR Bgee; ENSG00000164199; Expressed in right adrenal gland cortex and 137 other tissues.
DR ExpressionAtlas; Q8WXG9; baseline and differential.
DR Genevisible; Q8WXG9; HS.
DR GO; GO:0009986; C:cell surface; IDA:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:1990075; C:periciliary membrane compartment; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0002141; C:stereocilia ankle link; ISS:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IBA:GO_Central.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:1990696; C:USH2 complex; ISS:UniProtKB.
DR GO; GO:0010855; F:adenylate cyclase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:HGNC-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; IC:ComplexPortal.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:0048496; P:maintenance of animal organ identity; IMP:HGNC-UCL.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IMP:HGNC-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:HGNC-UCL.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:HGNC-UCL.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.2030; -; 35.
DR InterPro; IPR026919; ADGRV1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009039; EAR.
DR InterPro; IPR005492; EPTP.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR PANTHER; PTHR46682; PTHR46682; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF03160; Calx-beta; 35.
DR Pfam; PF03736; EPTP; 1.
DR SMART; SM00237; Calx_beta; 19.
DR SUPFAM; SSF141072; SSF141072; 38.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50912; EAR; 6.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Deafness;
KW G-protein coupled receptor; Hydrolase; Membrane; Receptor;
KW Reference proteome; Repeat; Retinitis pigmentosa; Sensory transduction;
KW Signal; Transducer; Transmembrane; Transmembrane helix; Usher syndrome;
KW Vision.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..6306
FT /note="Adhesion G-protein coupled receptor V1"
FT /id="PRO_0000232735"
FT CHAIN 30..5890
FT /note="ADGRV1 subunit alpha"
FT /evidence="ECO:0000250|UniProtKB:Q8VHN7"
FT /id="PRO_0000445731"
FT CHAIN 5891..6306
FT /note="ADGRV1 subunit beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VHN7"
FT /id="PRO_0000445732"
FT TOPO_DOM 30..5908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5909..5929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5930..5939
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5940..5960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5961..5979
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5980..6000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6001..6010
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6011..6031
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6032..6059
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6060..6080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6081..6104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6105..6125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6126..6133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6134..6154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6155..6306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..117
FT /note="Calx-beta 1"
FT /evidence="ECO:0000255"
FT DOMAIN 133..237
FT /note="Calx-beta 2"
FT /evidence="ECO:0000255"
FT DOMAIN 262..362
FT /note="Calx-beta 3"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 388..488
FT /note="Calx-beta 4"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 645..745
FT /note="Calx-beta 5"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 763..861
FT /note="Calx-beta 6"
FT /evidence="ECO:0000255"
FT DOMAIN 876..979
FT /note="Calx-beta 7"
FT /evidence="ECO:0000255"
FT DOMAIN 993..1093
FT /note="Calx-beta 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1108..1208
FT /note="Calx-beta 9"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 1444..1544
FT /note="Calx-beta 10"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 1564..1665
FT /note="Calx-beta 11"
FT /evidence="ECO:0000255"
FT DOMAIN 1710..1809
FT /note="Calx-beta 12"
FT /evidence="ECO:0000255"
FT DOMAIN 1850..1952
FT /note="Calx-beta 13"
FT /evidence="ECO:0000255"
FT DOMAIN 1966..2079
FT /note="Calx-beta 14"
FT /evidence="ECO:0000255"
FT DOMAIN 2107..2206
FT /note="Calx-beta 15"
FT /evidence="ECO:0000255"
FT DOMAIN 2222..2324
FT /note="Calx-beta 16"
FT /evidence="ECO:0000255"
FT DOMAIN 2441..2541
FT /note="Calx-beta 17"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 2584..2676
FT /note="Calx-beta 18"
FT /evidence="ECO:0000255"
FT DOMAIN 2689..2789
FT /note="Calx-beta 19"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 2814..2925
FT /note="Calx-beta 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2947..3048
FT /note="Calx-beta 21"
FT /evidence="ECO:0000255"
FT DOMAIN 3063..3172
FT /note="Calx-beta 22"
FT /evidence="ECO:0000255"
FT REPEAT 3255..3296
FT /note="EAR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3297..3345
FT /note="EAR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3348..3393
FT /note="EAR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3395..3439
FT /note="EAR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3441..3488
FT /note="EAR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3492..3534
FT /note="EAR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT DOMAIN 3525..3625
FT /note="Calx-beta 23"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 3639..3739
FT /note="Calx-beta 24"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 3775..3875
FT /note="Calx-beta 25"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 3899..4006
FT /note="Calx-beta 26"
FT /evidence="ECO:0000255"
FT DOMAIN 4020..4123
FT /note="Calx-beta 27"
FT /evidence="ECO:0000255"
FT DOMAIN 4139..4239
FT /note="Calx-beta 28"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 4255..4354
FT /note="Calx-beta 29"
FT /evidence="ECO:0000255"
FT DOMAIN 4387..4489
FT /note="Calx-beta 30"
FT /evidence="ECO:0000255"
FT DOMAIN 4512..4612
FT /note="Calx-beta 31"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 4634..4734
FT /note="Calx-beta 32"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 4992..5095
FT /note="Calx-beta 33"
FT /evidence="ECO:0000255"
FT DOMAIN 5288..5332
FT /note="Calx-beta 34"
FT /evidence="ECO:0000255"
FT DOMAIN 5368..5468
FT /note="Calx-beta 35"
FT /evidence="ECO:0000305|PubMed:11606593"
FT DOMAIN 5853..5902
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 6216..6248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6216..6244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 5890..5891
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q8VHN7"
FT VAR_SEQ 1..4339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10976914,
FT ECO:0000303|PubMed:11606593"
FT /id="VSP_017947"
FT VAR_SEQ 1461..1466
FT /note="PGILRI -> EGHHHN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_035313"
FT VAR_SEQ 1467..6306
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_035314"
FT VAR_SEQ 2296..2306
FT /note="PGETIQTLLLE -> RVVSGYPSATN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11606593"
FT /id="VSP_017948"
FT VAR_SEQ 2307..6306
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11606593"
FT /id="VSP_017949"
FT VAR_SEQ 4340..4359
FT /note="DDYPEGPEEFSLTITKVELQ -> MQLCIFCCCCILFYFDLYDF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10976914,
FT ECO:0000303|PubMed:11606593"
FT /id="VSP_017950"
FT VARIANT 127
FT /note="L -> R (in dbSNP:rs41311333)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_025995"
FT VARIANT 249
FT /note="R -> K (in dbSNP:rs41303344)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_025996"
FT VARIANT 551
FT /note="V -> A (in dbSNP:rs6889939)"
FT /id="VAR_046346"
FT VARIANT 1093
FT /note="L -> F (in dbSNP:rs2366777)"
FT /evidence="ECO:0000269|PubMed:11853319,
FT ECO:0000269|PubMed:14740321"
FT /id="VAR_025997"
FT VARIANT 1187
FT /note="I -> V (in dbSNP:rs16868935)"
FT /id="VAR_046347"
FT VARIANT 1916
FT /note="T -> I (in dbSNP:rs35791889)"
FT /id="VAR_046348"
FT VARIANT 1927
FT /note="T -> M (in dbSNP:rs17544552)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_025998"
FT VARIANT 1951
FT /note="V -> I (in dbSNP:rs4916684)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_025999"
FT VARIANT 1985
FT /note="N -> D (in dbSNP:rs41303352)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026000"
FT VARIANT 1987
FT /note="P -> L (in dbSNP:rs4916685)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026001"
FT VARIANT 2004
FT /note="L -> F (in dbSNP:rs16868972)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026002"
FT VARIANT 2097
FT /note="R -> C (in dbSNP:rs16868974)"
FT /id="VAR_046349"
FT VARIANT 2232
FT /note="Y -> C (in dbSNP:rs10037067)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026003"
FT VARIANT 2345
FT /note="N -> S (in dbSNP:rs2366926)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026004"
FT VARIANT 2379
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026005"
FT VARIANT 2584
FT /note="N -> S (in dbSNP:rs1878878)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14740321"
FT /id="VAR_026006"
FT VARIANT 2764
FT /note="S -> L (in dbSNP:rs16869016)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026007"
FT VARIANT 2803
FT /note="A -> T (in dbSNP:rs111033530)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026008"
FT VARIANT 3094
FT /note="V -> I (in dbSNP:rs13157270)"
FT /id="VAR_046350"
FT VARIANT 3217
FT /note="A -> V (in dbSNP:rs114137750)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026009"
FT VARIANT 3248
FT /note="G -> D (in dbSNP:rs16869032)"
FT /evidence="ECO:0000269|PubMed:14740321"
FT /id="VAR_026010"
FT VARIANT 3347
FT /note="F -> L (in dbSNP:rs10067636)"
FT /id="VAR_046351"
FT VARIANT 3471
FT /note="E -> K (in dbSNP:rs2366928)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14740321"
FT /id="VAR_026011"
FT VARIANT 3867
FT /note="E -> A (in dbSNP:rs16869088)"
FT /id="VAR_046352"
FT VARIANT 3868
FT /note="E -> A (in dbSNP:rs16869088)"
FT /id="VAR_055933"
FT VARIANT 4789
FT /note="R -> W (in USH2C; dbSNP:rs1131691924)"
FT /evidence="ECO:0000269|PubMed:22147658"
FT /id="VAR_068032"
FT VARIANT 5344
FT /note="E -> G (in dbSNP:rs2438374)"
FT /evidence="ECO:0000269|PubMed:10976914,
FT ECO:0000269|PubMed:11606593, ECO:0000269|PubMed:14740321,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_026012"
FT VARIANT 5437
FT /note="T -> A (in dbSNP:rs770471921)"
FT /id="VAR_026013"
FT VARIANT 5978
FT /note="H -> R (in USH2C; dbSNP:rs756460900)"
FT /evidence="ECO:0000269|PubMed:22147658"
FT /id="VAR_068033"
FT CONFLICT 107
FT /note="E -> G (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="T -> A (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="K -> E (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..437
FT /note="LTR -> VTP (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..472
FT /note="VV -> GG (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="E -> G (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="R -> W (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="T -> P (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1099
FT /note="T -> P (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1232
FT /note="V -> A (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1320
FT /note="R -> G (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1340..1342
FT /note="VNP -> GNS (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 1347
FT /note="S -> F (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 3230
FT /note="G -> D (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 3528
FT /note="A -> T (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 3552
FT /note="A -> V (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 4244
FT /note="E -> G (in Ref. 2; AAL30811)"
FT /evidence="ECO:0000305"
FT CONFLICT 5427
FT /note="V -> M (in Ref. 1; AAD55586, 2; AAL30811 and 6;
FT BAA31661)"
FT /evidence="ECO:0000305"
FT CONFLICT 5876
FT /note="V -> I (in Ref. 1; AAD55586, 2; AAL30811 and 6;
FT BAA31661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 6306 AA; 693069 MW; 30168F374ACEEF24 CRC64;
MSVFLGPGMP SASLLVNLLS ALLILFVFGE TEIRFTGQTE FVVNETSTTV IRLIIERIGE
PANVTAIVSL YGEDAGDFFD TYAAAFIPAG ETNRTVYIAV CDDDLPEPDE TFIFHLTLQK
PSANVKLGWP RTVTVTILSN DNAFGIISFN MLPSIAVSEP KGRNESMPLT LIREKGTYGM
VMVTFEVEGG PNPPDEDLSP VKGNITFPPG RATVIYNLTV LDDEVPENDE IFLIQLKSVE
GGAEINTSRN SIEIIIKKND SPVRFLQSIY LVPEEDHILI IPVVRGKDNN GNLIGSDEYE
VSISYAVTTG NSTAHAQQNL DFIDLQPNTT VVFPPFIHES HLKFQIVDDT IPEIAESFHI
MLLKDTLQGD AVLISPSVVQ VTIKPNDKPY GVLSFNSVLF ERTVIIDEDR ISRYEEITVV
RNGGTHGNVS ANWVLTRNST DPSPVTADIR PSSGVLHFAQ GQMLATIPLT VVDDDLPEEA
EAYLLQILPH TIRGGAEVSE PAELLFYIQD SDDVYGLITF FPMENQKIES SPGERYLSLS
FTRLGGTKGD VRLLYSVLYI PAGAVDPLQA KEGILNISRR NDLIFPEQKT QVTTKLPIRN
DAFLQNGAHF LVQLETVELL NIIPLIPPIS PRFGEICNIS LLVTPAIANG EIGFLSNLPI
ILHEPEDFAA EVVYIPLHRD GTDGQATVYW SLKPSGFNSK AVTPDDIGPF NGSVLFLSGQ
SDTTINITIK GDDIPEMNET VTLSLDRVNV ENQVLKSGYT SRDLIILEND DPGGVFEFSP
ASRGPYVIKE GESVELHIIR SRGSLVKQFL HYRVEPRDSN EFYGNTGVLE FKPGEREIVI
TLLARLDGIP ELDEHYWVVL SSHGERESKL GSATIVNITI LKNDDPHGII EFVSDGLIVM
INESKGDAIY SAVYDVVRNR GNFGDVSVSW VVSPDFTQDV FPVQGTVVFG DQEFSKNITI
YSLPDEIPEE MEEFTVILLN GTGGAKVGNR TTATLRIRRN DDPIYFAEPR VVRVQEGETA
NFTVLRNGSV DVTCMVQYAT KDGKATARER DFIPVEKGET LIFEVGSRQQ SISIFVNEDG
IPETDEPFYI ILLNSTGDTV VYQYGVATVI IEANDDPNGI FSLEPIDKAV EEGKTNAFWI
LRHRGYFGSV SVSWQLFQND SALQPGQEFY ETSGTVNFMD GEEAKPIILH AFPDKIPEFN
EFYFLKLVNI SGGSPGPGGQ LAETNLQVTV MVPFNDDPFG VFILDPECLE REVAEDVLSE
DDMSYITNFT ILRQQGVFGD VQLGWEILSS EFPAGLPPMI DFLLVGIFPT TVHLQQHMRR
HHSGTDALYF TGLEGAFGTV NPKYHPSRNN TIANFTFSAW VMPNANTNGF IIAKDDGNGS
IYYGVKIQTN ESHVTLSLHY KTLGSNATYI AKTTVMKYLE ESVWLHLLII LEDGIIEFYL
DGNAMPRGIK SLKGEAITDG PGILRIGAGI NGNDRFTGLM QDVRSYERKL TLEEIYELHA
MPAKSDLHPI SGYLEFRQGE TNKSFIISAR DDNDEEGEEL FILKLVSVYG GARISEENTT
ARLTIQKSDN ANGLFGFTGA CIPEIAEEGS TISCVVERTR GALDYVHVFY TISQIETDGI
NYLVDDFANA SGTITFLPWQ RSEVLNIYVL DDDIPELNEY FRVTLVSAIP GDGKLGSTPT
SGASIDPEKE TTDITIKASD HPYGLLQFST GLPPQPKDAM TLPASSVPHI TVEEEDGEIR
LLVIRAQGLL GRVTAEFRTV SLTAFSPEDY QNVAGTLEFQ PGERYKYIFI NITDNSIPEL
EKSFKVELLN LEGGVAELFR VDGSGSGDGD MEFFLPTIHK RASLGVASQI LVTIAASDHA
HGVFEFSPES LFVSGTEPED GYSTVTLNVI RHHGTLSPVT LHWNIDSDPD GDLAFTSGNI
TFEIGQTSAN ITVEILPDED PELDKAFSVS VLSVSSGSLG AHINATLTVL ASDDPYGIFI
FSEKNRPVKV EEATQNITLS IIRLKGLMGK VLVSYATLDD MEKPPYFPPN LARATQGRDY
IPASGFALFG ANQSEATIAI SILDDDEPER SESVFIELLN STLVAKVQSR SIPNSPRLGP
KVETIAQLII IANDDAFGTL QLSAPIVRVA ENHVGPIINV TRTGGAFADV SVKFKAVPIT
AIAGEDYSIA SSDVVLLEGE TSKAVPIYVI NDIYPELEES FLVQLMNETT GGARLGALTE
AVIIIEASDD PYGLFGFQIT KLIVEEPEFN SVKVNLPIIR NSGTLGNVTV QWVATINGQL
ATGDLRVVSG NVTFAPGETI QTLLLEVLAD DVPEIEEVIQ VQLTDASGGG TIGLDRIANI
IIPANDDPYG TVAFAQMVYR VQEPLERSSC ANITVRRSGG HFGRLLLFYS TSDIDVVALA
MEEGQDLLSY YESPIQGVPD PLWRTWMNVS AVGEPLYTCA TLCLKEQACS AFSFFSASEG
PQCFWMTSWI SPAVNNSDFW TYRKNMTRVA SLFSGQAVAG SDYEPVTRQW AIMQEGDEFA
NLTVSILPDD FPEMDESFLI SLLEVHLMNI SASLKNQPTI GQPNISTVVI ALNGDAFGVF
VIYNISPNTS EDGLFVEVQE QPQTLVELMI HRTGGSLGQV AVEWRVVGGT ATEGLDFIGA
GEILTFAEGE TKKTVILTIL DDSEPEDDES IIVSLVYTEG GSRILPSSDT VRVNILANDN
VAGIVSFQTA SRSVIGHEGE ILQFHVIRTF PGRGNVTVNW KIIGQNLELN FANFSGQLFF
PEGSLNTTLF VHLLDDNIPE EKEVYQVILY DVRTQGVPPA GIALLDAQGY AAVLTVEASD
EPHGVLNFAL SSRFVLLQEA NITIQLFINR EFGSLGAINV TYTTVPGMLS LKNQTVGNLA
EPEVDFVPII GFLILEEGET AAAINITILE DDVPELEEYF LVNLTYVGLT MAASTSFPPR
LDSEGLTAQV IIDANDGARG VIEWQQSRFE VNETHGSLTL VAQRSREPLG HVSLFVYAQN
LEAQVGLDYI FTPMILHFAD GERYKNVNIM ILDDDIPEGD EKFQLILTNP SPGLELGKNT
IALIIVLAND DGPGVLSFNN SEHFFLREPT ALYVQESVAV LYIVREPAQG LFGTVTVQFI
VTEVNSSNES KDLTPSKGYI VLEEGVRFKA LQISAILDTE PEMDEYFVCT LFNPTGGARL
GVHVQTLITV LQNQAPLGLF SISAVENRAT SIDIEEANRT VYLNVSRTNG IDLAVSVQWE
TVSETAFGMR GMDVVFSVFQ SFLDESASGW CFFTLENLIY GIMLRKSSVT VYRWQGIFIP
VEDLNIENPK TCEAFNIGFS PYFVITHEER NEEKPSLNSV FTFTSGFKLF LVQTIIILES
SQVRYFTSDS QDYLIIASQR DDSELTQVFR WNGGSFVLHQ KLPVRGVLTV ALFNKGGSVF
LAISQANARL NSLLFRWSGS GFINFQEVPV SGTTEVEALS SANDIYLIFA ENVFLGDQNS
IDIFIWEMGQ SSFRYFQSVD FAAVNRIHSF TPASGIAHIL LIGQDMSALY CWNSERNQFS
FVLEVPSAYD VASVTVKSLN SSKNLIALVG AHSHIYELAY ISSHSDFIPS SGELIFEPGE
REATIAVNIL DDTVPEKEES FKVQLKNPKG GAEIGINDSV TITILSNDDA YGIVAFAQNS
LYKQVEEMEQ DSLVTLNVER LKGTYGRITI AWEADGSISD IFPTSGVILF TEGQVLSTIT
LTILADNIPE LSEVVIVTLT RITTEGVEDS YKGATIDQDR SKSVITTLPN DSPFGLVGWR
AASVFIRVAE PKENTTTLQL QIARDKGLLG DIAIHLRAQP NFLLHVDNQA TENEDYVLQE
TIIIMKENIK EAHAEVSILP DDLPELEEGF IVTITEVNLV NSDFSTGQPS VRRPGMEIAE
IMIEENDDPR GIFMFHVTRG AGEVITAYEV PPPLNVLQVP VVRLAGSFGA VNVYWKASPD
SAGLEDFKPS HGILEFADKQ VTAMIEITII DDAEFELTET FNISLISVAG GGRLGDDVVV
TVVIPQNDSP FGVFGFEEKT VMIDESLSSD DPDSYVTLTV VRSPGGKGTV RLEWTIDEKA
KHNLSPLNGT LHFDETESQK TIVLHTLQDT VLEEDRRFTI QLISIDEVEI SPVKGSASII
IRGDKRASGE VGIAPSSRHI LIGEPSAKYN GTAIISLVRG PGILGEVTVF WRIFPPSVGE
FAETSGKLTM RDEQSAVIVV IQALNDDIPE EKSFYEFQLT AVSEGGVLSE SSSTANITVV
ASDSPYGRFA FSHEQLRVSE AQRVNITIIR SSGDFGHVRL WYKTMSGTAE AGLDFVPAAG
ELLFEAGEMR KSLHVEILDD DYPEGPEEFS LTITKVELQG RGYDFTIQEN GLQIDQPPEI
GNISIVRIII MKNDNAEGII EFDPKYTAFE VEEDVGLIMI PVVRLHGTYG YVTADFISQS
SSASPGGVDY ILHGSTVTFQ HGQNLSFINI SIIDDNESEF EEPIEILLTG ATGGAVLGRH
LVSRIIIAKS DSPFGVIRFL NQSKISIANP NSTMILSLVL ERTGGLLGEI QVNWETVGPN
SQEALLPQNR DIADPVSGLF YFGEGEGGVR TIILTIYPHE EIEVEETFII KLHLVKGEAK
LDSRAKDVTL TIQEFGDPNG VVQFAPETLS KKTYSEPLAL EGPLLITFFV RRVKGTFGEI
MVYWELSSEF DITEDFLSTS GFFTIADGES EASFDVHLLP DEVPEIEEDY VIQLVSVEGG
AELDLEKSIT WFSVYANDDP HGVFALYSDR QSILIGQNLI RSIQINITRL AGTFGDVAVG
LRISSDHKEQ PIVTENAERQ LVVKDGATYK VDVVPIKNQV FLSLGSNFTL QLVTVMLVGG
RFYGMPTILQ EAKSAVLPVS EKAANSQVGF ESTAFQLMNI TAGTSHVMIS RRGTYGALSV
AWTTGYAPGL EIPEFIVVGN MTPTLGSLSF SHGEQRKGVF LWTFPSPGWP EAFVLHLSGV
QSSAPGGAQL RSGFIVAEIE PMGVFQFSTS SRNIIVSEDT QMIRLHVQRL FGFHSDLIKV
SYQTTAGSAK PLEDFEPVQN GELFFQKFQT EVDFEITIIN DQLSEIEEFF YINLTSVEIR
GLQKFDVNWS PRLNLDFSVA VITILDNDDL AGMDISFPET TVAVAVDTTL IPVETESTTY
LSTSKTTTIL QPTNVVAIVT EATGVSAIPE KLVTLHGTPA VSEKPDVATV TANVSIHGTF
SLGPSIVYIE EEMKNGTFNT AEVLIRRTGG FTGNVSITVK TFGERCAQME PNALPFRGIY
GISNLTWAVE EEDFEEQTLT LIFLDGERER KVSVQILDDD EPEGQEFFYV FLTNPQGGAQ
IVEEKDDTGF AAFAMVIITG SDLHNGIIGF SEESQSGLEL REGAVMRRLH LIVTRQPNRA
FEDVKVFWRV TLNKTVVVLQ KDGVNLVEEL QSVSGTTTCT MGQTKCFISI ELKPEKVPQV
EVYFFVELYE ATAGAAINNS ARFAQIKILE SDESQSLVYF SVGSRLAVAH KKATLISLQV
ARDSGTGLMM SVNFSTQELR SAETIGRTII SPAISGKDFV ITEGTLVFEP GQRSTVLDVI
LTPETGSLNS FPKRFQIVLF DPKGGARIDK VYGTANITLV SDADSQAIWG LADQLHQPVN
DDILNRVLHT ISMKVATENT DEQLSAMMHL IEKITTEGKI QAFSVASRTL FYEILCSLIN
PKRKDTRGFS HFAEVTENFA FSLLTNVTCG SPGEKSKTIL DSCPYLSILA LHWYPQQING
HKFEGKEGDY IRIPERLLDV QDAEIMAGKS TCKLVQFTEY SSQQWFISGN NLPTLKNKVL
SLSVKGQSSQ LLTNDNEVLY RIYAAEPRII PQTSLCLLWN QAAASWLSDS QFCKVVEETA
DYVECACSHM SVYAVYARTD NLSSYNEAFF TSGFICISGL CLAVLSHIFC ARYSMFAAKL
LTHMMAASLG TQILFLASAY ASPQLAEESC SAMAAVTHYL YLCQFSWMLI QSVNFWYVLV
MNDEHTERRY LLFFLLSWGL PAFVVILLIV ILKGIYHQSM SQIYGLIHGD LCFIPNVYAA
LFTAALVPLT CLVVVFVVFI HAYQVKPQWK AYDDVFRGRT NAAEIPLILY LFALISVTWL
WGGLHMAYRH FWMLVLFVIF NSLQGLYVFM VYFILHNQMC CPMKASYTVE MNGHPGPSTA
FFTPGSGMPP AGGEISKSTQ NLIGAMEEVP PDWERASFQQ GSQASPDLKP SPQNGATFPS
SGGYGQGSLI ADEESQEFDD LIFALKTGAG LSVSDNESGQ GSQEGGTLTD SQIVELRRIP
IADTHL
