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   24-JAN-2024, entry version 173.
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, VLGR1
GN   {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; 58.
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   GlyCosmos; Q8WXG9; 4 sites, 3 glycans.
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; 9606-ENSP00000384582; -.
DR   PeptideAtlas; Q8WXG9; -.
DR   ProteomicsDB; 75040; -. [Q8WXG9-1]
DR   ProteomicsDB; 75041; -. [Q8WXG9-2]
DR   ProteomicsDB; 75042; -. [Q8WXG9-3]
DR   ProteomicsDB; 75043; -. [Q8WXG9-4]
DR   Antibodypedia; 6556; 144 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   AGR; HGNC:17416; -.
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; RYTAFEV; -.
DR   OrthoDB; 2912542at2759; -.
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; 15 hits in 1157 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 138 other cell types or tissues.
DR   ExpressionAtlas; Q8WXG9; baseline and differential.
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:0016020; C:membrane; TAS:GDB.
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: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; NAS: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; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.60.40.2030; -; 35.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR46682; ADHESION G-PROTEIN COUPLED RECEPTOR V1; 1.
DR   PANTHER; PTHR46682:SF1; ADHESION G-PROTEIN COUPLED RECEPTOR V1; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF03160; Calx-beta; 32.
DR   Pfam; PF03736; EPTP; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00237; Calx_beta; 19.
DR   SUPFAM; SSF141072; CalX-like; 38.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50912; EAR; 6.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   Genevisible; Q8WXG9; HS.
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
//