AGRV1_MOUSE
ID AGRV1_MOUSE Reviewed; 6298 AA.
AC Q8VHN7; Q6ZQ69; Q810D2; Q810D3; Q91ZS0; Q91ZS1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adhesion G-protein coupled receptor V1 {ECO:0000305};
DE Short=ADGRV1 {ECO:0000305};
DE EC=3.4.-.- {ECO:0000269|PubMed:24962568};
DE AltName: Full=G-protein coupled receptor 98;
DE AltName: Full=Monogenic audiogenic seizure susceptibility protein 1 {ECO:0000303|PubMed:24191038};
DE Short=MASS1 {ECO:0000303|PubMed:24191038};
DE AltName: Full=Neurepin;
DE AltName: Full=Protein rueda {ECO:0000303|PubMed:17329413};
DE AltName: Full=Very large G-protein coupled receptor 1 {ECO:0000303|PubMed:24191038};
DE Short=VLGR1 {ECO:0000303|PubMed:24191038};
DE Contains:
DE RecName: Full=ADGRV1 subunit alpha {ECO:0000305};
DE Contains:
DE RecName: Full=ADGRV1 subunit beta {ECO:0000305};
DE AltName: Full=VLGR1 subunit beta {ECO:0000303|PubMed:24962568};
DE Short=Vbeta {ECO:0000303|PubMed:24962568};
DE Flags: Precursor;
GN Name=Adgrv1 {ECO:0000312|MGI:MGI:1274784};
GN Synonyms=Gpr98, Kiaa0686, Mass1 {ECO:0000303|PubMed:24191038},
GN Vlgr1 {ECO:0000303|PubMed:17567809, ECO:0000303|PubMed:20502675,
GN ECO:0000303|PubMed:24191038};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND INVOLVEMENT IN MONOGENIC
RP AUDIOGENIC SEIZURE SUSCEPTIBILITY.
RC STRAIN=C57BL/6J;
RX PubMed=11545713; DOI=10.1016/s0896-6273(01)00397-x;
RA Skradski S.L., Clark A.M., Jiang H., White H.S., Fu Y., Ptacek L.J.;
RT "A novel gene causing a Mendelian audiogenic mouse epilepsy.";
RL Neuron 31:537-544(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
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 [MRNA] (ISOFORMS 4 AND 5), DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15606908; DOI=10.1111/j.1471-4159.2004.02875.x;
RA Yagi H., Takamura Y., Yoneda T., Konno D., Akagi Y., Yoshida K., Sato M.;
RT "Vlgr1 knockout mice show audiogenic seizure susceptibility.";
RL J. Neurochem. 92:191-202(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4816-6298.
RC TISSUE=Pancreatic islet;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DOMAIN.
RX PubMed=16775142; DOI=10.1523/jneurosci.0693-06.2006;
RA McGee J., Goodyear R.J., McMillan D.R., Stauffer E.A., Holt J.R.,
RA Locke K.G., Birch D.G., Legan P.K., White P.C., Walsh E.J.,
RA Richardson G.P.;
RT "The very large G-protein-coupled receptor VLGR1: a component of the ankle
RT link complex required for the normal development of auditory hair
RT bundles.";
RL J. Neurosci. 26:6543-6553(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17329413; DOI=10.1523/jneurosci.4975-06.2007;
RA Schwander M., Sczaniecka A., Grillet N., Bailey J.S., Avenarius M.,
RA Najmabadi H., Steffy B.M., Federe G.C., Lagler E.A., Banan R., Hice R.,
RA Grabowski-Boase L., Keithley E.M., Ryan A.F., Housley G.D., Wiltshire T.,
RA Smith R.J., Tarantino L.M., Mueller U.;
RT "A forward genetics screen in mice identifies recessive deafness traits and
RT reveals that pejvakin is essential for outer hair cell function.";
RL J. Neurosci. 27:2163-2175(2007).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH MYO7A.
RX PubMed=17567809; DOI=10.1523/jneurosci.0342-07.2007;
RA Michalski N., Michel V., Bahloul A., Lefevre G., Barral J., Yagi H.,
RA Chardenoux S., Weil D., Martin P., Hardelin J.P., Sato M., Petit C.;
RT "Molecular characterization of the ankle-link complex in cochlear hair
RT cells and its role in the hair bundle functioning.";
RL J. Neurosci. 27:6478-6488(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION IN
RP THE USH2 COMPLEX.
RX PubMed=20502675; DOI=10.1371/journal.pgen.1000955;
RA Yang J., Liu X., Zhao Y., Adamian M., Pawlyk B., Sun X., McMillan D.R.,
RA Liberman M.C., Li T.;
RT "Ablation of whirlin long isoform disrupts the USH2 protein complex and
RT causes vision and hearing loss.";
RL PLoS Genet. 6:E1000955-E1000955(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22419726; DOI=10.1210/jc.2011-2393;
RA Urano T., Shiraki M., Yagi H., Ito M., Sasaki N., Sato M., Ouchi Y.,
RA Inoue S.;
RT "GPR98/Gpr98 gene is involved in the regulation of human and mouse bone
RT mineral density.";
RL J. Clin. Endocrinol. Metab. 97:E565-E574(2012).
RN [11]
RP INTERACTION WITH PDZD7 AND WHRN.
RX PubMed=23055499; DOI=10.1523/jneurosci.3071-12.2012;
RA Grati M., Shin J.B., Weston M.D., Green J., Bhat M.A., Gillespie P.G.,
RA Kachar B.;
RT "Localization of PDZD7 to the stereocilia ankle-link associates this
RT scaffolding protein with the Usher syndrome protein network.";
RL J. Neurosci. 32:14288-14293(2012).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24191038; DOI=10.1073/pnas.1318501110;
RA Shin D., Lin S.T., Fu Y.H., Ptacek L.J.;
RT "Very large G protein-coupled receptor 1 regulates myelin-associated
RT glycoprotein via Galphas/Galphaq-mediated protein kinases A/C.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19101-19106(2013).
RN [13]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, SUBUNIT, MUTAGENESIS OF HIS-5882; SER-5884
RP AND ARG-6002, AND INTERACTION WITH PDZD7.
RX PubMed=24962568; DOI=10.1074/jbc.m114.549816;
RA Hu Q.X., Dong J.H., Du H.B., Zhang D.L., Ren H.Z., Ma M.L., Cai Y.,
RA Zhao T.C., Yin X.L., Yu X., Xue T., Xu Z.G., Sun J.P.;
RT "Constitutive Galphai coupling activity of very large G protein-coupled
RT receptor 1 (VLGR1) and its regulation by PDZD7 protein.";
RL J. Biol. Chem. 289:24215-24225(2014).
RN [14]
RP IDENTIFICATION IN THE USH2 COMPLEX.
RX PubMed=25406310; DOI=10.1074/jbc.m114.610535;
RA Chen Q., Zou J., Shen Z., Zhang W., Yang J.;
RT "Whirlin and PDZ domain-containing 7 (PDZD7) proteins are both required to
RT form the quaternary protein complex associated with Usher syndrome type
RT 2.";
RL J. Biol. Chem. 289:36070-36088(2014).
RN [15]
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=24334608; DOI=10.1093/hmg/ddt629;
RA Zou J., Zheng T., Ren C., Askew C., Liu X.P., Pan B., Holt J.R., Wang Y.,
RA Yang J.;
RT "Deletion of PDZD7 disrupts the Usher syndrome type 2 protein complex in
RT cochlear hair cells and causes hearing loss in mice.";
RL Hum. Mol. Genet. 23:2374-2390(2014).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=27525485; DOI=10.7554/elife.18312;
RA Morgan C.P., Krey J.F., Grati M., Zhao B., Fallen S., Kannan-Sundhari A.,
RA Liu X.Z., Choi D., Mueller U., Barr-Gillespie P.G.;
RT "PDZD7-MYO7A complex identified in enriched stereocilia membranes.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: G-protein coupled receptor which has an essential role in the
CC development of hearing and vision (PubMed:16775142, PubMed:17567809,
CC PubMed:20502675, PubMed:24191038). 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 (PubMed:24191038, PubMed:24962568). Required for the hair bundle ankle
CC formation, which connects growing stereocilia in developing cochlear
CC hair cells of the inner ear (PubMed:16775142, PubMed:17567809). 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 (PubMed:24191038). In retina photoreceptors, the USH2
CC complex is required for the maintenance of periciliary membrane complex
CC that seems to play a role in regulating intracellular protein transport
CC (PubMed:20502675). Involved in the regulation of bone metabolism
CC (PubMed:22419726). {ECO:0000269|PubMed:16775142,
CC ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:22419726, ECO:0000269|PubMed:24191038,
CC ECO:0000269|PubMed:24962568}.
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:0000269|PubMed:24962568}.
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) (PubMed:24962568). Interacts (via the cytoplasmic
CC region) with PDZD7 (PubMed:24962568, PubMed:23055499). Component of
CC USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN
CC (PubMed:20502675, PubMed:25406310). Interacts with USH2A and WHRN
CC (PubMed:20502675, PubMed:23055499). Interacts (via the cytoplasmic
CC region) with MYO7A (via MyTH4-FERM domains) (PubMed:17567809).
CC {ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:24962568,
CC ECO:0000269|PubMed:25406310}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15606908};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15606908}. Cell
CC projection, stereocilium membrane {ECO:0000269|PubMed:16775142,
CC ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}.
CC Photoreceptor inner segment {ECO:0000269|PubMed:20502675,
CC ECO:0000269|PubMed:24334608}. Note=Localizes at the ankle region of the
CC stereocilia (PubMed:16775142, PubMed:27525485). In photoreceptors,
CC localizes at a plasma membrane microdomain in the apical inner segment
CC that surrounds the connecting cilia called periciliary membrane complex
CC (PubMed:20502675, PubMed:24334608). {ECO:0000269|PubMed:16775142,
CC ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608,
CC ECO:0000269|PubMed:27525485}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted
CC {ECO:0000269|PubMed:15606908}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted
CC {ECO:0000269|PubMed:15606908}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8VHN7-1; Sequence=Displayed;
CC Name=2; Synonyms=Mass1.2;
CC IsoId=Q8VHN7-2; Sequence=VSP_017952, VSP_017955, VSP_017959,
CC VSP_017960;
CC Name=3; Synonyms=Mass1.3;
CC IsoId=Q8VHN7-3; Sequence=VSP_017951, VSP_017958, VSP_017959,
CC VSP_017960;
CC Name=4; Synonyms=Neurepin-2, Vlgr1e;
CC IsoId=Q8VHN7-4; Sequence=VSP_017956, VSP_017957;
CC Name=5; Synonyms=Neurepin-1, Vlgr1d;
CC IsoId=Q8VHN7-5; Sequence=VSP_017953, VSP_017954;
CC -!- TISSUE SPECIFICITY: Expressed by oligodendrocytes. In midbrain,
CC enriched in the myelinated regions of the superior and inferior
CC colliculi (PubMed:24191038). In the cochlea, expressed in developing
CC hair cells (PubMed:16775142, PubMed:20502675, PubMed:17567809).
CC Expressed by photoreceptors in the retina (PubMed:20502675).
CC {ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:17567809,
CC ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24191038}.
CC -!- DEVELOPMENTAL STAGE: High level expression restricted to the developing
CC central nervous system and eye. At mid-gestation expression is
CC prominent in the ventricular zone and in the eye. At late gestation
CC expression declines (PubMed:11606593). In the inner ear, highly
CC expressed at 17 dpc at the base of emerging hair bundle and on
CC peripheral subpopulation of microvilli located at the neural edge of
CC the hair cell apical surface. At P0-P1, the expression extends from the
CC very base of the stereocilia. From P4 to P9, expression becomes
CC restricted, forming a basal band-like pattern at the ankle link level
CC above the stereocilia. From P12 onward, no longer detectable in the
CC cochlear hair cells (PubMed:16775142, PubMed:20502675). In the utricle
CC of the vestibular system, the expression persists for longer, being
CC present at both P4 and P11, but no longer detectable by P18
CC (PubMed:16775142). {ECO:0000269|PubMed:11606593,
CC ECO:0000269|PubMed:16775142, ECO:0000269|PubMed:20502675}.
CC -!- DOMAIN: The 7 transmembrane domain is required in hair cells for the
CC hair bundle ankle formation. {ECO:0000269|PubMed:16775142}.
CC -!- PTM: Autoproteolytically cleaved into 2 subunits, an extracellular
CC alpha subunit and a seven-transmembrane subunit.
CC {ECO:0000269|PubMed:24962568}.
CC -!- DISRUPTION PHENOTYPE: Mice display hearing loss and audiogenic epilepsy
CC (PubMed:15606908, PubMed:17329413). Audiogenic epilepsy syndrome is an
CC autosomal recessive mutation, characterized by generalized self-
CC sustained convulsive seizures in which acoustics stimulations evoke
CC wild running, tonic flexion and extension (PubMed:15606908). They are
CC induced by exposing animals to a loud noise during the early stages of
CC their development (PubMed:15606908). Mutants show a decreased bone
CC mineral density (PubMed:22419726). {ECO:0000269|PubMed:15606908,
CC ECO:0000269|PubMed:17329413, ECO:0000269|PubMed:22419726}.
CC -!- MISCELLANEOUS: [Isoform 4]: Secreted. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Secreted. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AF405693; AAL06013.1; -; mRNA.
DR EMBL; AF405694; AAL06014.1; -; mRNA.
DR EMBL; AF435926; AAL30812.1; -; mRNA.
DR EMBL; AB086166; BAC66505.2; -; mRNA.
DR EMBL; AB086167; BAC66506.1; -; mRNA.
DR EMBL; AK129190; BAC98000.3; -; mRNA.
DR CCDS; CCDS36737.1; -. [Q8VHN7-1]
DR ComplexPortal; CPX-2501; USH2 complex.
DR CORUM; Q8VHN7; -.
DR IntAct; Q8VHN7; 1.
DR STRING; 10090.ENSMUSP00000093245; -.
DR iPTMnet; Q8VHN7; -.
DR PhosphoSitePlus; Q8VHN7; -.
DR MaxQB; Q8VHN7; -.
DR PaxDb; Q8VHN7; -.
DR PRIDE; Q8VHN7; -.
DR ProteomicsDB; 271279; -. [Q8VHN7-1]
DR ProteomicsDB; 271280; -. [Q8VHN7-2]
DR ProteomicsDB; 271282; -. [Q8VHN7-4]
DR ProteomicsDB; 271283; -. [Q8VHN7-5]
DR Antibodypedia; 6556; 130 antibodies from 24 providers.
DR Ensembl; ENSMUST00000128585; ENSMUSP00000121899; ENSMUSG00000069170. [Q8VHN7-5]
DR UCSC; uc007rht.1; mouse. [Q8VHN7-5]
DR MGI; MGI:1274784; Adgrv1.
DR VEuPathDB; HostDB:ENSMUSG00000069170; -.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000154880; -.
DR InParanoid; Q8VHN7; -.
DR PhylomeDB; Q8VHN7; -.
DR ChiTaRS; Adgrv1; mouse.
DR PRO; PR:Q8VHN7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VHN7; protein.
DR Bgee; ENSMUSG00000069170; Expressed in floor plate of midbrain and 126 other tissues.
DR ExpressionAtlas; Q8VHN7; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0002141; C:stereocilia ankle link; IDA:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; EXP:MGI.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990696; C:USH2 complex; IDA:UniProtKB.
DR GO; GO:0010855; F:adenylate cyclase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IPI:MGI.
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; IDA:MGI.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; IC:ComplexPortal.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0048496; P:maintenance of animal organ identity; ISO:MGI.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IDA:MGI.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
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 InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR46682; PTHR46682; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF03160; Calx-beta; 37.
DR Pfam; PF03736; EPTP; 1.
DR SMART; SM00237; Calx_beta; 20.
DR SMART; SM00560; LamGL; 1.
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;
KW Developmental protein; G-protein coupled receptor; Hydrolase; Membrane;
KW Receptor; Reference proteome; Repeat; Secreted; Sensory transduction;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..6298
FT /note="Adhesion G-protein coupled receptor V1"
FT /id="PRO_0000232736"
FT CHAIN 29..5883
FT /note="ADGRV1 subunit alpha"
FT /evidence="ECO:0000303|PubMed:24962568"
FT /id="PRO_0000445733"
FT CHAIN 5884..6298
FT /note="ADGRV1 subunit beta"
FT /evidence="ECO:0000303|PubMed:24962568"
FT /id="PRO_0000445734"
FT TOPO_DOM 29..5901
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5902..5922
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5923..5932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5933..5953
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5954..5973
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5974..5994
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5995..6003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6004..6024
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6025..6052
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6053..6073
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6074..6097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6098..6118
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6119..6126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6127..6147
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 6148..6298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..116
FT /note="Calx-beta 1"
FT /evidence="ECO:0000255"
FT DOMAIN 132..236
FT /note="Calx-beta 2"
FT /evidence="ECO:0000255"
FT DOMAIN 251..362
FT /note="Calx-beta 3"
FT /evidence="ECO:0000255"
FT DOMAIN 389..489
FT /note="Calx-beta 4"
FT /evidence="ECO:0000305"
FT DOMAIN 646..746
FT /note="Calx-beta 5"
FT /evidence="ECO:0000305"
FT DOMAIN 764..862
FT /note="Calx-beta 6"
FT /evidence="ECO:0000255"
FT DOMAIN 877..980
FT /note="Calx-beta 7"
FT /evidence="ECO:0000255"
FT DOMAIN 994..1094
FT /note="Calx-beta 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1108..1208
FT /note="Calx-beta 9"
FT /evidence="ECO:0000305"
FT DOMAIN 1440..1540
FT /note="Calx-beta 10"
FT /evidence="ECO:0000305"
FT DOMAIN 1562..1662
FT /note="Calx-beta 11"
FT /evidence="ECO:0000305"
FT DOMAIN 1706..1805
FT /note="Calx-beta 12"
FT /evidence="ECO:0000255"
FT DOMAIN 1846..1948
FT /note="Calx-beta 13"
FT /evidence="ECO:0000255"
FT DOMAIN 1962..2075
FT /note="Calx-beta 14"
FT /evidence="ECO:0000255"
FT DOMAIN 2103..2202
FT /note="Calx-beta 15"
FT /evidence="ECO:0000255"
FT DOMAIN 2218..2320
FT /note="Calx-beta 16"
FT /evidence="ECO:0000255"
FT DOMAIN 2437..2537
FT /note="Calx-beta 17"
FT /evidence="ECO:0000305"
FT DOMAIN 2576..2672
FT /note="Calx-beta 18"
FT /evidence="ECO:0000255"
FT DOMAIN 2687..2786
FT /note="Calx-beta 19"
FT /evidence="ECO:0000255"
FT DOMAIN 2810..2921
FT /note="Calx-beta 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2945..3044
FT /note="Calx-beta 21"
FT /evidence="ECO:0000255"
FT DOMAIN 3067..3167
FT /note="Calx-beta 22"
FT /evidence="ECO:0000305"
FT REPEAT 3251..3292
FT /note="EAR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3293..3341
FT /note="EAR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3344..3389
FT /note="EAR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3391..3435
FT /note="EAR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3437..3484
FT /note="EAR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 3488..3530
FT /note="EAR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT DOMAIN 3581..3622
FT /note="Calx-beta 23"
FT /evidence="ECO:0000255"
FT DOMAIN 3636..3736
FT /note="Calx-beta 24"
FT /evidence="ECO:0000305"
FT DOMAIN 3772..3872
FT /note="Calx-beta 25"
FT /evidence="ECO:0000305"
FT DOMAIN 3919..4003
FT /note="Calx-beta 26"
FT /evidence="ECO:0000255"
FT DOMAIN 4017..4120
FT /note="Calx-beta 27"
FT /evidence="ECO:0000255"
FT DOMAIN 4135..4235
FT /note="Calx-beta 28"
FT /evidence="ECO:0000305"
FT DOMAIN 4251..4351
FT /note="Calx-beta 29"
FT /evidence="ECO:0000255"
FT DOMAIN 4384..4484
FT /note="Calx-beta 30"
FT /evidence="ECO:0000255"
FT DOMAIN 4507..4607
FT /note="Calx-beta 31"
FT /evidence="ECO:0000305"
FT DOMAIN 4628..4728
FT /note="Calx-beta 32"
FT /evidence="ECO:0000305"
FT DOMAIN 4989..5089
FT /note="Calx-beta 33"
FT /evidence="ECO:0000255"
FT DOMAIN 5281..5325
FT /note="Calx-beta 34"
FT /evidence="ECO:0000255"
FT DOMAIN 5361..5461
FT /note="Calx-beta 35"
FT /evidence="ECO:0000305"
FT DOMAIN 5846..5895
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 6206..6242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6264..6283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6206..6233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6264..6282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 5883..5884
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:24962568"
FT VAR_SEQ 1..1804
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017951"
FT VAR_SEQ 1..720
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017952"
FT VAR_SEQ 615..616
FT /note="LE -> VL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15606908"
FT /id="VSP_017953"
FT VAR_SEQ 617..6298
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15606908"
FT /id="VSP_017954"
FT VAR_SEQ 721..748
FT /note="QNETSINITVKGDDIPELNETVTLSLDR -> MCLPSLCPSHCSFCVDRVET
FT ERFVVYFG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017955"
FT VAR_SEQ 1213..1218
FT /note="PGGQLA -> TNLSHL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15606908"
FT /id="VSP_017956"
FT VAR_SEQ 1219..6298
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15606908"
FT /id="VSP_017957"
FT VAR_SEQ 1805..1810
FT /note="LNLDGG -> MCVACE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017958"
FT VAR_SEQ 2938..2958
FT /note="DSEGLTAQIVIDANDGAQGMI -> GMGLSFMNLLTNCESQRTSLF (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017959"
FT VAR_SEQ 2959..6298
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11545713"
FT /id="VSP_017960"
FT MUTAGEN 5882
FT /note="H->A: Reduces autoproteolysis. No effect on
FT inhibition of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:24962568"
FT MUTAGEN 5884
FT /note="S->A: Abolishes autoproteolysis. No effect on
FT inhibition of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:24962568"
FT MUTAGEN 6002
FT /note="R->A: Abolishes coupling to G(i)-proteins. Abolishes
FT inhibition of adenylate cyclase activity. No effect on
FT interaction with PDZD7."
FT /evidence="ECO:0000269|PubMed:24962568"
FT CONFLICT 412..416
FT /note="SSRFE -> RYNLL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="A -> S (in Ref. 3; BAC66506)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="V -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="R -> C (in Ref. 3; BAC66506)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="S -> T (in Ref. 3; BAC66506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1282
FT /note="E -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1508
FT /note="G -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1933
FT /note="S -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1955
FT /note="L -> M (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1994
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2047
FT /note="V -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2251..2252
FT /note="NV -> SA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2672
FT /note="G -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 4816..4832
FT /note="VITDGARYKVGLVPLKN -> PLIGCPCSSGWCSTMHI (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5084
FT /note="Y -> F (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5127
FT /note="A -> V (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5205
FT /note="V -> L (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5282
FT /note="V -> F (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5314..5315
FT /note="DA -> EP (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5417
FT /note="A -> L (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5578
FT /note="A -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5630
FT /note="R -> Q (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 6122
FT /note="G -> R (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 6298 AA; 687458 MW; F99E731B0ADBD66D CRC64;
MSVTSEPGMI SSFLLVYLST LFISFVFGEA EIRFTGQTEF FVNETSTTVI RLVIERIGEP
ANVTAIVSLS GEDTGDFFDT YAAAFIPARG TNRTVYIAVC DDDLPEPDET FTFHLTLQKP
SANVKLGWPR AASVTILSND NAFGIISFST PSSISVIEPR SRNASVPLTL IREKGTYGMV
TVTFDVSGGP NPPEEDLNPV RGNITFPPGR ATVIYNVTVL DDEVPENDEL FLIQLRSVEG
GAEINASRSS VEIIVKKNDS PVNFMQSVYV VPEDDHVLTI PVLRGKDSDG NLIGSDETQV
SIRYKVMTWD STAHAQQNVD FIDLQPDTTL VFPPFVHESH LKFQIIDDLI PEIAESFHIM
LLKNTLQGDA VLMGPSTVQV TIKPNDKPYG VLSFNSILFE RPVIIDEDTA SSSRFEEIAV
VRNGGTHGNV SVSWVLTRNS SDPSPVTADI TPASGTLQFA QGQMLAPISL VVFDDDLPEE
AEAYLLTILP HTIQGGAEVS EPAQLLFYIQ DSDNVYGEIA FFPGESQKIE SSPSERSLSL
SLARRGGSKG DVRVIYSALY IPAGAMDPLR AKDGILNTSR RSSLLFPEQN QQVSIKLPIR
NDAFLQNGAH FLVQLEAVVL VNIFPPIPPV SPRFGEIRNI SLLVTPAIAN GEIGFLSNLP
IILHEPKDSS AEVVSIPLHR DGTDGQATVY WSLRPSGFNS KAVTLDDAGP FNGSVVFLSG
QNETSINITV KGDDIPELNE TVTLSLDRVS VDSDVLKSGY TSRDLIILEN DDPGGIFEFS
YDSRGPYVIK EGDAVELRIT RSRGSLVKQF LRFHVEPRES NEFYGNMGVL EFTPGEREVV
ITLLTRLDGT PELDEHFWVI LSSHGERESK LGRATLVNIT ILKNDYPHGI IEFVSDGLSA
SIKESKGEDI YHAVYGVIRT RGNFGAVNVS WMVSPDFTQD VFPVQGTVCF GDQEFFKNIT
VYSLVDEIPE EMEEFTIILL NATGGAQTGI RTTASLRILR NDDPVYFAEP CVLRVQEGET
ANFTVLRNGS VDGACTVQYA TVDGKASGEE GDFAPVEKGE TLVFEVGSRE QSISVHVKDD
GIPETDEPFY IVLFNSTGDT VVYEYGVATV IIEANDDPNG VFSLEPIDKA VEEGKTNAFW
ILRHRGHFGN VSVAWQLFQN ASLQPGQEFY ETSGTVNFTD GEETKPVILR AFPDRIPEFN
EFYILRLVNI SGPGGQLAET NFQVTVMIPF NDDPFGIFIL DPECLEREVA EDVLSEDDMS
YITSFTILRQ QGVFGDVRVG WEVLSREFTA GLPPMIDFIL LGSFPSTVPL QPHMRRHHSG
TDVLYFSGLE GAFGTVDPKY QPFRNNTIAN FTFSAWVMPN ANTNGFLIAK DDSHGSIYYG
VKIQTNETHV TLSLHYKTFG SNVTYIAKST VMKYLEEGVW LHVLIILDDG IIEFYLDGKA
MPRGIKSLKG EAITDGPGIL RIGAGMDGGA RFTGWMQDVR TYERKLTPEE IYELHAVPAR
TDLHPISGYL EFRQGESNKS FIVAARDDSE EEGEELFLLK LVSVDGGAQI SKENTTARLR
IQKSDNANGL FGFTGACIPE MTEEGSTVSC VVERTRGALG YVHVFYTISQ IESEGINYLV
DDFANASGTI TFLPWQRSEV LNLYVLDEDM PELNEYFRVT LVSAVPGDGK LGSTPISGAS
IDPEKETTGI TVKASDHPYG LMQFSTGLPP QPEDSMSLPA SSVPHITVQE EDGEIRLLVI
RAQGLLGRVT VGFRTVSLTA FSPEDYQSTA GTLEFQSGER YKYIFVNITD NSIPELEKSF
KVELLNLDGG VSDLFRVDGS GSGEADTDFF LPPVLPHASL GVASQILVTI AASDHAHGVF
EFSPESLFVS GTEPEDGYST VVLNVTRTRG ALSAVTLQWK VDSDLDGDLA ITSGNITFET
GQRIASITVE ILSDEEPELD KALTVSILNV SSGSLGVLTN ATLTILASDD PYGVFIFPNK
TRPLSVEEAT QNVALSIIRL KGLMGEVAVS YATIDDMEKP PYFPPNLARA TQGGDYISAS
GLALFRVNQT EATITISILD DAEPERSESV FIELFNSSLV DKVQNRPIPH SPRLGPKVET
VAHLVIVAND DAFGTVQLSA TSVHVAENHV GPIINVTRTG GTFADVSVKF KAVPITAAAG
EDYSIASSDV VLLEGETTKA VPIYIINDIY PELEETFLVQ LLNETTGGAT LGPLREAVIT
IEASDDPYGL FGFQNTKFIV EEPEFNSVRV NVPIIRNSGT LGNVTVQWVA IINGQFATGD
LRVVSGNVTF APGETIQTLL LEVLADDVPE IEEVVQVQLA AASGGGTIGL DRVANIVIPA
NDNPYGSVAF VQSVFRVQEP LERSSYANIT VRRSGGHFGR LLLCYGTSDI DVVARAVEEG
EDVLSYYESP TQGVPDPLWR TWVNVSAVEE TQYTCATLCL KERACSAFSV VSGAEGPRCF
WMTSWVSGTV NSSDFQTYKK NMTRVASLFS GQAVAGSDYE PVTRQWAVIL EGDEFANLTV
SVLPDDAPEM DESFLISLLE VHLMNISDSF KNQPTIGHPN TSAVVIGLNG DAFGVFIIYS
VSPNTSEDGL CVEVQEQPQT SVELVIYRTG GSLGQVMVEW RVVGGTATEG LDFMGAGDIL
TFAEGETKKM AILTILDDSE PEDNESILVR LGATEGGSRI LPSSDTVTVN ILANDNVAGI
VSFQTASRSV IGHEGEMLQF HVVRTPPGRG NVTVNWKVVG QNLEVNFANF TGQLFFSEGT
LNKTIFVHLL DDNIPEEKEV YQVVLYDVKT QGVSPAGVAL LDAQGYAAVL TVEASDEPHG
VLNFALSSRF VVLQEANVTI QLFVNREFGS LGAINVTYAT VPGIVSLKNN TEGNLAEPES
DFIPVVGSLV LEEGETTAAI SITVLEDDIP ELKEYFLVNL THVDLIMAPL TSSPPRLDSE
GLTAQIVIDA NDGAQGMIEW QRNRFEVNET DGVVTLVAQR SRAALGQVSL FMYAQNLEAQ
AGLDYMRTPQ ILHFTDGERF KHVDVMILDD DMPEGDERFQ LLLTNPSPGL ELGKNTIALI
TVLANDDGPG VLSFNNSGHI FLREPTSLYV QESVAVLVIV REPAQGLFGT VAVQFVVTEV
NSSTESKDLS PSKGFIVLEE GVRSKTLRIS AILDTEPEMD EHFVCTLFNP TGGARLGAHV
QTLITIFQNQ APLGLFSISA VENSATSIDV EESNRSVYLN VSRTNGLDLT ASVQWETVSE
TAFGMRGMDV VFSIFQSFFD KTALDWCFFT VEGSVYGVML RKSSLVVYRW QGTFVPVEDL
KVESPKTCEA FNIGVSPYLV ITHGERSGEK PSINSVYMLT AGFRLVLIQT IIISGSCQVR
HFTSDSQDYF IIASRRNDSE LTQVFRWNGN NFAWHQTLPV RGVLGMALFS RGGSVFLAIS
QANIRQTSLL FTWSGTQFIN FQELPISGIT QVEALSSGDD VYLCFAKNTF LGNQNAIDIF
VWEMGHSSLR YFQSLDFAAV KRIRSFTPAS GIVHILLTAQ DGSALYCWNS ELNAFSFVLE
APAAHDAAFV TVKSLNSSKT LIALVGATDS HLYELTYVSS QSDFIPSLGE LIFEPGDKEA
IIAVNVLDDT VPEKEESFRV QLKSPRGGAE IGINSSVRVT VLANDGAYGV VAFAQNSLHK
QLEELERDSL VTLNVERLRG THGRITVAWE AAGSVSDVFP TSGVISFTED QAMSMITLTV
LADDLPELSE AVVVTLTQIV TEGVEDPLKG ATIDQSRSRS VLTILPSDSP YGAVRWHTES
LFNRVPEPTE NITVVQLHIV RDKGLFGDIS IHLIAKPNFL LHINNQATED EDFVLQDSVI
IMKENIKETH AEVAILPDEV PELDEGLIVT IAAVNLVNPN FPAEQPRVQR PRMESAEILI
EENDDPRGIF NFHVVRDVGG VIIAHEGPPP LNVLQVPVVR MAGTFETVNV YWKATPDSAG
LEDFQPSHGM LQFADGQVIA PILVTIIDDS EFELLETFTI SLVSVTGGGR LGDDVSVNVV
IAPNDSPFGI FGFEKKTVMV DGPLLSDDPD SYVTLTVVRS PGGKGAVRLH WAIEEKAKDD
LSPLNGTLYF DETESQKSVI LHTLKDGMVG EDRRFIIELT AADEVEISPV KGSASVIIRG
DKSISEVGIA SSSRHIIIGE PSATYNGTAI IDLVRGPGVS GEITVNWKIL PPSRGEFVET
SGQLTMLDGQ TAATVVIQVL NDDIPEEKCH YEFQLTEISE GRMLHEASVS ARITMVASDA
PYGRFSFSHE QLHVSKAAQR VNVTVVRSGG SFGRARVLYE TGSRTAEAGW DFVPASGELL
FEAREKMKSL YIDILDDDLP EGPEEFVLAI TRVDLQGRGY DFTIQENGLQ IDQPPEIGNI
SIVRIIIMKN DNAEGIIEFD PKYTDISVEE DAGVITLPVL RLHGTYGHVS ADFSSRGFSA
VPGGYVLRGS SVTFQHGQNL SFINVSIIDD NGSEFEKQFE ILLIGATGGA ILGRHLVSKI
TIAKSDSPFG IIRFLNQSKI SLPNPSSTMA LHLVLERTGG LLGEIQVSWE VVGPDAEEPL
PPHNGDFADP VSGTVSFGDG EGGVRSIILR VCPHEETEAE ETFIVQLKPL REAKLDPRAK
AVTLTIQKFG DPNGVIHFAP ESLSKRRFSE PPPSDGPLLV SFLVTRSKGT SGDIKVHWEL
SSEFDITRDF LSTRGFFTIA DGESDANFDV HLLPDDVPEI EEEYAVQLVS VEGGAELDLG
KCTARFSVSA NDDPHGVFAL YSDRQSVLIG QNLDRSIQIN ITRLAGAFGA VAVRVQILSD
NKEDPVATEN EERQLVITDG ARYKVGLVPL KNQVFLSLGS NFTLQLVSVR LLSGPFYGIP
TILQEAKNAI LSVPEEAANS QVGFESAAFQ LMDIKAGTSQ VMVSRKGTYG RLSVAWTTGY
APGSEIPEPI VIGNMTPTLG SLSFVHGEER KGVLLWTFPS PGRPEAFVLH LSGLRSSAAG
GAQLRSGFTT AEIEPMGVFQ FSPSSRNITV SEDAQTIRIC VQRLFGFHGD LIKVSYETTA
GSAKPPEDFE AVQKGEVFFQ RFQPEIDFEI TIINDQLPEI EETYYINLTS VETRGLGKGG
VNWRPRLNPD LSVAVVTIVD NDDLTGAAVS VPVTAGTVAV DSTLLAMETG STTHPNKSKI
TTIPYTTEVF APVTETVTVS AIPEKLATAH SVISVKPDVV PGTVVASVYG TLSIGPPIVY
VSEEMKNGTL STADILIQRM GGFAGNVTIT VKTFGGRCAQ KEPSVWPFQD VYGVGNLTTW
AVEEEDFEEQ LLTLTFLYGE RERKIAVQIL DDDDAEGQEF FYVFLTDPQG GAEIVRGKDS
TGFSAFAVII ISGSDLHNGI IGFSEESQRG LELREGADKN SQRLVVTRQP NRAFEEVQIF
WRVTLNQTVT ILQEKGANLT DELRFVAGVT TCTGGQTRCF IHLELNPKKV HQVEMPFFVE
LYDVTAGAAI NNSARFAPIK LSKSGAPQSL VSFSVGSRLA VAHKKSTLIS LQVARDSGTG
IMMSVNFITQ ELRSAETVGR VLISPAVSGK DFVRTEGTLV FEPGQKSAVL DVVLTPEAGS
LNKFPKRFQI VLFDPKGGAR IDKVYGTANI TLISDADSQA VWGLEDLLHR PLHEDILNRV
LHNLNLRVAT ESTDEQLSAV MLIMEKITME GRNQAFSIKS RTLLYELLCV LINPKRKDTR
GFSHFVEVAE HFAFSLLTDV TCGSPGEKSK TILDSCPYLS ILALHWNPQQ INGHKFEGKE
GDYIQIPERL LDVPEAEMLD GKNACTLVQF VEYSSQQWFI AGDNLPALKD KVLSLNVKGQ
SAQPLPNNNE VLYRIHAAEP RVVPHTSRCL LWNQAAASWL SDSQFCKVVE DASDYVECAC
SHMSVYAVYA QTDNSSSYNE AFFSAGLICI SGLCLAVVSH MFCARHSMFA AKLLTHMMVA
SLGTQILFLA SAYASPHLSE ESCSAVAAVA HYLYLCQFSW MLIQSVNFWY VLVVSDEHTE
RRCLLFCLLS WGLPSFVVIL LILILRGIYH RSMPQIYGLI HGDLCFIPNI YAALFTAALV
PLMCLVVVFV VFIHAYQLKP QWKGYDDVFR GRTNAAEIPL ILYLFALISM TWLWGGLHMA
YGHFWMLVLF VIFNSLQGLY VFVVYFILHN QTCCPMKASY TVEMNGHPGP STAFFTPGSG
IPPAGEINKS TQNLINAMEE VPSDWERSSF QQTSQASPDL KTSPQNGASF PSSGGYGPGS
LIADEESQEF DDLIFALKTG AGLSVSDNES GQGSQEGGTL TDSQIVELRR IPIADTHL
