ID   OGR1_HUMAN              Reviewed;         365 AA.
AC   Q15743; Q13334; Q4VBB4; Q6IX34;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Ovarian cancer G-protein coupled receptor 1;
DE            Short=OGR-1;
DE   AltName: Full=G-protein coupled receptor 68;
DE   AltName: Full=GPR12A;
DE   AltName: Full=Sphingosylphosphorylcholine receptor;
GN   Name=GPR68; Synonyms=OGR1;
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].
RX   PubMed=7498459; DOI=10.1016/0014-5793(95)01196-l;
RA   An S., Tsai C., Goetzl E.J.;
RT   "Cloning, sequencing and tissue distribution of two related G protein-
RT   coupled receptor candidates expressed prominently in human lung tissue.";
RL   FEBS Lett. 375:121-124(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Ovarian carcinoma;
RX   PubMed=8661159; DOI=10.1006/geno.1996.0377;
RA   Xu Y., Casey G.;
RT   "Identification of human OGR1, a novel G protein-coupled receptor that maps
RT   to chromosome 14.";
RL   Genomics 35:397-402(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Kaighin V.A., Martin A.L., Aronstam R.S.;
RT   "Isolation of cDNA coding for human orphan G protein receptor 68.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RA   King M.M., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   RETRACTED PAPER.
RX   PubMed=10806476; DOI=10.1038/35010529;
RA   Xu Y., Zhu K., Hong G., Wu W., Baudhuin L.M., Xiao Y.-J., Damron D.S.;
RT   "Sphingosylphosphorylcholine is a ligand for ovarian cancer G-protein-
RT   coupled receptor 1.";
RL   Nat. Cell Biol. 2:261-267(2000).
RN   [9]
RP   ERRATUM OF PUBMED:10806476, AND RETRACTION NOTICE OF PUBMED:10806476.
RX   PubMed=16508674; DOI=10.1038/ncb1377;
RA   Xu Y., Zhu K., Hong G., Wu W., Baudhuin L.M., Xiao Y.-J., Damron D.S.;
RL   Nat. Cell Biol. 8:299-299(2006).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-17; HIS-20; HIS-84;
RP   HIS-89; HIS-159; HIS-175; HIS-245 AND HIS-269.
RX   PubMed=12955148; DOI=10.1038/nature01905;
RA   Ludwig M.-G., Vanek M., Guerini D., Gasser J.A., Jones C.E., Junker U.,
RA   Hofstetter H., Wolf R.M., Seuwen K.;
RT   "Proton-sensing G-protein-coupled receptors.";
RL   Nature 425:93-98(2003).
RN   [11]
RP   INVOLVEMENT IN AI2A6, AND VARIANT AI2A6 PRO-74.
RX   PubMed=27693231; DOI=10.1016/j.ajhg.2016.08.020;
RA   Parry D.A., Smith C.E., El-Sayed W., Poulter J.A., Shore R.C., Logan C.V.,
RA   Mogi C., Sato K., Okajima F., Harada A., Zhang H., Koruyucu M., Seymen F.,
RA   Hu J.C., Simmer J.P., Ahmed M., Jafri H., Johnson C.A., Inglehearn C.F.,
RA   Mighell A.J.;
RT   "Mutations in the pH-sensing G-protein-coupled receptor GPR68 cause
RT   amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 99:984-990(2016).
RN   [12]
RP   VARIANT SER-39.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA   Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA   Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA   Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA   Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA   Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA   Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA   Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT   PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Proton-sensing receptor involved in pH homeostasis. May
CC       represents an osteoblastic pH sensor regulating cell-mediated responses
CC       to acidosis in bone. Mediates its action by association with G proteins
CC       that stimulates inositol phosphate (IP) production or Ca(2+)
CC       mobilization. The receptor is almost silent at pH 7.8 but fully
CC       activated at pH 6.8. Also functions as a metastasis suppressor gene in
CC       prostate cancer (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:12955148}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Found at low level in a wide range of tissues, but
CC       significantly expressed in lung, kidney, bone and nervous system.
CC       {ECO:0000269|PubMed:12955148}.
CC   -!- DISEASE: Amelogenesis imperfecta, hypomaturation type, 2A6 (AI2A6)
CC       [MIM:617217]: A defect of enamel formation. The disorder involves both
CC       primary and secondary dentitions. The teeth have a shiny agar jelly
CC       appearance and the enamel is softer than normal. Brown pigment is
CC       present in middle layers of enamel. {ECO:0000269|PubMed:27693231}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: Was originally (PubMed:10806476) thought to be a receptor for
CC       sphingosylphosphorylcholine (SPC). However, this work has been
CC       retracted (PubMed:16508674). {ECO:0000305|PubMed:10806476,
CC       ECO:0000305|PubMed:16508674}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH96072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH96073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH96074.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH98567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAT38917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACG60649.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAW81447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/40745/GPR68";
CC   ---------------------------------------------------------------------------
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DR   EMBL; U35398; AAA79060.1; -; mRNA.
DR   EMBL; U48405; AAC50596.1; -; Genomic_DNA.
DR   EMBL; EU883575; ACG60649.1; ALT_INIT; mRNA.
DR   EMBL; AY615372; AAT38917.1; ALT_INIT; mRNA.
DR   EMBL; AL135818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81447.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC067472; AAH67472.1; -; mRNA.
DR   EMBL; BC069592; AAH69592.1; -; mRNA.
DR   EMBL; BC096071; AAH96071.1; ALT_INIT; mRNA.
DR   EMBL; BC096072; AAH96072.1; ALT_INIT; mRNA.
DR   EMBL; BC096073; AAH96073.1; ALT_INIT; mRNA.
DR   EMBL; BC096074; AAH96074.1; ALT_INIT; mRNA.
DR   EMBL; BC098567; AAH98567.1; ALT_INIT; mRNA.
DR   CCDS; CCDS9894.2; -.
DR   PIR; S68208; S68208.
DR   RefSeq; NP_001171147.1; NM_001177676.1.
DR   RefSeq; NP_001335366.1; NM_001348437.1.
DR   RefSeq; NP_003476.3; NM_003485.3.
DR   RefSeq; XP_005268167.1; XM_005268110.4.
DR   RefSeq; XP_005268168.1; XM_005268111.3.
DR   RefSeq; XP_005268169.1; XM_005268112.3.
DR   RefSeq; XP_006720325.1; XM_006720262.3.
DR   RefSeq; XP_011535498.1; XM_011537196.2.
DR   RefSeq; XP_011535499.1; XM_011537197.2.
DR   RefSeq; XP_011535500.1; XM_011537198.2.
DR   RefSeq; XP_011535501.1; XM_011537199.2.
DR   AlphaFoldDB; Q15743; -.
DR   SMR; Q15743; -.
DR   STRING; 9606.ENSP00000498702; -.
DR   BindingDB; Q15743; -.
DR   ChEMBL; CHEMBL3713916; -.
DR   GuidetoPHARMACOLOGY; 114; -.
DR   GlyCosmos; Q15743; 2 sites, No reported glycans.
DR   GlyGen; Q15743; 2 sites.
DR   iPTMnet; Q15743; -.
DR   PhosphoSitePlus; Q15743; -.
DR   SwissPalm; Q15743; -.
DR   BioMuta; GPR68; -.
DR   DMDM; 3024266; -.
DR   jPOST; Q15743; -.
DR   MassIVE; Q15743; -.
DR   PaxDb; 9606-ENSP00000434045; -.
DR   PeptideAtlas; Q15743; -.
DR   ProteomicsDB; 60731; -.
DR   ABCD; Q15743; 3 sequenced antibodies.
DR   Antibodypedia; 13584; 336 antibodies from 30 providers.
DR   DNASU; 8111; -.
DR   Ensembl; ENST00000531499.2; ENSP00000434045.2; ENSG00000119714.11.
DR   Ensembl; ENST00000535815.5; ENSP00000440797.1; ENSG00000119714.11.
DR   Ensembl; ENST00000650645.1; ENSP00000498702.1; ENSG00000119714.11.
DR   GeneID; 8111; -.
DR   KEGG; hsa:8111; -.
DR   MANE-Select; ENST00000650645.1; ENSP00000498702.1; NM_001177676.2; NP_001171147.1.
DR   UCSC; uc001xzg.4; human.
DR   AGR; HGNC:4519; -.
DR   CTD; 8111; -.
DR   DisGeNET; 8111; -.
DR   GeneCards; GPR68; -.
DR   HGNC; HGNC:4519; GPR68.
DR   HPA; ENSG00000119714; Tissue enhanced (pituitary).
DR   MalaCards; GPR68; -.
DR   MIM; 601404; gene.
DR   MIM; 617217; phenotype.
DR   neXtProt; NX_Q15743; -.
DR   OpenTargets; ENSG00000119714; -.
DR   Orphanet; 100033; Hypomaturation amelogenesis imperfecta.
DR   PharmGKB; PA28911; -.
DR   VEuPathDB; HostDB:ENSG00000119714; -.
DR   eggNOG; ENOG502QQJA; Eukaryota.
DR   GeneTree; ENSGT00950000183136; -.
DR   InParanoid; Q15743; -.
DR   OMA; TCCFVFT; -.
DR   OrthoDB; 2906444at2759; -.
DR   PhylomeDB; Q15743; -.
DR   TreeFam; TF331803; -.
DR   PathwayCommons; Q15743; -.
DR   Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 8111; 16 hits in 1153 CRISPR screens.
DR   ChiTaRS; GPR68; human.
DR   GeneWiki; GPR68; -.
DR   GenomeRNAi; 8111; -.
DR   Pharos; Q15743; Tchem.
DR   PRO; PR:Q15743; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q15743; Protein.
DR   Bgee; ENSG00000119714; Expressed in tendon of biceps brachii and 148 other cell types or tissues.
DR   ExpressionAtlas; Q15743; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
DR   CDD; cd15367; 7tmA_GPR68_OGR1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR005389; OGR1_rcpt.
DR   PANTHER; PTHR24234; LYSOPHOSPHATIDIC ACID RECEPTOR 5/SPHINGOSYLPHOSPHORYLCHOLINE RECEPTOR; 1.
DR   PANTHER; PTHR24234:SF5; OVARIAN CANCER G-PROTEIN COUPLED RECEPTOR 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01564; OGR1RECEPTOR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q15743; HS.
PE   1: Evidence at protein level;
KW   Amelogenesis imperfecta; Cell membrane; Disease variant; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix;
KW   Tumor suppressor.
FT   CHAIN           1..365
FT                   /note="Ovarian cancer G-protein coupled receptor 1"
FT                   /id="PRO_0000070113"
FT   TOPO_DOM        1..21
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..46
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..80
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..117
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..158
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..183
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..205
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          345..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         39
FT                   /note="N -> S (found in a renal cell carcinoma case;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064716"
FT   VARIANT         53
FT                   /note="R -> Q (in dbSNP:rs2230339)"
FT                   /id="VAR_058714"
FT   VARIANT         74
FT                   /note="L -> P (in AI2A6; dbSNP:rs1057517672)"
FT                   /evidence="ECO:0000269|PubMed:27693231"
FT                   /id="VAR_077874"
FT   MUTAGEN         17
FT                   /note="H->F: Failed to stimulate IP formation at pH 6.8,
FT                   activity is restored at more acid pH."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         20
FT                   /note="H->F: Failed to stimulate IP formation at pH 6.8,
FT                   activity is restored at more acid pH."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         84
FT                   /note="H->F: Failed to stimulate IP formation at pH 6.8,
FT                   activity is restored at more acid pH."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         89
FT                   /note="H->F: No effect on pH-sensing activity."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         159
FT                   /note="H->F: No effect on pH-sensing activity."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         169
FT                   /note="H->F: Failed to stimulate IP formation at pH 6.8,
FT                   activity is restored at more acid pH."
FT   MUTAGEN         175
FT                   /note="H->F: No effect on pH-sensing activity."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         245
FT                   /note="H->F: Severe loss pH-sensing activity."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   MUTAGEN         269
FT                   /note="H->F: Failed to stimulate IP formation at pH 6.8,
FT                   activity is restored at more acid pH."
FT                   /evidence="ECO:0000269|PubMed:12955148"
FT   CONFLICT        140..142
FT                   /note="GVS -> RVT (in Ref. 1; AAA79060)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   365 AA;  41077 MW;  05919AFD5B842CCD CRC64;
     MGNITADNSS MSCTIDHTIH QTLAPVVYVT VLVVGFPANC LSLYFGYLQI KARNELGVYL
     CNLTVADLFY ICSLPFWLQY VLQHDNWSHG DLSCQVCGIL LYENIYISVG FLCCISVDRY
     LAVAHPFRFH QFRTLKAAVG VSVVIWAKEL LTSIYFLMHE EVIEDENQHR VCFEHYPIQA
     WQRAINYYRF LVGFLFPICL LLASYQGILR AVRRSHGTQK SRKDQIQRLV LSTVVIFLAC
     FLPYHVLLLV RSVWEASCDF AKGVFNAYHF SLLLTSFNCV ADPVLYCFVS ETTHRDLARL
     RGACLAFLTC SRTGRAREAY PLGAPEASGK SGAQGEEPEL LTKLHPAFQT PNSPGSGGFP
     TGRLA
//