GPR4_HUMAN
ID GPR4_HUMAN Reviewed; 362 AA.
AC P46093; A8K3T3; B0M0K1; Q6NWM4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=G-protein coupled receptor 4;
DE AltName: Full=G-protein coupled receptor 6C.l {ECO:0000303|PubMed:7498459};
DE Short=GPR6C.l {ECO:0000303|PubMed:7498459};
GN Name=GPR4;
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 [GENOMIC DNA].
RX PubMed=7832990; DOI=10.1089/dna.1995.14.25;
RA Heiber M., Docherty J.M., Shah G., Nguyen T., Cheng R., Heng H.H.Q.,
RA Marchese A., Tsui L.-C., Shi X., George S.R., O'Dowd B.F.;
RT "Isolation of three novel human genes encoding G protein-coupled
RT receptors.";
RL DNA Cell Biol. 14:25-35(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8595909; DOI=10.1006/geno.1995.0013;
RA Mahadevan M.S., Baird S., Bailly J.E., Shutler G.G., Sabourin L.A.,
RA Tsilfidis C., Neville C.E., Narang M., Korneluk R.G.;
RT "Isolation of a novel G protein-coupled receptor (GPR4) localized to
RT chromosome 19q13.3.";
RL Genomics 30:84-88(1995).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
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 [8]
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 [9]
RP RETRACTED PAPER.
RX PubMed=11535583; DOI=10.1074/jbc.m008057200;
RA Zhu K., Baudhuin L.M., Hong G., Williams F.S., Cristina K.L.,
RA Kabarowski J.H., Witte O.N., Xu Y.;
RT "Sphingosylphosphorylcholine and lysophosphatidylcholine are ligands for
RT the G protein-coupled receptor GPR4.";
RL J. Biol. Chem. 276:41325-41335(2001).
RN [10]
RP RETRACTION NOTICE OF PUBMED:11535583.
RX PubMed=16498716;
RA Zhu K., Baudhuin L.M., Hong G., Williams F.S., Cristina K.L.,
RA Kabarowski J.H., Witte O.N., Xu Y.;
RL J. Biol. Chem. 280:43280-43280(2005).
RN [11]
RP FUNCTION.
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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17462861; DOI=10.1016/j.cellsig.2007.03.009;
RA Tobo M., Tomura H., Mogi C., Wang J.Q., Liu J.P., Komachi M., Damirin A.,
RA Kimura T., Murata N., Kurose H., Sato K., Okajima F.;
RT "Previously postulated 'ligand-independent' signaling of GPR4 is mediated
RT through proton-sensing mechanisms.";
RL Cell. Signal. 19:1745-1753(2007).
RN [13]
RP MUTAGENESIS OF HIS-4; HIS-10; HIS-17; HIS-79; HIS-80; HIS-85; HIS-165 AND
RP HIS-269, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20211729; DOI=10.1016/j.phrs.2010.02.013;
RA Liu J.P., Nakakura T., Tomura H., Tobo M., Mogi C., Wang J.Q., He X.D.,
RA Takano M., Damirin A., Komachi M., Sato K., Okajima F.;
RT "Each one of certain histidine residues in G-protein-coupled receptor GPR4
RT is critical for extracellular proton-induced stimulation of multiple G-
RT protein-signaling pathways.";
RL Pharmacol. Res. 61:499-505(2010).
RN [14]
RP MUTAGENESIS OF ARG-115, AND FUNCTION.
RX PubMed=22110680; DOI=10.1371/journal.pone.0027586;
RA Chen A., Dong L., Leffler N.R., Asch A.S., Witte O.N., Yang L.V.;
RT "Activation of GPR4 by acidosis increases endothelial cell adhesion through
RT the cAMP/Epac pathway.";
RL PLoS ONE 6:e27586-e27586(2011).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ARG-115.
RX PubMed=32058960; DOI=10.1016/j.isci.2020.100848;
RA Krewson E.A., Sanderlin E.J., Marie M.A., Akhtar S.N., Velcicky J.,
RA Loetscher P., Yang L.V.;
RT "The Proton-Sensing GPR4 Receptor Regulates Paracellular Gap Formation and
RT Permeability of Vascular Endothelial Cells.";
RL IScience 23:100848-100848(2020).
CC -!- FUNCTION: Proton-sensing G-protein coupled receptor couples to multiple
CC intracellular signaling pathways, including GNAS/cAMP,
CC GNAQ/phospholipase C (PLC), and GNA12/GNA13/Rho pathways
CC (PubMed:12955148, PubMed:17462861, PubMed:22110680, PubMed:20211729).
CC Acidosis-induced GPR4 activation increases paracellular gap formation
CC and permeability of vascular endothelial cells through the
CC GNA12/GNA13/Rho GTPase signaling pathway (PubMed:32058960). In the
CC brain may mediate central respiratory sensitivity to CO(2)H(+) (By
CC similarity). {ECO:0000250|UniProtKB:Q8BUD0,
CC ECO:0000269|PubMed:12955148, ECO:0000269|PubMed:17462861,
CC ECO:0000269|PubMed:20211729, ECO:0000269|PubMed:22110680,
CC ECO:0000269|PubMed:32058960}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17462861,
CC ECO:0000269|PubMed:20211729}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be a receptor for
CC sphingosylphosphorylcholine and lysophosphatidylcholine
CC (PubMed:11535583). However, this work has been retracted.
CC {ECO:0000269|PubMed:11535583, ECO:0000305|PubMed:16498716}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63180.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L36148; AAA63180.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U21051; AAA98457.1; -; Genomic_DNA.
DR EMBL; U35399; AAA79061.1; -; mRNA.
DR EMBL; EU432116; ABY87915.1; -; mRNA.
DR EMBL; AK290698; BAF83387.1; -; mRNA.
DR EMBL; AC011480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57368.1; -; Genomic_DNA.
DR EMBL; BC067535; AAH67535.1; -; mRNA.
DR EMBL; BC067536; AAH67536.1; -; mRNA.
DR CCDS; CCDS12669.1; -.
DR PIR; A57641; A57641.
DR PIR; I53033; I53033.
DR PIR; S68207; S68207.
DR RefSeq; NP_005273.1; NM_005282.2.
DR RefSeq; XP_016882096.1; XM_017026607.1.
DR RefSeq; XP_016882097.1; XM_017026608.1.
DR AlphaFoldDB; P46093; -.
DR SMR; P46093; -.
DR STRING; 9606.ENSP00000319744; -.
DR BindingDB; P46093; -.
DR ChEMBL; CHEMBL3638324; -.
DR GuidetoPHARMACOLOGY; 84; -.
DR GlyGen; P46093; 2 sites.
DR iPTMnet; P46093; -.
DR PhosphoSitePlus; P46093; -.
DR BioMuta; GPR4; -.
DR DMDM; 1708027; -.
DR EPD; P46093; -.
DR PaxDb; P46093; -.
DR PeptideAtlas; P46093; -.
DR PRIDE; P46093; -.
DR ProteomicsDB; 55719; -.
DR Antibodypedia; 2958; 211 antibodies from 30 providers.
DR DNASU; 2828; -.
DR Ensembl; ENST00000323040.5; ENSP00000319744.3; ENSG00000177464.5.
DR GeneID; 2828; -.
DR KEGG; hsa:2828; -.
DR MANE-Select; ENST00000323040.5; ENSP00000319744.3; NM_005282.3; NP_005273.1.
DR UCSC; uc002pcm.4; human.
DR CTD; 2828; -.
DR DisGeNET; 2828; -.
DR GeneCards; GPR4; -.
DR HGNC; HGNC:4497; GPR4.
DR HPA; ENSG00000177464; Tissue enhanced (adipose tissue, lung).
DR MIM; 600551; gene.
DR neXtProt; NX_P46093; -.
DR OpenTargets; ENSG00000177464; -.
DR PharmGKB; PA28886; -.
DR VEuPathDB; HostDB:ENSG00000177464; -.
DR eggNOG; ENOG502QS9G; Eukaryota.
DR GeneTree; ENSGT01050000244810; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P46093; -.
DR OMA; RTWEGCH; -.
DR OrthoDB; 716326at2759; -.
DR PhylomeDB; P46093; -.
DR TreeFam; TF331803; -.
DR PathwayCommons; P46093; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 2828; 7 hits in 1065 CRISPR screens.
DR GeneWiki; GPR4; -.
DR GenomeRNAi; 2828; -.
DR Pharos; P46093; Tchem.
DR PRO; PR:P46093; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P46093; protein.
DR Bgee; ENSG00000177464; Expressed in omental fat pad and 140 other tissues.
DR Genevisible; P46093; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0043114; P:regulation of vascular permeability; ISS:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IDA:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002276; GPR4_orph.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01147; GPR4RECEPTOR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..362
FT /note="G-protein coupled receptor 4"
FT /id="PRO_0000069512"
FT TOPO_DOM 1..17
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..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..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 295
FT /note="S -> N (in dbSNP:rs36012326)"
FT /id="VAR_049390"
FT MUTAGEN 4
FT /note="H->Y: No effect on pH-sensing activity."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 10
FT /note="H->Y: No effect on pH-sensing activity."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 17
FT /note="H->Y: No effect on pH-sensing activity."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 79
FT /note="H->Y: Displays smaller cAMP, rho, PLC responses to
FT mildly alkaline to acidic pH of 7.1 but almost the same or
FT higher responses to severely acidic pH values of 6.5-6.2."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 80
FT /note="H->Y: No effect on pH-sensing activity."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 85
FT /note="H->Y: No effect on pH-sensing activity."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 115
FT /note="R->A: Signaling-defective mutant. Endothelial
FT permeability is decreased under acid conditions."
FT /evidence="ECO:0000269|PubMed:22110680,
FT ECO:0000269|PubMed:32058960"
FT MUTAGEN 165
FT /note="H->Y: Displays smaller cAMP, rho, PLC responses to
FT mildly alkaline to acidic pH of 7.1 but almost the same or
FT higher responses to severely acidic pH values of 6.5-6.2."
FT /evidence="ECO:0000269|PubMed:20211729"
FT MUTAGEN 269
FT /note="H->Y: Displays smaller cAMP, rho, PLC responses to
FT mildly alkaline to acidic pH of 7.1 but almost the same or
FT higher responses to severely acidic pH values of 6.5-6.2."
FT /evidence="ECO:0000269|PubMed:20211729"
FT CONFLICT 57
FT /note="M -> L (in Ref. 3; AAA79061)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="T -> S (in Ref. 3; AAA79061)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="R -> C (in Ref. 8; AAH67535)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="P -> L (in Ref. 5; BAF83387)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> V (in Ref. 3; AAA79061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40982 MW; 6C75D97C36204541 CRC64;
MGNHTWEGCH VDSRVDHLFP PSLYIFVIGV GLPTNCLALW AAYRQVQQRN ELGVYLMNLS
IADLLYICTL PLWVDYFLHH DNWIHGPGSC KLFGFIFYTN IYISIAFLCC ISVDRYLAVA
HPLRFARLRR VKTAVAVSSV VWATELGANS APLFHDELFR DRYNHTFCFE KFPMEGWVAW
MNLYRVFVGF LFPWALMLLS YRGILRAVRG SVSTERQEKA KIKRLALSLI AIVLVCFAPY
HVLLLSRSAI YLGRPWDCGF EERVFSAYHS SLAFTSLNCV ADPILYCLVN EGARSDVAKA
LHNLLRFLAS DKPQEMANAS LTLETPLTSK RNSTAKAMTG SWAATPPSQG DQVQLKMLPP
AQ
