PF2R_HUMAN
ID PF2R_HUMAN Reviewed; 359 AA.
AC P43088; A8K9Y0; Q2KHP3; Q6RYQ6; Q9P1X4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Prostaglandin F2-alpha receptor;
DE Short=PGF receptor;
DE Short=PGF2-alpha receptor;
DE AltName: Full=Prostanoid FP receptor;
GN Name=PTGFR;
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 1).
RC TISSUE=Uterus;
RX PubMed=8300593; DOI=10.1016/s0021-9258(17)41991-0;
RA Abramovitz M., Boie Y., Nguyen T., Rushmore T.H., Bayne M.A., Metters K.M.,
RA Slipetz D.M., Grygorczyk R.;
RT "Cloning and expression of a cDNA for the human prostanoid FP receptor.";
RL J. Biol. Chem. 269:2632-2636(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ocular ciliary body;
RX PubMed=9341156; DOI=10.1074/jbc.272.43.27147;
RA Kunapuli P., Lawson J.A., Rokach J., FitzGerald G.A.;
RT "Functional characterization of the ocular prostaglandin f2alpha
RT (PGF2alpha) receptor. Activation by the isoprostane, 12-iso-PGF2alpha.";
RL J. Biol. Chem. 272:27147-27154(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Kopatz S.A., 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 (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=14984197; DOI=10.1016/j.abb.2003.10.021;
RA Vielhauer G.A., Fujino H., Regan J.W.;
RT "Cloning and localization of hFP(S): a six-transmembrane mRNA splice
RT variant of the human FP prostanoid receptor.";
RL Arch. Biochem. Biophys. 421:175-185(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266.
RC TISSUE=Liver;
RA Nishizawa M., Ito S.;
RT "Structure of human prostaglandin F2alpha receptor gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND SUBUNIT.
RX PubMed=18587449; DOI=10.1038/bjp.2008.142;
RA Liang Y., Woodward D.F., Guzman V.M., Li C., Scott D.F., Wang J.W.,
RA Wheeler L.A., Garst M.E., Landsverk K., Sachs G., Krauss A.H., Cornell C.,
RA Martos J., Pettit S., Fliri H.;
RT "Identification and pharmacological characterization of the prostaglandin
RT FP receptor and FP receptor variant complexes.";
RL Br. J. Pharmacol. 154:1079-1093(2008).
CC -!- FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The
CC activity of this receptor is mediated by G proteins which activate a
CC phosphatidylinositol-calcium second messenger system. Initiates
CC luteolysis in the corpus luteum (By similarity). Isoforms 2 to 7 do not
CC bind PGF2-alpha but are proposed to modulate signaling by participating
CC in variant receptor complexes; heterodimers between isoform 1 and
CC isoform 5 are proposed to be a receptor for prostamides including the
CC synthetic analog bimatoprost. {ECO:0000250,
CC ECO:0000269|PubMed:18587449}.
CC -!- SUBUNIT: Isoform 1 can form heterodimers with isoform 5 (and probably
CC other isoforms). {ECO:0000269|PubMed:18587449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=P43088-1; Sequence=Displayed;
CC Name=2; Synonyms=FP(S), VAR-1;
CC IsoId=P43088-2; Sequence=VSP_042025;
CC Name=3; Synonyms=VAR-2;
CC IsoId=P43088-3; Sequence=VSP_053589, VSP_053595;
CC Name=4; Synonyms=VAR-3;
CC IsoId=P43088-4; Sequence=VSP_053588, VSP_053596;
CC Name=5; Synonyms=altFP4, VAR-4;
CC IsoId=P43088-5; Sequence=VSP_053593, VSP_053597;
CC Name=6; Synonyms=VAR-5;
CC IsoId=P43088-6; Sequence=VSP_053591, VSP_053592;
CC Name=7; Synonyms=VAR-6;
CC IsoId=P43088-7; Sequence=VSP_053590, VSP_053594;
CC -!- TISSUE SPECIFICITY: Eye. {ECO:0000269|PubMed:18587449}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L24470; AAA17684.1; -; mRNA.
DR EMBL; AF004021; AAB63152.1; -; mRNA.
DR EMBL; AY337000; AAQ76788.1; -; mRNA.
DR EMBL; AY485530; AAR84381.1; -; mRNA.
DR EMBL; AK292845; BAF85534.1; -; mRNA.
DR EMBL; AC096531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06351.1; -; Genomic_DNA.
DR EMBL; BC112965; AAI12966.1; -; mRNA.
DR EMBL; AB041713; BAA94756.1; -; Genomic_DNA.
DR CCDS; CCDS30759.1; -. [P43088-2]
DR CCDS; CCDS686.1; -. [P43088-1]
DR PIR; A49973; A49973.
DR RefSeq; NP_000950.1; NM_000959.3. [P43088-1]
DR RefSeq; NP_001034674.1; NM_001039585.1. [P43088-2]
DR RefSeq; XP_016857362.1; XM_017001873.1. [P43088-4]
DR AlphaFoldDB; P43088; -.
DR SMR; P43088; -.
DR BioGRID; 111709; 19.
DR IntAct; P43088; 9.
DR STRING; 9606.ENSP00000359793; -.
DR BindingDB; P43088; -.
DR ChEMBL; CHEMBL1987; -.
DR DrugBank; DB00905; Bimatoprost.
DR DrugBank; DB01160; Dinoprost tromethamine.
DR DrugBank; DB00654; Latanoprost.
DR DrugBank; DB11660; Latanoprostene bunod.
DR DrugBank; DB08819; Tafluprost.
DR DrugBank; DB00287; Travoprost.
DR DrugCentral; P43088; -.
DR GuidetoPHARMACOLOGY; 344; -.
DR SwissLipids; SLP:000001573; -.
DR GlyGen; P43088; 2 sites.
DR iPTMnet; P43088; -.
DR PhosphoSitePlus; P43088; -.
DR BioMuta; PTGFR; -.
DR DMDM; 1172442; -.
DR MassIVE; P43088; -.
DR PaxDb; P43088; -.
DR PeptideAtlas; P43088; -.
DR PRIDE; P43088; -.
DR ProteomicsDB; 55578; -. [P43088-1]
DR Antibodypedia; 19743; 190 antibodies from 27 providers.
DR DNASU; 5737; -.
DR Ensembl; ENST00000370756.3; ENSP00000359792.3; ENSG00000122420.10. [P43088-2]
DR Ensembl; ENST00000370757.8; ENSP00000359793.3; ENSG00000122420.10. [P43088-1]
DR Ensembl; ENST00000370758.5; ENSP00000359794.1; ENSG00000122420.10. [P43088-1]
DR GeneID; 5737; -.
DR KEGG; hsa:5737; -.
DR MANE-Select; ENST00000370757.8; ENSP00000359793.3; NM_000959.4; NP_000950.1.
DR UCSC; uc001dim.4; human. [P43088-1]
DR CTD; 5737; -.
DR DisGeNET; 5737; -.
DR GeneCards; PTGFR; -.
DR HGNC; HGNC:9600; PTGFR.
DR HPA; ENSG00000122420; Tissue enhanced (tongue).
DR MIM; 600563; gene.
DR neXtProt; NX_P43088; -.
DR OpenTargets; ENSG00000122420; -.
DR PharmGKB; PA290; -.
DR VEuPathDB; HostDB:ENSG00000122420; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P43088; -.
DR OMA; HIEMICQ; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43088; -.
DR TreeFam; TF324982; -.
DR PathwayCommons; P43088; -.
DR Reactome; R-HSA-391908; Prostanoid ligand receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P43088; -.
DR SIGNOR; P43088; -.
DR BioGRID-ORCS; 5737; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; PTGFR; human.
DR GeneWiki; Prostaglandin_F_receptor; -.
DR GenomeRNAi; 5737; -.
DR Pharos; P43088; Tclin.
DR PRO; PR:P43088; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P43088; protein.
DR Bgee; ENSG00000122420; Expressed in calcaneal tendon and 135 other tissues.
DR ExpressionAtlas; P43088; baseline and differential.
DR Genevisible; P43088; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004958; F:prostaglandin F receptor activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:UniProtKB.
DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0007567; P:parturition; TAS:ProtInc.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000141; PglndnF_rcpt.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR PANTHER; PTHR11866:SF4; PTHR11866:SF4; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00855; PRSTNOIDFPR.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Prostaglandin F2-alpha receptor"
FT /id="PRO_0000070070"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 267..359
FT /note="VTMANIGINGNHSLETCETTLFALRMATWNQILDPWVYILLRKAVLKNLYKL
FT ASQCCGVHVISLHIWELSSIKNSLKVAAISESPVAEKSAST -> GYRIILNGKEKYKV
FT YEEQSDFLHRLQWPTLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14984197"
FT /id="VSP_042025"
FT VAR_SEQ 267..291
FT /note="VTMANIGINGNHSLETCETTLFALR -> GYRIILNGKEKYKVYEEQSDFLH
FT RK (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_053588"
FT VAR_SEQ 267..275
FT /note="VTMANIGIN -> KIEGKIKVT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053589"
FT VAR_SEQ 267..274
FT /note="VTMANIGI -> THWGKEIP (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_053590"
FT VAR_SEQ 267
FT /note="V -> R (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_053591"
FT VAR_SEQ 268..359
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_053592"
FT VAR_SEQ 268..296
FT /note="TMANIGINGNHSLETCETTLFALRMATWN -> KETHLQMRLWTWDFRVNAL
FT EDYCEGLTVF (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_053593"
FT VAR_SEQ 275..359
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_053594"
FT VAR_SEQ 276..359
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053595"
FT VAR_SEQ 292..359
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_053596"
FT VAR_SEQ 297..359
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_053597"
SQ SEQUENCE 359 AA; 40055 MW; 08077045C0B20BCA CRC64;
MSMNNSKQLV SPAAALLSNT TCQTENRLSV FFSVIFMTVG ILSNSLAIAI LMKAYQRFRQ
KSKASFLLLA SGLVITDFFG HLINGAIAVF VYASDKEWIR FDQSNVLCSI FGICMVFSGL
CPLLLGSVMA IERCIGVTKP IFHSTKITSK HVKMMLSGVC LFAVFIALLP ILGHRDYKIQ
ASRTWCFYNT EDIKDWEDRF YLLLFSFLGL LALGVSLLCN AITGITLLRV KFKSQQHRQG
RSHHLEMVIQ LLAIMCVSCI CWSPFLVTMA NIGINGNHSL ETCETTLFAL RMATWNQILD
PWVYILLRKA VLKNLYKLAS QCCGVHVISL HIWELSSIKN SLKVAAISES PVAEKSAST
