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   27-MAR-2024, entry version 195.
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   PDB; 8IUK; EM; 2.67 A; R=1-359.
DR   PDB; 8IUL; EM; 2.78 A; R=1-359.
DR   PDB; 8IUM; EM; 3.14 A; R=1-359.
DR   PDBsum; 8IUK; -.
DR   PDBsum; 8IUL; -.
DR   PDBsum; 8IUM; -.
DR   AlphaFoldDB; P43088; -.
DR   EMDB; EMD-35724; -.
DR   EMDB; EMD-35725; -.
DR   EMDB; EMD-35726; -.
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   GlyCosmos; P43088; 2 sites, No reported glycans.
DR   GlyGen; P43088; 2 sites.
DR   iPTMnet; P43088; -.
DR   PhosphoSitePlus; P43088; -.
DR   SwissPalm; P43088; -.
DR   BioMuta; PTGFR; -.
DR   DMDM; 1172442; -.
DR   MassIVE; P43088; -.
DR   PaxDb; 9606-ENSP00000359793; -.
DR   PeptideAtlas; P43088; -.
DR   ProteomicsDB; 55578; -. [P43088-1]
DR   Antibodypedia; 19743; 222 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   AGR; HGNC:9600; -.
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; TSYHIEM; -.
DR   OrthoDB; 5355693at2759; -.
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; 13 hits in 1156 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 137 other cell types or tissues.
DR   ExpressionAtlas; P43088; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
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   CDD; cd15145; 7tmA_FP; 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; IPR000141; PglndnF_rcpt.
DR   InterPro; IPR008365; Prostanoid_rcpt.
DR   PANTHER; PTHR11866; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1.
DR   PANTHER; PTHR11866:SF4; PROSTAGLANDIN F2-ALPHA RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00855; PRSTNOIDFPR.
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; P43088; HS.
PE   1: Evidence at protein level;
KW   3D-structure; 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"
FT   HELIX           31..58
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           65..92
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   TURN            93..96
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           107..138
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           140..144
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           149..167
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           196..233
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           245..275
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           283..298
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           300..304
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:8IUK"
FT   HELIX           309..322
FT                   /evidence="ECO:0007829|PDB:8IUK"
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
//