PTAFR_HUMAN
ID PTAFR_HUMAN Reviewed; 342 AA.
AC P25105; A3KMC8; A8K2H5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Platelet-activating factor receptor;
DE Short=PAF-R;
DE Short=PAFr;
GN Name=PTAFR; Synonyms=PAFR;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Granulocyte;
RX PubMed=1656963; DOI=10.1016/s0006-291x(05)81261-6;
RA Ye R.D., Prossnitz E.R., Zou A., Cochrane C.G.;
RT "Characterization of a human cDNA that encodes a functional receptor for
RT platelet activating factor.";
RL Biochem. Biophys. Res. Commun. 180:105-111(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Leukocyte;
RX PubMed=1657923; DOI=10.1016/s0021-9258(18)54936-x;
RA Nakamura M., Honda Z., Izumi T., Sakanaka C., Mutoh H., Minami M., Bito H.,
RA Seyama Y., Matsumoto T., Noma M., Shimizu T.;
RT "Molecular cloning and expression of platelet-activating factor receptor
RT from human leukocytes.";
RL J. Biol. Chem. 266:20400-20405(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Leukocyte;
RX PubMed=1374385; DOI=10.1016/s0021-9258(19)50394-5;
RA Kunz D., Gerard N.P., Gerard C.;
RT "The human leukocyte platelet-activating factor receptor. cDNA cloning,
RT cell surface expression, and construction of a novel epitope-bearing
RT analog.";
RL J. Biol. Chem. 267:9101-9106(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Fetal liver;
RX PubMed=1322356; DOI=10.1016/0888-7543(92)90162-l;
RA Seyfried C.E., Schweickart V.L., Godiska R., Gray P.W.;
RT "The human platelet-activating factor receptor gene (PTAFR) contains no
RT introns and maps to chromosome 1.";
RL Genomics 13:832-834(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart ventricle;
RX PubMed=1281995; DOI=10.1016/0006-291x(92)92245-s;
RA Sugimoto T., Tsuchimochi H., McGregor C.G.A., Mutoh H., Shimizu T.,
RA Kurachi Y.;
RT "Molecular cloning and characterization of the platelet-activating factor
RT receptor gene expressed in the human heart.";
RL Biochem. Biophys. Res. Commun. 189:617-624(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RA Behal R.H., Debuysere M.S., Olson M.S.;
RT "Nucleotide sequence of platelet-activating-factor receptor derived from
RT HeLa cell genomic DNA and Rhesus monkey genomic DNA.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383507; DOI=10.1165/ajrcmb/8.3.240;
RA Chase P.B., Halonen M., Regan J.W.;
RT "Cloning of a human platelet-activating factor receptor gene: evidence for
RT an intron in the 5'-untranslated region.";
RL Am. J. Respir. Cell Mol. Biol. 8:240-244(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RA Warren C.N., 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-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [11]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lymph;
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 [13]
RP INTERACTION WITH ARRB1.
RX PubMed=16709866; DOI=10.4049/jimmunol.176.11.7039;
RA McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., Hamiel C.,
RA Sheppard F.R., Moore E.E., Silliman C.C.;
RT "Platelet-activating factor-induced clathrin-mediated endocytosis requires
RT beta-arrestin-1 recruitment and activation of the p38 MAPK signalosome at
RT the plasma membrane for actin bundle formation.";
RL J. Immunol. 176:7039-7050(2006).
RN [14]
RP VARIANTS ASP-224 AND SER-338.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [15]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: Receptor for platelet activating factor, a chemotactic
CC phospholipid mediator that possesses potent inflammatory, smooth-muscle
CC contractile and hypotensive activity. Seems to mediate its action via a
CC G protein that activates a phosphatidylinositol-calcium second
CC messenger system. {ECO:0000269|PubMed:1281995,
CC ECO:0000269|PubMed:1374385, ECO:0000269|PubMed:1656963,
CC ECO:0000269|PubMed:1657923}.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000269|PubMed:16709866}.
CC -!- INTERACTION:
CC P25105; Q05397: PTK2; NbExp=2; IntAct=EBI-3906092, EBI-702142;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1374385};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1374385}.
CC -!- TISSUE SPECIFICITY: Expressed in the placenta, lung, left and right
CC heart ventricles, heart atrium, leukocytes and differentiated HL-60
CC granulocytes. {ECO:0000269|PubMed:1281995, ECO:0000269|PubMed:1656963,
CC ECO:0000269|PubMed:1657923}.
CC -!- INDUCTION: By CSF2/GM-CSF, IL5/interleukin-5 and n-butyrate.
CC {ECO:0000269|PubMed:1657923}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M80436; AAA60001.1; -; mRNA.
DR EMBL; D10202; BAA01050.1; -; mRNA.
DR EMBL; M76674; AAA60002.1; -; mRNA.
DR EMBL; M88177; AAA60214.1; -; Genomic_DNA.
DR EMBL; S52624; AAB24695.2; -; mRNA.
DR EMBL; L07334; AAA60108.1; -; mRNA.
DR EMBL; S56396; AAB25755.1; -; Genomic_DNA.
DR EMBL; AY275466; AAP32298.1; -; mRNA.
DR EMBL; BT009801; AAP88803.1; -; mRNA.
DR EMBL; AK290240; BAF82929.1; -; mRNA.
DR EMBL; CH471059; EAX07711.1; -; Genomic_DNA.
DR EMBL; BC013816; AAH13816.1; -; mRNA.
DR EMBL; BC063000; AAH63000.1; -; mRNA.
DR CCDS; CCDS318.1; -.
DR PIR; A40191; A40191.
DR RefSeq; NP_000943.1; NM_000952.4.
DR RefSeq; NP_001158193.1; NM_001164721.1.
DR RefSeq; NP_001158194.1; NM_001164722.2.
DR RefSeq; NP_001158195.1; NM_001164723.2.
DR AlphaFoldDB; P25105; -.
DR SMR; P25105; -.
DR BioGRID; 111696; 50.
DR CORUM; P25105; -.
DR IntAct; P25105; 16.
DR MINT; P25105; -.
DR STRING; 9606.ENSP00000362965; -.
DR BindingDB; P25105; -.
DR ChEMBL; CHEMBL250; -.
DR DrugBank; DB09166; Etizolam.
DR DrugBank; DB02261; Platelet Activating Factor.
DR DrugBank; DB11614; Rupatadine.
DR DrugCentral; P25105; -.
DR GuidetoPHARMACOLOGY; 334; -.
DR SwissLipids; SLP:000001565; -.
DR TCDB; 9.A.14.13.3; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P25105; 1 site.
DR iPTMnet; P25105; -.
DR PhosphoSitePlus; P25105; -.
DR BioMuta; PTAFR; -.
DR DMDM; 129557; -.
DR EPD; P25105; -.
DR jPOST; P25105; -.
DR MassIVE; P25105; -.
DR PaxDb; P25105; -.
DR PeptideAtlas; P25105; -.
DR PRIDE; P25105; -.
DR ProteomicsDB; 54261; -.
DR ABCD; P25105; 1 sequenced antibody.
DR Antibodypedia; 30903; 192 antibodies from 26 providers.
DR DNASU; 5724; -.
DR Ensembl; ENST00000305392.3; ENSP00000301974.3; ENSG00000169403.12.
DR Ensembl; ENST00000373857.8; ENSP00000362965.3; ENSG00000169403.12.
DR Ensembl; ENST00000539896.1; ENSP00000442658.1; ENSG00000169403.12.
DR GeneID; 5724; -.
DR KEGG; hsa:5724; -.
DR MANE-Select; ENST00000373857.8; ENSP00000362965.3; NM_000952.5; NP_000943.1.
DR UCSC; uc001bpl.4; human.
DR CTD; 5724; -.
DR DisGeNET; 5724; -.
DR GeneCards; PTAFR; -.
DR HGNC; HGNC:9582; PTAFR.
DR HPA; ENSG00000169403; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 173393; gene.
DR neXtProt; NX_P25105; -.
DR OpenTargets; ENSG00000169403; -.
DR PharmGKB; PA33933; -.
DR VEuPathDB; HostDB:ENSG00000169403; -.
DR eggNOG; ENOG502QTQI; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P25105; -.
DR OMA; AIHVIIC; -.
DR OrthoDB; 800525at2759; -.
DR PhylomeDB; P25105; -.
DR TreeFam; TF350009; -.
DR PathwayCommons; P25105; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P25105; -.
DR SIGNOR; P25105; -.
DR BioGRID-ORCS; 5724; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; PTAFR; human.
DR GeneWiki; Platelet-activating_factor_receptor; -.
DR GenomeRNAi; 5724; -.
DR Pharos; P25105; Tchem.
DR PRO; PR:P25105; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P25105; protein.
DR Bgee; ENSG00000169403; Expressed in monocyte and 191 other tissues.
DR Genevisible; P25105; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IEA:Ensembl.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0004992; F:platelet activating factor receptor activity; IDA:UniProtKB.
DR GO; GO:1904317; P:cellular response to 2-O-acetyl-1-O-hexadecyl-sn-glycero-3-phosphocholine; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0071258; P:cellular response to gravity; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0007567; P:parturition; IEA:Ensembl.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
DR GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:1904303; P:positive regulation of maternal process involved in parturition; IEA:Ensembl.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; IEA:Ensembl.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IEA:Ensembl.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1904300; P:positive regulation of transcytosis; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0009609; P:response to symbiotic bacterium; IEA:Ensembl.
DR GO; GO:0045056; P:transcytosis; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002282; PAF_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01153; PAFRECEPTOR.
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; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Platelet-activating factor receptor"
FT /id="PRO_0000070092"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..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..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 224
FT /note="A -> D (in dbSNP:rs5938)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011851"
FT VARIANT 338
FT /note="N -> S (in dbSNP:rs5939)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_011852"
FT CONFLICT 28
FT /note="L -> P (in Ref. 6; AAA60108)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="F -> L (in Ref. 6; AAA60108)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="C -> R (in Ref. 6; AAA60108)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="KR -> TG (in Ref. 4; AAA60214)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="KR -> TT (in Ref. 6; AAA60108)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="P -> A (in Ref. 6; AAA60108)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="K -> N (in Ref. 5; AAB24695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 39203 MW; 890073C9EBA79228 CRC64;
MEPHDSSHMD SEFRYTLFPI VYSIIFVLGV IANGYVLWVF ARLYPCKKFN EIKIFMVNLT
MADMLFLITL PLWIVYYQNQ GNWILPKFLC NVAGCLFFIN TYCSVAFLGV ITYNRFQAVT
RPIKTAQANT RKRGISLSLV IWVAIVGAAS YFLILDSTNT VPDSAGSGNV TRCFEHYEKG
SVPVLIIHIF IVFSFFLVFL IILFCNLVII RTLLMQPVQQ QRNAEVKRRA LWMVCTVLAV
FIICFVPHHV VQLPWTLAEL GFQDSKFHQA INDAHQVTLC LLSTNCVLDP VIYCFLTKKF
RKHLTEKFYS MRSSRKCSRA TTDTVTEVVV PFNQIPGNSL KN
