CXCR1_HUMAN
ID CXCR1_HUMAN Reviewed; 350 AA.
AC P25024; B2R6Q3; Q2YEF8; Q2YEG4; Q2YEG5; Q2YEG7; Q2YEG8; Q53R18; Q6IN95;
AC Q8N6T6; Q9P2T8; Q9P2T9; Q9P2U0; Q9P2U1; Q9P2U2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=C-X-C chemokine receptor type 1;
DE Short=CXC-R1;
DE Short=CXCR-1;
DE AltName: Full=CDw128a;
DE AltName: Full=High affinity interleukin-8 receptor A;
DE Short=IL-8R A;
DE AltName: Full=IL-8 receptor type 1;
DE AltName: CD_antigen=CD181;
GN Name=CXCR1; Synonyms=CMKAR1, IL8RA;
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 / MRNA], VARIANT THR-276, AND INTERACTION
RP WITH IL8.
RX PubMed=1840701; DOI=10.1126/science.1840701;
RA Holmes W.E., Lee J., Kuang W.-J., Rice G.C., Wood W.I.;
RT "Structure and functional expression of a human interleukin-8 receptor.";
RL Science 253:1278-1280(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=8384312; DOI=10.1016/0161-5890(93)90065-j;
RA Cerretti D.P., Kozlosky C.J., Vanden Bos T., Nelson N., Gearing D.P.,
RA Beckmann M.P.;
RT "Molecular characterization of receptors for human interleukin-8,
RT GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-
RT 2.";
RL Mol. Immunol. 30:359-367(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8486366; DOI=10.1006/geno.1993.1167;
RA Mollereau C., Passage E., Mattei M.-G., Vassart G., Parmentier M.;
RT "The high-affinity interleukin 8 receptor gene (IL8RA) maps to the 2q33-q36
RT region of the human genome: cloning of a pseudogene (IL8RBP) for the low-
RT affinity receptor.";
RL Genomics 16:248-251(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7929358; DOI=10.1016/s0021-9258(18)47205-5;
RA Ahuja S.K., Shetty A., Tiffany H.L., Murphy P.M.;
RT "Comparison of the genomic organization and promoter function for human
RT interleukin-8 receptors A and B.";
RL J. Biol. Chem. 269:26381-26389(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-31; THR-276 AND
RP CYS-335.
RX PubMed=16205979; DOI=10.1007/s00239-005-0039-x;
RA Liu Y., Yang S., Lin A.A., Cavalli-Sforza L.L., Su B.;
RT "Molecular evolution of CXCR1, a G protein-coupled receptor involved in
RT signal transduction of neutrophils.";
RL J. Mol. Evol. 61:691-696(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-31; THR-276; CYS-335
RP AND LEU-342.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-31 AND CYS-335.
RC TISSUE=Blood;
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 [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-350, AND VARIANTS THR-276; THR-306
RP AND CYS-335.
RX PubMed=11196695; DOI=10.1038/sj.gene.6363682;
RA Kato H., Tsuchiya N., Tokunaga K.;
RT "Single nucleotide polymorphisms in the coding regions of human CXC-
RT chemokine receptors CXCR1, CXCR2 and CXCR3.";
RL Genes Immun. 1:330-337(2000).
RN [13]
RP FUNCTION, AND INTERACTION WITH GNAI2.
RX PubMed=8662698; DOI=10.1074/jbc.271.22.12783;
RA Damaj B.B., McColl S.R., Mahana W., Crouch M.F., Naccache P.H.;
RT "Physical association of Gi2alpha with interleukin-8 receptors.";
RL J. Biol. Chem. 271:12783-12789(1996).
RN [14]
RP CHARACTERIZATION.
RX PubMed=1379593; DOI=10.1016/s0021-9258(18)41997-7;
RA Lee J., Horuk R., Rice G.C., Bennett G.L., Camerato T., Wood W.I.;
RT "Characterization of two high affinity human interleukin-8 receptors.";
RL J. Biol. Chem. 267:16283-16287(1992).
RN [15]
RP STRUCTURE BY NMR OF 9-29 IN COMPLEX WITH IL-8.
RX PubMed=10368283; DOI=10.1016/s0969-2126(99)80022-7;
RA Skelton N.J., Quan C., Reilly D., Lowman H.;
RT "Structure of a CXC chemokine-receptor fragment in complex with
RT interleukin-8.";
RL Structure 7:157-168(1999).
CC -!- FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils
CC chemotactic factor (PubMed:1840701). Binding of IL-8 to the receptor
CC causes activation of neutrophils. This response is mediated via a G-
CC protein that activates a phosphatidylinositol-calcium second messenger
CC system (PubMed:8662698). {ECO:0000269|PubMed:1840701,
CC ECO:0000269|PubMed:8662698}.
CC -!- SUBUNIT: Interacts with IL8 (PubMed:1840701). Interacts with GNAI2
CC (PubMed:8662698). {ECO:0000269|PubMed:1840701,
CC ECO:0000269|PubMed:8662698}.
CC -!- INTERACTION:
CC P25024; Q9NY35: CLDND1; NbExp=3; IntAct=EBI-3905522, EBI-4319704;
CC P25024; Q969F0: FATE1; NbExp=3; IntAct=EBI-3905522, EBI-743099;
CC P25024; P24593: IGFBP5; NbExp=3; IntAct=EBI-3905522, EBI-720480;
CC P25024; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-3905522, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXC chemokine receptors entry;
CC URL="https://en.wikipedia.org/wiki/CXC_chemokine_receptors";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il8ra/";
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DR EMBL; L19591; AAB59436.1; -; mRNA.
DR EMBL; L19592; AAA59160.1; -; Genomic_DNA.
DR EMBL; M68932; AAA59159.1; -; mRNA.
DR EMBL; X65858; CAA46688.1; -; Genomic_DNA.
DR EMBL; U11870; AAA64378.1; -; Genomic_DNA.
DR EMBL; AY916762; AAY21512.1; -; Genomic_DNA.
DR EMBL; AY916763; AAY21513.1; -; Genomic_DNA.
DR EMBL; AY916764; AAY21514.1; -; Genomic_DNA.
DR EMBL; AY916765; AAY21515.1; -; Genomic_DNA.
DR EMBL; AY916766; AAY21516.1; -; Genomic_DNA.
DR EMBL; AY916769; AAY21519.1; -; Genomic_DNA.
DR EMBL; AY916772; AAY21522.1; -; Genomic_DNA.
DR EMBL; AY916773; AAY21523.1; -; Genomic_DNA.
DR EMBL; CR541994; CAG46791.1; -; mRNA.
DR EMBL; CR542029; CAG46826.1; -; mRNA.
DR EMBL; AK312668; BAG35550.1; -; mRNA.
DR EMBL; AY651785; AAT46689.1; -; Genomic_DNA.
DR EMBL; AC097483; AAX93212.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70590.1; -; Genomic_DNA.
DR EMBL; BC028221; AAH28221.1; -; mRNA.
DR EMBL; BC072397; AAH72397.1; -; mRNA.
DR EMBL; AB032728; BAA92290.1; -; Genomic_DNA.
DR EMBL; AB032729; BAA92291.1; -; Genomic_DNA.
DR EMBL; AB032730; BAA92292.1; -; Genomic_DNA.
DR EMBL; AB032731; BAA92293.1; -; Genomic_DNA.
DR EMBL; AB032732; BAA92294.1; -; Genomic_DNA.
DR CCDS; CCDS2409.1; -.
DR PIR; I37449; A39445.
DR RefSeq; NP_000625.1; NM_000634.2.
DR PDB; 1ILP; NMR; -; C=9-29.
DR PDB; 1ILQ; NMR; -; C=9-29.
DR PDB; 2LNL; NMR; -; A=20-328.
DR PDB; 6XMN; NMR; -; B=1-29.
DR PDBsum; 1ILP; -.
DR PDBsum; 1ILQ; -.
DR PDBsum; 2LNL; -.
DR PDBsum; 6XMN; -.
DR AlphaFoldDB; P25024; -.
DR BMRB; P25024; -.
DR SMR; P25024; -.
DR BioGRID; 109791; 9.
DR DIP; DIP-3779N; -.
DR IntAct; P25024; 8.
DR STRING; 9606.ENSP00000295683; -.
DR BindingDB; P25024; -.
DR ChEMBL; CHEMBL4029; -.
DR DrugBank; DB01009; Ketoprofen.
DR DrugCentral; P25024; -.
DR GuidetoPHARMACOLOGY; 68; -.
DR GlyGen; P25024; 2 sites.
DR iPTMnet; P25024; -.
DR PhosphoSitePlus; P25024; -.
DR BioMuta; CXCR1; -.
DR DMDM; 108936015; -.
DR MassIVE; P25024; -.
DR PaxDb; P25024; -.
DR PeptideAtlas; P25024; -.
DR PRIDE; P25024; -.
DR ProteomicsDB; 54245; -.
DR Antibodypedia; 4267; 629 antibodies from 46 providers.
DR DNASU; 3577; -.
DR Ensembl; ENST00000295683.3; ENSP00000295683.2; ENSG00000163464.8.
DR GeneID; 3577; -.
DR KEGG; hsa:3577; -.
DR MANE-Select; ENST00000295683.3; ENSP00000295683.2; NM_000634.3; NP_000625.1.
DR UCSC; uc002vhc.4; human.
DR CTD; 3577; -.
DR DisGeNET; 3577; -.
DR GeneCards; CXCR1; -.
DR HGNC; HGNC:6026; CXCR1.
DR HPA; ENSG00000163464; Tissue enhanced (lymphoid).
DR MalaCards; CXCR1; -.
DR MIM; 146929; gene.
DR neXtProt; NX_P25024; -.
DR OpenTargets; ENSG00000163464; -.
DR PharmGKB; PA29842; -.
DR VEuPathDB; HostDB:ENSG00000163464; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P25024; -.
DR OMA; NDTAKWR; -.
DR OrthoDB; 865441at2759; -.
DR PhylomeDB; P25024; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P25024; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P25024; -.
DR SIGNOR; P25024; -.
DR BioGRID-ORCS; 3577; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; CXCR1; human.
DR EvolutionaryTrace; P25024; -.
DR GeneWiki; Interleukin_8_receptor,_alpha; -.
DR GenomeRNAi; 3577; -.
DR Pharos; P25024; Tchem.
DR PRO; PR:P25024; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P25024; protein.
DR Bgee; ENSG00000163464; Expressed in blood and 112 other tissues.
DR Genevisible; P25024; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0019959; F:interleukin-8 binding; IPI:UniProtKB.
DR GO; GO:0004918; F:interleukin-8 receptor activity; IDA:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR InterPro; IPR001355; Chemokine_CXCR1.
DR InterPro; IPR000174; Chemokine_CXCR_1/2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00427; INTRLEUKIN8R.
DR PRINTS; PR00572; INTRLEUKN8AR.
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 3D-structure; Cell membrane; Chemotaxis; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="C-X-C chemokine receptor type 1"
FT /id="PRO_0000069330"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 31
FT /note="M -> R (in dbSNP:rs16858811)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16205979, ECO:0000269|Ref.8"
FT /id="VAR_021061"
FT VARIANT 71
FT /note="R -> C (in dbSNP:rs1805038)"
FT /id="VAR_016236"
FT VARIANT 268
FT /note="M -> L (in dbSNP:rs9282752)"
FT /id="VAR_026525"
FT VARIANT 276
FT /note="S -> T (in dbSNP:rs2234671)"
FT /evidence="ECO:0000269|PubMed:11196695,
FT ECO:0000269|PubMed:16205979, ECO:0000269|PubMed:1840701,
FT ECO:0000269|Ref.8"
FT /id="VAR_003479"
FT VARIANT 306
FT /note="A -> T (in dbSNP:rs201583693)"
FT /evidence="ECO:0000269|PubMed:11196695"
FT /id="VAR_016237"
FT VARIANT 335
FT /note="R -> C (in dbSNP:rs16858808)"
FT /evidence="ECO:0000269|PubMed:11196695,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16205979,
FT ECO:0000269|Ref.8"
FT /id="VAR_016238"
FT VARIANT 342
FT /note="S -> L (in dbSNP:rs16858806)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_021062"
FT CONFLICT 154
FT /note="K -> N (in Ref. 11; AAH72397)"
FT /evidence="ECO:0000305"
FT HELIX 38..66
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:2LNL"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 108..138
FT /evidence="ECO:0007829|PDB:2LNL"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2LNL"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 149..173
FT /evidence="ECO:0007829|PDB:2LNL"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2LNL"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:2LNL"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2LNL"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 240..267
FT /evidence="ECO:0007829|PDB:2LNL"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:2LNL"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:2LNL"
SQ SEQUENCE 350 AA; 39791 MW; 2463E868C0EB0DE2 CRC64;
MSNITDPQMW DFDDLNFTGM PPADEDYSPC MLETETLNKY VVIIAYALVF LLSLLGNSLV
MLVILYSRVG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN
FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMNLSLP FFLFRQAYHP
NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA
MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNIGRALDAT EILGFLHSCL
NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL
