CXCR2_HUMAN
ID CXCR2_HUMAN Reviewed; 360 AA.
AC P25025; Q8IUZ1; Q9P2T6; Q9P2T7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=C-X-C chemokine receptor type 2;
DE Short=CXC-R2;
DE Short=CXCR-2;
DE AltName: Full=CDw128b;
DE AltName: Full=GRO/MGSA receptor;
DE AltName: Full=High affinity interleukin-8 receptor B;
DE Short=IL-8R B;
DE AltName: Full=IL-8 receptor type 2;
DE AltName: CD_antigen=CD182;
GN Name=CXCR2; Synonyms=IL8RB;
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], AND INTERACTION WITH IL8.
RX PubMed=1891716; DOI=10.1126/science.1891716;
RA Murphy P.M., Tiffany H.L.;
RT "Cloning of complementary DNA encoding a functional human interleukin-8
RT receptor.";
RL Science 253:1280-1283(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 / MRNA].
RX PubMed=7512557; DOI=10.1016/s0021-9258(19)78092-2;
RA Sprenger H., Lloyd A.R., Lautens L.L., Bonner T.I., Kelvin D.J.;
RT "Structure, genomic organization, and expression of the human interleukin-8
RT receptor B gene.";
RL J. Biol. Chem. 269:11065-11072(1994).
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].
RG SeattleSNPs variation discovery resource;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-162 AND 191-301, AND VARIANT
RP CYS-80.
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION AT SER-347; SER-351; SER-352 AND SER-353.
RX PubMed=9079638; DOI=10.1074/jbc.272.13.8207;
RA Mueller S.G., White J.R., Schraw W.P., Lam V., Richmond A.;
RT "Ligand-induced desensitization of the human CXC chemokine receptor-2 is
RT modulated by multiple serine residues in the carboxyl-terminal domain of
RT the receptor.";
RL J. Biol. Chem. 272:8207-8214(1997).
RN [11]
RP CLEAVAGE BY STAPHYLOCOCCUS AUREUS STAPHOPAIN A (MICROBIAL INFECTION).
RX PubMed=22850671; DOI=10.1038/emboj.2012.212;
RA Laarman A.J., Mijnheer G., Mootz J.M., van Rooijen W.J., Ruyken M.,
RA Malone C.L., Heezius E.C., Ward R., Milligan G., van Strijp J.A.,
RA de Haas C.J., Horswill A.R., van Kessel K.P., Rooijakkers S.H.;
RT "Staphylococcus aureus Staphopain A inhibits CXCR2-dependent neutrophil
RT activation and chemotaxis.";
RL EMBO J. 31:3607-3619(2012).
RN [12]
RP INVOLVEMENT IN WHIMS2.
RX PubMed=24777453; DOI=10.1038/ng.2962;
RA Auer P.L., Teumer A., Schick U., O'Shaughnessy A., Lo K.S., Chami N.,
RA Carlson C., de Denus S., Dube M.P., Haessler J., Jackson R.D.,
RA Kooperberg C., Perreault L.P., Nauck M., Peters U., Rioux J.D., Schmidt F.,
RA Turcot V., Voelker U., Voelzke H., Greinacher A., Hsu L., Tardif J.C.,
RA Diaz G.A., Reiner A.P., Lettre G.;
RT "Rare and low-frequency coding variants in CXCR2 and other genes are
RT associated with hematological traits.";
RL Nat. Genet. 46:629-634(2014).
CC -!- FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil
CC chemotactic factor (PubMed:1891716). 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). Binds to IL-8 with high affinity. Also binds
CC with high affinity to CXCL3, GRO/MGSA and NAP-2.
CC {ECO:0000269|PubMed:1891716, ECO:0000269|PubMed:8662698}.
CC -!- SUBUNIT: Interacts with IL8 (PubMed:1891716). Interacts with GNAI2
CC (PubMed:8662698). {ECO:0000269|PubMed:1891716,
CC ECO:0000269|PubMed:8662698}.
CC -!- INTERACTION:
CC P25025; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-2835281, EBI-12069500;
CC P25025; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-2835281, EBI-12003442;
CC P25025; P04233: CD74; NbExp=2; IntAct=EBI-2835281, EBI-2622890;
CC P25025; Q8N7P3: CLDN22; NbExp=3; IntAct=EBI-2835281, EBI-17766761;
CC P25025; P10145: CXCL8; NbExp=3; IntAct=EBI-2835281, EBI-3917999;
CC P25025; P54849: EMP1; NbExp=3; IntAct=EBI-2835281, EBI-4319440;
CC P25025; Q14318: FKBP8; NbExp=3; IntAct=EBI-2835281, EBI-724839;
CC P25025; P46940: IQGAP1; NbExp=12; IntAct=EBI-2835281, EBI-297509;
CC P25025; Q05940: SLC18A2; NbExp=3; IntAct=EBI-2835281, EBI-18036244;
CC P25025; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-2835281, EBI-12898013;
CC P25025; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-2835281, EBI-8640191;
CC P25025; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-2835281, EBI-348587;
CC P25025; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-2835281, EBI-11742770;
CC P25025; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-2835281, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated upon ligand binding; which is required for
CC desensitization. {ECO:0000269|PubMed:9079638}.
CC -!- PTM: (Microbial infection) Proteolytically cleaved by Staphylococcus
CC aureus staphopain A/SspP. This cleavage inhibits CXCR2-dependent
CC neutrophil activation and chemotaxis. {ECO:0000269|PubMed:22850671}.
CC -!- DISEASE: WHIM syndrome 2 (WHIMS2) [MIM:619407]: An autosomal recessive
CC form of WHIM syndrome, a primary immunodeficiency disorder
CC characterized by warts, hypogammaglobulinemia, infections, and
CC myelokathexis. Myelokathexis is a unique form of non-cyclic severe
CC congenital neutropenia caused by accumulation of mature and
CC degenerating neutrophils in the bone marrow. Monocytopenia and
CC lymphopenia, especially B lymphopenia, also commonly occur. There is
CC significant phenotypic variation among patients, such that some
CC individuals may have an incomplete form of the disorder in which one or
CC more of the classic tetrad features are not present.
CC {ECO:0000269|PubMed:24777453}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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/il8rb/";
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DR EMBL; M73969; AAA83148.1; -; mRNA.
DR EMBL; M94582; AAA36108.1; -; mRNA.
DR EMBL; M99412; AAC14460.1; -; Genomic_DNA.
DR EMBL; L19593; AAB59437.1; -; mRNA.
DR EMBL; U11869; AAB60656.1; -; Genomic_DNA.
DR EMBL; AY714242; AAT97985.1; -; Genomic_DNA.
DR EMBL; BC037961; AAH37961.2; -; mRNA.
DR EMBL; AB032733; BAA92295.1; -; Genomic_DNA.
DR EMBL; AB032734; BAA92296.1; -; Genomic_DNA.
DR CCDS; CCDS2408.1; -.
DR PIR; I37898; A53611.
DR RefSeq; NP_001161770.1; NM_001168298.1.
DR RefSeq; NP_001548.1; NM_001557.3.
DR RefSeq; XP_005246587.1; XM_005246530.3.
DR RefSeq; XP_016859479.1; XM_017003990.1.
DR RefSeq; XP_016859480.1; XM_017003991.1.
DR RefSeq; XP_016859481.1; XM_017003992.1.
DR PDB; 4Q3H; X-ray; 1.44 A; A/B=356-360.
DR PDB; 5TYT; X-ray; 2.40 A; A/B/C/D=356-360.
DR PDB; 6KVA; X-ray; 2.20 A; B/b=9-19.
DR PDB; 6KVF; X-ray; 2.79 A; B/b=9-19.
DR PDB; 6LFM; EM; 3.50 A; R=1-360.
DR PDB; 6LFO; EM; 3.40 A; R=1-360.
DR PDBsum; 4Q3H; -.
DR PDBsum; 5TYT; -.
DR PDBsum; 6KVA; -.
DR PDBsum; 6KVF; -.
DR PDBsum; 6LFM; -.
DR PDBsum; 6LFO; -.
DR AlphaFoldDB; P25025; -.
DR SMR; P25025; -.
DR BioGRID; 109793; 22.
DR CORUM; P25025; -.
DR DIP; DIP-3782N; -.
DR IntAct; P25025; 43.
DR MINT; P25025; -.
DR STRING; 9606.ENSP00000319635; -.
DR BindingDB; P25025; -.
DR ChEMBL; CHEMBL2434; -.
DR DrugCentral; P25025; -.
DR GuidetoPHARMACOLOGY; 69; -.
DR GlyGen; P25025; 1 site.
DR iPTMnet; P25025; -.
DR PhosphoSitePlus; P25025; -.
DR BioMuta; CXCR2; -.
DR DMDM; 1352454; -.
DR jPOST; P25025; -.
DR MassIVE; P25025; -.
DR PaxDb; P25025; -.
DR PeptideAtlas; P25025; -.
DR PRIDE; P25025; -.
DR ProteomicsDB; 54246; -.
DR ABCD; P25025; 1 sequenced antibody.
DR Antibodypedia; 4268; 1019 antibodies from 49 providers.
DR DNASU; 3579; -.
DR Ensembl; ENST00000318507.7; ENSP00000319635.2; ENSG00000180871.8.
DR GeneID; 3579; -.
DR KEGG; hsa:3579; -.
DR MANE-Select; ENST00000318507.7; ENSP00000319635.2; NM_001557.4; NP_001548.1.
DR CTD; 3579; -.
DR DisGeNET; 3579; -.
DR GeneCards; CXCR2; -.
DR HGNC; HGNC:6027; CXCR2.
DR HPA; ENSG00000180871; Tissue enhanced (esophagus, lymphoid tissue).
DR MalaCards; CXCR2; -.
DR MIM; 146928; gene.
DR MIM; 619407; phenotype.
DR neXtProt; NX_P25025; -.
DR OpenTargets; ENSG00000180871; -.
DR Orphanet; 420699; Autosomal recessive severe congenital neutropenia due to CXCR2 deficiency.
DR PharmGKB; PA29843; -.
DR VEuPathDB; HostDB:ENSG00000180871; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P25025; -.
DR OMA; QSICYEN; -.
DR OrthoDB; 865441at2759; -.
DR PhylomeDB; P25025; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P25025; -.
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; P25025; -.
DR SIGNOR; P25025; -.
DR BioGRID-ORCS; 3579; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; CXCR2; human.
DR GenomeRNAi; 3579; -.
DR Pharos; P25025; Tchem.
DR PRO; PR:P25025; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P25025; protein.
DR Bgee; ENSG00000180871; Expressed in blood and 131 other tissues.
DR ExpressionAtlas; P25025; baseline and differential.
DR Genevisible; P25025; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0042629; C:mast cell granule; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0016494; F:C-X-C chemokine receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0019959; F:interleukin-8 binding; IPI:UniProtKB.
DR GO; GO:0004918; F:interleukin-8 receptor activity; IDA:UniProtKB.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
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:0006968; P:cellular defense response; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0038112; P:interleukin-8-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0072173; P:metanephric tubule morphogenesis; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; IEA:Ensembl.
DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR IDEAL; IID00625; -.
DR InterPro; IPR000057; Chemokine_CXCR2.
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; PR00573; INTRLEUKN8BR.
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; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="C-X-C chemokine receptor type 2"
FT /id="PRO_0000069337"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 35..36
FT /note="(Microbial infection) Cleavage; by Staphylococcus
FT aureus/SspP"
FT /evidence="ECO:0000269|PubMed:22850671"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:9079638"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:9079638"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:9079638"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:9079638"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 80
FT /note="R -> C (in dbSNP:rs138773569)"
FT /evidence="ECO:0000269|PubMed:11196695"
FT /id="VAR_014679"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 48..74
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:6LFO"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:6LFO"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 162..183
FT /evidence="ECO:0007829|PDB:6LFO"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6LFM"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6LFM"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:6LFO"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 288..304
FT /evidence="ECO:0007829|PDB:6LFO"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:6LFO"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:6LFO"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:6LFO"
SQ SEQUENCE 360 AA; 40759 MW; 564F04A8BCC0A197 CRC64;
MEDFNMESDS FEDFWKGEDL SNYSYSSTLP PFLLDAAPCE PESLEINKYF VVIIYALVFL
LSLLGNSLVM LVILYSRVGR SVTDVYLLNL ALADLLFALT LPIWAASKVN GWIFGTFLCK
VVSLLKEVNF YSGILLLACI SVDRYLAIVH ATRTLTQKRY LVKFICLSIW GLSLLLALPV
LLFRRTVYSS NVSPACYEDM GNNTANWRML LRILPQSFGF IVPLLIMLFC YGFTLRTLFK
AHMGQKHRAM RVIFAVVLIF LLCWLPYNLV LLADTLMRTQ VIQETCERRN HIDRALDATE
ILGILHSCLN PLIYAFIGQK FRHGLLKILA IHGLISKDSL PKDSRPSFVG SSSGHTSTTL
