ITAX_HUMAN
ID ITAX_HUMAN Reviewed; 1163 AA.
AC P20702; Q8IVA6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Integrin alpha-X;
DE AltName: Full=CD11 antigen-like family member C;
DE AltName: Full=Leu M5;
DE AltName: Full=Leukocyte adhesion glycoprotein p150,95 alpha chain;
DE AltName: Full=Leukocyte adhesion receptor p150,95;
DE AltName: CD_antigen=CD11c;
DE Flags: Precursor;
GN Name=ITGAX; Synonyms=CD11C;
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 VARIANT THR-251.
RX PubMed=3327687; DOI=10.1002/j.1460-2075.1987.tb02746.x;
RA Corbi A.L., Miller L.J., O'Connor K., Larson R.S., Springer T.A.;
RT "cDNA cloning and complete primary structure of the alpha subunit of a
RT leukocyte adhesion glycoprotein, p150,95.";
RL EMBO J. 6:4023-4028(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-201 AND THR-251.
RX PubMed=2303426; DOI=10.1016/s0021-9258(19)39870-9;
RA Corbi A.L., Garcia-Aguilar J., Springer T.A.;
RT "Genomic structure of an integrin alpha subunit, the leukocyte p150,95
RT molecule.";
RL J. Biol. Chem. 265:2782-2788(1990).
RN [3]
RP ERRATUM OF PUBMED:2303426.
RA Corbi A.L., Garcia-Aguilar J., Springer T.A.;
RL J. Biol. Chem. 265:12750-12751(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-547.
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 [5]
RP PROTEIN SEQUENCE OF 20-43.
RX PubMed=3549901;
RA Miller L.J., Wiebe M., Springer T.A.;
RT "Purification and alpha subunit N-terminal sequences of human Mac-1 and
RT p150,95 leukocyte adhesion proteins.";
RL J. Immunol. 138:2381-2383(1987).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-899.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 20-1103 IN COMPLEX WITH ITGB2,
RP GLYCOSYLATION AT ASN-61; ASN-392; ASN-697; ASN-735 AND ASN-899, DISULFIDE
RP BONDS, METAL-BINDING SITES, AND SUBUNIT.
RX PubMed=20033057; DOI=10.1038/emboj.2009.367;
RA Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.;
RT "Structure of an integrin with an alphaI domain, complement receptor type
RT 4.";
RL EMBO J. 29:666-679(2010).
RN [8]
RP STRUCTURE BY NMR OF 1129-1163.
RX PubMed=22844534; DOI=10.1371/journal.pone.0041924;
RA Chua G.L., Tang X.Y., Patra A.T., Tan S.M., Bhattacharjya S.;
RT "Structure and binding interface of the cytosolic tails of alphaXbeta2
RT integrin.";
RL PLoS ONE 7:E41924-E41924(2012).
RN [9]
RP VARIANT VAL-1012.
RX PubMed=21763482; DOI=10.1016/j.ajhg.2011.06.001;
RA Vilarino-Guell C., Wider C., Ross O.A., Dachsel J.C., Kachergus J.M.,
RA Lincoln S.J., Soto-Ortolaza A.I., Cobb S.A., Wilhoite G.J., Bacon J.A.,
RA Behrouz B., Melrose H.L., Hentati E., Puschmann A., Evans D.M.,
RA Conibear E., Wasserman W.W., Aasly J.O., Burkhard P.R., Djaldetti R.,
RA Ghika J., Hentati F., Krygowska-Wajs A., Lynch T., Melamed E., Rajput A.,
RA Rajput A.H., Solida A., Wu R.M., Uitti R.J., Wszolek Z.K., Vingerhoets F.,
RA Farrer M.J.;
RT "VPS35 mutations in Parkinson disease.";
RL Am. J. Hum. Genet. 89:162-167(2011).
CC -!- FUNCTION: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It
CC recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell
CC interaction during inflammatory responses. It is especially important
CC in monocyte adhesion and chemotaxis.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-X associates
CC with beta-2. {ECO:0000269|PubMed:20033057}.
CC -!- INTERACTION:
CC P20702; P05107: ITGB2; NbExp=3; IntAct=EBI-2568308, EBI-300173;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and
CC granulocytes.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; M81695; AAA59180.1; -; mRNA.
DR EMBL; M29165; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M29487; AAA51620.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M29482; AAA51620.1; JOINED; Genomic_DNA.
DR EMBL; M29483; AAA51620.1; JOINED; Genomic_DNA.
DR EMBL; M29484; AAA51620.1; JOINED; Genomic_DNA.
DR EMBL; M29485; AAA51620.1; JOINED; Genomic_DNA.
DR EMBL; M29486; AAA51620.1; JOINED; Genomic_DNA.
DR EMBL; BC038237; AAH38237.1; -; mRNA.
DR CCDS; CCDS10711.1; -.
DR PIR; A36584; RWHU1C.
DR RefSeq; NP_000878.2; NM_000887.4.
DR RefSeq; NP_001273304.1; NM_001286375.1.
DR PDB; 1N3Y; X-ray; 1.65 A; A=147-338.
DR PDB; 2LUV; NMR; -; A=1129-1163.
DR PDB; 3K6S; X-ray; 3.50 A; A/C/E/G=20-1103.
DR PDB; 3K71; X-ray; 3.95 A; A/C/E/G=20-1103.
DR PDB; 3K72; X-ray; 3.70 A; A/C=20-1103.
DR PDB; 4NEH; X-ray; 2.75 A; A=20-1101.
DR PDB; 4NEN; X-ray; 2.90 A; A=20-1101.
DR PDB; 5ES4; X-ray; 3.30 A; A/C/E/G=20-1103.
DR PDBsum; 1N3Y; -.
DR PDBsum; 2LUV; -.
DR PDBsum; 3K6S; -.
DR PDBsum; 3K71; -.
DR PDBsum; 3K72; -.
DR PDBsum; 4NEH; -.
DR PDBsum; 4NEN; -.
DR PDBsum; 5ES4; -.
DR AlphaFoldDB; P20702; -.
DR BMRB; P20702; -.
DR SMR; P20702; -.
DR BioGRID; 109893; 4.
DR ComplexPortal; CPX-1827; Integrin alphaX-beta2 complex.
DR DIP; DIP-59369N; -.
DR IntAct; P20702; 2.
DR STRING; 9606.ENSP00000454623; -.
DR DrugBank; DB00095; Efalizumab.
DR GlyConnect; 1413; 2 N-Linked glycans (3 sites).
DR GlyGen; P20702; 8 sites, 2 N-linked glycans (3 sites).
DR iPTMnet; P20702; -.
DR PhosphoSitePlus; P20702; -.
DR BioMuta; ITGAX; -.
DR DMDM; 146345441; -.
DR jPOST; P20702; -.
DR MassIVE; P20702; -.
DR PaxDb; P20702; -.
DR PeptideAtlas; P20702; -.
DR PRIDE; P20702; -.
DR ProteomicsDB; 53777; -.
DR Antibodypedia; 1499; 2422 antibodies from 52 providers.
DR CPTC; P20702; 1 antibody.
DR DNASU; 3687; -.
DR Ensembl; ENST00000268296.9; ENSP00000268296.5; ENSG00000140678.17.
DR GeneID; 3687; -.
DR KEGG; hsa:3687; -.
DR MANE-Select; ENST00000268296.9; ENSP00000268296.5; NM_000887.5; NP_000878.2.
DR UCSC; uc002ebu.2; human.
DR CTD; 3687; -.
DR DisGeNET; 3687; -.
DR GeneCards; ITGAX; -.
DR HGNC; HGNC:6152; ITGAX.
DR HPA; ENSG00000140678; Tissue enhanced (bone marrow, lung, lymphoid tissue).
DR MIM; 151510; gene.
DR neXtProt; NX_P20702; -.
DR OpenTargets; ENSG00000140678; -.
DR PharmGKB; PA29952; -.
DR VEuPathDB; HostDB:ENSG00000140678; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000154838; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; P20702; -.
DR OMA; YCETFTL; -.
DR OrthoDB; 73876at2759; -.
DR PhylomeDB; P20702; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P20702; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P20702; -.
DR SIGNOR; P20702; -.
DR BioGRID-ORCS; 3687; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; ITGAX; human.
DR EvolutionaryTrace; P20702; -.
DR GeneWiki; CD11c; -.
DR GenomeRNAi; 3687; -.
DR Pharos; P20702; Tbio.
DR PRO; PR:P20702; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P20702; protein.
DR Bgee; ENSG00000140678; Expressed in granulocyte and 105 other tissues.
DR ExpressionAtlas; P20702; baseline and differential.
DR Genevisible; P20702; 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:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0034689; C:integrin alphaX-beta2 complex; TAS:ARUK-UCL.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:ARUK-UCL.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:1905956; P:positive regulation of endothelial tube morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0031643; P:positive regulation of myelination; ISS:ARUK-UCL.
DR Gene3D; 2.130.10.130; -; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3549901"
FT CHAIN 20..1163
FT /note="Integrin alpha-X"
FT /id="PRO_0000016294"
FT TOPO_DOM 20..1107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1129..1163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 23..78
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 79..138
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 165..339
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 340..391
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 392..443
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 444..504
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 507..565
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 570..630
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1131..1135
FT /note="GFFKR motif"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 534
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 593
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 597
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20033057"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20033057"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20033057"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20033057"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20033057"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..76
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 108..126
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 116..145
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 495..506
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 639..722
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 655..712
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 771..777
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 848..863
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 998..1022
FT /evidence="ECO:0000269|PubMed:20033057"
FT DISULFID 1027..1032
FT /evidence="ECO:0000269|PubMed:20033057"
FT VARIANT 48
FT /note="W -> R (in dbSNP:rs2230424)"
FT /id="VAR_018672"
FT VARIANT 201
FT /note="F -> L (in dbSNP:rs1574566)"
FT /evidence="ECO:0000269|PubMed:2303426"
FT /id="VAR_049632"
FT VARIANT 251
FT /note="A -> T (in dbSNP:rs2230428)"
FT /evidence="ECO:0000269|PubMed:2303426,
FT ECO:0000269|PubMed:3327687"
FT /id="VAR_031925"
FT VARIANT 517
FT /note="P -> R (in dbSNP:rs2230429)"
FT /id="VAR_031926"
FT VARIANT 547
FT /note="E -> K (in dbSNP:rs17853815)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031927"
FT VARIANT 564
FT /note="I -> V (in dbSNP:rs189592567)"
FT /id="VAR_059363"
FT VARIANT 971
FT /note="F -> L (in dbSNP:rs2230427)"
FT /id="VAR_031928"
FT VARIANT 1012
FT /note="A -> V (in dbSNP:rs181404376)"
FT /evidence="ECO:0000269|PubMed:21763482"
FT /id="VAR_066662"
FT CONFLICT 209
FT /note="S -> T (in Ref. 1; AAA59180 and 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> T (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="N -> T (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="K -> R (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="A -> P (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="A -> P (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="S -> T (in Ref. 1; AAA59180)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="A -> P (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="G -> A (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="D -> L (in Ref. 1; AAA59180)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="I -> V (in Ref. 4; AAH38237)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="H -> L (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="P -> G (in Ref. 2; AAA51620)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161..1163
FT /note="SEK -> TPHYPQDNV (in Ref. 4; AAH38237)"
FT /evidence="ECO:0000305"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 48..59
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5ES4"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 104..116
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4NEN"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:1N3Y"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1N3Y"
FT STRAND 186..201
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:1N3Y"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1N3Y"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1N3Y"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:1N3Y"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1N3Y"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:1N3Y"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3K6S"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3K6S"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 407..424
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 475..484
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:4NEN"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 618..632
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:3K6S"
FT STRAND 648..661
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:3K6S"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:5ES4"
FT STRAND 673..682
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:3K6S"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 696..706
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 708..719
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:5ES4"
FT STRAND 730..740
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 744..747
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 782..786
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 791..795
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 800..808
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 814..824
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 847..853
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 854..857
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 858..870
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 875..884
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 892..901
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:5ES4"
FT STRAND 914..924
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 926..930
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:4NEN"
FT STRAND 937..941
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 948..959
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 965..977
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 980..989
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 991..993
FT /evidence="ECO:0007829|PDB:4NEN"
FT STRAND 999..1003
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 1010..1016
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1019..1021
FT /evidence="ECO:0007829|PDB:4NEN"
FT TURN 1022..1024
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1025..1037
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1042..1053
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 1054..1058
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1062..1073
FT /evidence="ECO:0007829|PDB:4NEH"
FT TURN 1076..1078
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 1086..1089
FT /evidence="ECO:0007829|PDB:4NEH"
FT STRAND 1090..1100
FT /evidence="ECO:0007829|PDB:4NEH"
FT HELIX 1133..1144
FT /evidence="ECO:0007829|PDB:2LUV"
FT STRAND 1147..1149
FT /evidence="ECO:0007829|PDB:2LUV"
FT TURN 1150..1154
FT /evidence="ECO:0007829|PDB:2LUV"
FT TURN 1160..1162
FT /evidence="ECO:0007829|PDB:2LUV"
SQ SEQUENCE 1163 AA; 127829 MW; 8947288C43E76BE2 CRC64;
MTRTRAALLL FTALATSLGF NLDTEELTAF RVDSAGFGDS VVQYANSWVV VGAPQKITAA
NQTGGLYQCG YSTGACEPIG LQVPPEAVNM SLGLSLASTT SPSQLLACGP TVHHECGRNM
YLTGLCFLLG PTQLTQRLPV SRQECPRQEQ DIVFLIDGSG SISSRNFATM MNFVRAVISQ
FQRPSTQFSL MQFSNKFQTH FTFEEFRRSS NPLSLLASVH QLQGFTYTAT AIQNVVHRLF
HASYGARRDA AKILIVITDG KKEGDSLDYK DVIPMADAAG IIRYAIGVGL AFQNRNSWKE
LNDIASKPSQ EHIFKVEDFD ALKDIQNQLK EKIFAIEGTE TTSSSSFELE MAQEGFSAVF
TPDGPVLGAV GSFTWSGGAF LYPPNMSPTF INMSQENVDM RDSYLGYSTE LALWKGVQSL
VLGAPRYQHT GKAVIFTQVS RQWRMKAEVT GTQIGSYFGA SLCSVDVDSD GSTDLVLIGA
PHYYEQTRGG QVSVCPLPRG WRRWWCDAVL YGEQGHPWGR FGAALTVLGD VNGDKLTDVV
IGAPGEEENR GAVYLFHGVL GPSISPSHSQ RIAGSQLSSR LQYFGQALSG GQDLTQDGLV
DLAVGARGQV LLLRTRPVLW VGVSMQFIPA EIPRSAFECR EQVVSEQTLV QSNICLYIDK
RSKNLLGSRD LQSSVTLDLA LDPGRLSPRA TFQETKNRSL SRVRVLGLKA HCENFNLLLP
SCVEDSVTPI TLRLNFTLVG KPLLAFRNLR PMLAADAQRY FTASLPFEKN CGADHICQDN
LGISFSFPGL KSLLVGSNLE LNAEVMVWND GEDSYGTTIT FSHPAGLSYR YVAEGQKQGQ
LRSLHLTCDS APVGSQGTWS TSCRINHLIF RGGAQITFLA TFDVSPKAVL GDRLLLTANV
SSENNTPRTS KTTFQLELPV KYAVYTVVSS HEQFTKYLNF SESEEKESHV AMHRYQVNNL
GQRDLPVSIN FWVPVELNQE AVWMDVEVSH PQNPSLRCSS EKIAPPASDF LAHIQKNPVL
DCSIAGCLRF RCDVPSFSVQ EELDFTLKGN LSFGWVRQIL QKKVSVVSVA EITFDTSVYS
QLPGQEAFMR AQTTTVLEKY KVHNPTPLIV GSSIGGLLLL ALITAVLYKV GFFKRQYKEM
MEEANGQIAP ENGTQTPSPP SEK
