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Database: UniProt
Entry: P20702
LinkDB: P20702
Original site: P20702 
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   02-JUN-2021, entry version 200.
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;
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   BMRB; P20702; -.
DR   SMR; P20702; -.
DR   BioGRID; 109893; 3.
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.
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; 2343 antibodies.
DR   DNASU; 3687; -.
DR   Ensembl; ENST00000268296; ENSP00000268296; ENSG00000140678.
DR   GeneID; 3687; -.
DR   KEGG; hsa:3687; -.
DR   UCSC; uc002ebu.2; human.
DR   CTD; 3687; -.
DR   DisGeNET; 3687; -.
DR   GeneCards; ITGAX; -.
DR   HGNC; HGNC:6152; ITGAX.
DR   HPA; ENSG00000140678; Tissue enhanced (adipose tissue, blood, lung, lymphoid tissue).
DR   MIM; 151510; gene.
DR   neXtProt; NX_P20702; -.
DR   OpenTargets; ENSG00000140678; -.
DR   PharmGKB; PA29952; -.
DR   VEuPathDB; HostDB:ENSG00000140678.16; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000154838; -.
DR   HOGENOM; CLU_004111_3_0_1; -.
DR   InParanoid; P20702; -.
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; 5 hits in 988 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 blood and 140 other tissues.
DR   ExpressionAtlas; P20702; baseline and differential.
DR   Genevisible; P20702; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
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; TAS:ProtInc.
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; TAS:ARUK-UCL.
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:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
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   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   CA_BIND         466..474
FT   CA_BIND         530..538
FT   CA_BIND         593..601
FT   MOTIF           1131..1135
FT                   /note="GFFKR motif"
FT   METAL           157
FT                   /note="Magnesium"
FT   METAL           159
FT                   /note="Magnesium"
FT   METAL           161
FT                   /note="Magnesium"
FT   METAL           259
FT                   /note="Magnesium"
FT   METAL           466
FT                   /note="Calcium 2"
FT   METAL           468
FT                   /note="Calcium 2"
FT   METAL           470
FT                   /note="Calcium 2"
FT   METAL           472
FT                   /note="Calcium 2; via carbonyl oxygen"
FT   METAL           532
FT                   /note="Calcium 3"
FT   METAL           534
FT                   /note="Calcium 3"
FT   METAL           536
FT                   /note="Calcium 3; via carbonyl oxygen"
FT   METAL           593
FT                   /note="Calcium 1"
FT   METAL           595
FT                   /note="Calcium 1"
FT   METAL           597
FT                   /note="Calcium 1"
FT   METAL           599
FT                   /note="Calcium 1; via carbonyl oxygen"
FT   METAL           601
FT                   /note="Calcium 1"
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
//
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