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Integrin alpha-X (CD11 antigen-like family member C) (Leu M5) (Leukocyte adhesion glycoprotein p150,95 alpha chain) (Leukocyte adhesion receptor p150,95) (CD antigen CD11c)

 ITAX_HUMAN              Reviewed;        1163 AA.
P20702; Q8IVA6;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
20-JUN-2018, entry version 179.
RecName: Full=Integrin alpha-X;
AltName: Full=CD11 antigen-like family member C;
AltName: Full=Leu M5;
AltName: Full=Leukocyte adhesion glycoprotein p150,95 alpha chain;
AltName: Full=Leukocyte adhesion receptor p150,95;
AltName: CD_antigen=CD11c;
Flags: Precursor;
Name=ITGAX; Synonyms=CD11C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-251.
PubMed=3327687;
Corbi A.L., Miller L.J., O'Connor K., Larson R.S., Springer T.A.;
"cDNA cloning and complete primary structure of the alpha subunit of a
leukocyte adhesion glycoprotein, p150,95.";
EMBO J. 6:4023-4028(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-201 AND THR-251.
PubMed=2303426;
Corbi A.L., Garcia-Aguilar J., Springer T.A.;
"Genomic structure of an integrin alpha subunit, the leukocyte p150,95
molecule.";
J. Biol. Chem. 265:2782-2788(1990).
[3]
ERRATUM.
Corbi A.L., Garcia-Aguilar J., Springer T.A.;
J. Biol. Chem. 265:12750-12751(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-547.
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 20-43.
PubMed=3549901;
Miller L.J., Wiebe M., Springer T.A.;
"Purification and alpha subunit N-terminal sequences of human Mac-1
and p150,95 leukocyte adhesion proteins.";
J. Immunol. 138:2381-2383(1987).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-899.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 20-1103 IN COMPLEX WITH
ITGB2, GLYCOSYLATION AT ASN-61; ASN-392; ASN-697; ASN-735 AND ASN-899,
DISULFIDE BONDS, METAL-BINDING SITES, AND SUBUNIT.
PubMed=20033057; DOI=10.1038/emboj.2009.367;
Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.;
"Structure of an integrin with an alphaI domain, complement receptor
type 4.";
EMBO J. 29:666-679(2010).
[8]
STRUCTURE BY NMR OF 1129-1163.
PubMed=22844534; DOI=10.1371/journal.pone.0041924;
Chua G.L., Tang X.Y., Patra A.T., Tan S.M., Bhattacharjya S.;
"Structure and binding interface of the cytosolic tails of alphaXbeta2
integrin.";
PLoS ONE 7:E41924-E41924(2012).
[9]
VARIANT VAL-1012.
PubMed=21763482; DOI=10.1016/j.ajhg.2011.06.001;
Vilarino-Guell C., Wider C., Ross O.A., Dachsel J.C., Kachergus J.M.,
Lincoln S.J., Soto-Ortolaza A.I., Cobb S.A., Wilhoite G.J.,
Bacon J.A., Behrouz B., Melrose H.L., Hentati E., Puschmann A.,
Evans D.M., Conibear E., Wasserman W.W., Aasly J.O., Burkhard P.R.,
Djaldetti R., Ghika J., Hentati F., Krygowska-Wajs A., Lynch T.,
Melamed E., Rajput A., Rajput A.H., Solida A., Wu R.M., Uitti R.J.,
Wszolek Z.K., Vingerhoets F., Farrer M.J.;
"VPS35 mutations in Parkinson disease.";
Am. J. Hum. Genet. 89:162-167(2011).
-!- FUNCTION: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It
recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell
interaction during inflammatory responses. It is especially
important in monocyte adhesion and chemotaxis.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-X
associates with beta-2. {ECO:0000269|PubMed:20033057}.
-!- INTERACTION:
P05107:ITGB2; NbExp=3; IntAct=EBI-2568308, EBI-300173;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and
granulocytes.
-!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
with I-domains do not undergo protease cleavage.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
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EMBL; M81695; AAA59180.1; -; mRNA.
EMBL; M29165; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M29487; AAA51620.1; ALT_SEQ; Genomic_DNA.
EMBL; M29482; AAA51620.1; JOINED; Genomic_DNA.
EMBL; M29483; AAA51620.1; JOINED; Genomic_DNA.
EMBL; M29484; AAA51620.1; JOINED; Genomic_DNA.
EMBL; M29485; AAA51620.1; JOINED; Genomic_DNA.
EMBL; M29486; AAA51620.1; JOINED; Genomic_DNA.
EMBL; BC038237; AAH38237.1; -; mRNA.
CCDS; CCDS10711.1; -.
PIR; A36584; RWHU1C.
RefSeq; NP_000878.2; NM_000887.4.
RefSeq; NP_001273304.1; NM_001286375.1.
UniGene; Hs.248472; -.
PDB; 1N3Y; X-ray; 1.65 A; A=147-338.
PDB; 2LUV; NMR; -; A=1129-1163.
PDB; 3K6S; X-ray; 3.50 A; A/C/E/G=20-1103.
PDB; 3K71; X-ray; 3.95 A; A/C/E/G=20-1103.
PDB; 3K72; X-ray; 3.70 A; A/C=20-1103.
PDB; 4NEH; X-ray; 2.75 A; A=20-1101.
PDB; 4NEN; X-ray; 2.90 A; A=20-1101.
PDB; 5ES4; X-ray; 3.30 A; A/C/E/G=20-1103.
PDBsum; 1N3Y; -.
PDBsum; 2LUV; -.
PDBsum; 3K6S; -.
PDBsum; 3K71; -.
PDBsum; 3K72; -.
PDBsum; 4NEH; -.
PDBsum; 4NEN; -.
PDBsum; 5ES4; -.
ProteinModelPortal; P20702; -.
SMR; P20702; -.
BioGrid; 109893; 1.
ComplexPortal; CPX-1827; Integrin alphaX-beta2 complex.
DIP; DIP-59369N; -.
IntAct; P20702; 2.
STRING; 9606.ENSP00000268296; -.
iPTMnet; P20702; -.
PhosphoSitePlus; P20702; -.
BioMuta; ITGAX; -.
DMDM; 146345441; -.
PaxDb; P20702; -.
PeptideAtlas; P20702; -.
PRIDE; P20702; -.
ProteomicsDB; 53777; -.
DNASU; 3687; -.
Ensembl; ENST00000268296; ENSP00000268296; ENSG00000140678.
GeneID; 3687; -.
KEGG; hsa:3687; -.
UCSC; uc002ebu.2; human.
CTD; 3687; -.
DisGeNET; 3687; -.
EuPathDB; HostDB:ENSG00000140678.16; -.
GeneCards; ITGAX; -.
H-InvDB; HIX0012988; -.
HGNC; HGNC:6152; ITGAX.
HPA; CAB004458; -.
HPA; CAB072871; -.
HPA; HPA004723; -.
MIM; 151510; gene.
neXtProt; NX_P20702; -.
OpenTargets; ENSG00000140678; -.
PharmGKB; PA29952; -.
eggNOG; ENOG410IPBA; Eukaryota.
eggNOG; ENOG410ZFBE; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000113114; -.
HOVERGEN; HBG100530; -.
InParanoid; P20702; -.
KO; K06462; -.
PhylomeDB; P20702; -.
TreeFam; TF105391; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P20702; -.
SIGNOR; P20702; -.
ChiTaRS; ITGAX; human.
EvolutionaryTrace; P20702; -.
GeneWiki; CD11c; -.
GenomeRNAi; 3687; -.
PRO; PR:P20702; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140678; -.
CleanEx; HS_ITGAX; -.
ExpressionAtlas; P20702; baseline and differential.
Genevisible; P20702; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
Gene3D; 2.130.10.130; -; 2.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
Pfam; PF00092; VWA; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
Magnesium; Membrane; Metal-binding; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:3549901}.
CHAIN 20 1163 Integrin alpha-X.
/FTId=PRO_0000016294.
TOPO_DOM 20 1107 Extracellular. {ECO:0000255}.
TRANSMEM 1108 1128 Helical. {ECO:0000255}.
TOPO_DOM 1129 1163 Cytoplasmic. {ECO:0000255}.
REPEAT 23 78 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 79 138 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
DOMAIN 165 339 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REPEAT 340 391 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 392 443 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 444 504 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 507 565 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 570 630 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 466 474
CA_BIND 530 538
CA_BIND 593 601
MOTIF 1131 1135 GFFKR motif.
METAL 157 157 Magnesium.
METAL 159 159 Magnesium.
METAL 161 161 Magnesium.
METAL 259 259 Magnesium.
METAL 466 466 Calcium 2.
METAL 468 468 Calcium 2.
METAL 470 470 Calcium 2.
METAL 472 472 Calcium 2; via carbonyl oxygen.
METAL 532 532 Calcium 3.
METAL 534 534 Calcium 3.
METAL 536 536 Calcium 3; via carbonyl oxygen.
METAL 593 593 Calcium 1.
METAL 595 595 Calcium 1.
METAL 597 597 Calcium 1.
METAL 599 599 Calcium 1; via carbonyl oxygen.
METAL 601 601 Calcium 1.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20033057}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20033057}.
CARBOHYD 697 697 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20033057}.
CARBOHYD 735 735 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20033057}.
CARBOHYD 899 899 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20033057}.
CARBOHYD 939 939 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1050 1050 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 69 76 {ECO:0000269|PubMed:20033057}.
DISULFID 108 126 {ECO:0000269|PubMed:20033057}.
DISULFID 116 145 {ECO:0000269|PubMed:20033057}.
DISULFID 495 506 {ECO:0000269|PubMed:20033057}.
DISULFID 639 722 {ECO:0000269|PubMed:20033057}.
DISULFID 655 712 {ECO:0000269|PubMed:20033057}.
DISULFID 771 777 {ECO:0000269|PubMed:20033057}.
DISULFID 848 863 {ECO:0000269|PubMed:20033057}.
DISULFID 998 1022 {ECO:0000269|PubMed:20033057}.
DISULFID 1027 1032 {ECO:0000269|PubMed:20033057}.
VARIANT 48 48 W -> R (in dbSNP:rs2230424).
/FTId=VAR_018672.
VARIANT 201 201 F -> L (in dbSNP:rs1574566).
{ECO:0000269|PubMed:2303426}.
/FTId=VAR_049632.
VARIANT 251 251 A -> T (in dbSNP:rs2230428).
{ECO:0000269|PubMed:2303426,
ECO:0000269|PubMed:3327687}.
/FTId=VAR_031925.
VARIANT 517 517 P -> R (in dbSNP:rs2230429).
/FTId=VAR_031926.
VARIANT 547 547 E -> K (in dbSNP:rs17853815).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031927.
VARIANT 564 564 I -> V (in dbSNP:rs189592567).
/FTId=VAR_059363.
VARIANT 971 971 F -> L (in dbSNP:rs2230427).
/FTId=VAR_031928.
VARIANT 1012 1012 A -> V (in dbSNP:rs181404376).
{ECO:0000269|PubMed:21763482}.
/FTId=VAR_066662.
CONFLICT 209 209 S -> T (in Ref. 1; AAA59180 and 2;
AAA51620). {ECO:0000305}.
CONFLICT 266 266 S -> T (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 327 327 N -> T (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 330 330 K -> R (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 335 335 A -> P (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 460 460 A -> P (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 469 469 S -> T (in Ref. 1; AAA59180).
{ECO:0000305}.
CONFLICT 480 480 A -> P (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 490 490 G -> A (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 756 756 D -> L (in Ref. 1; AAA59180).
{ECO:0000305}.
CONFLICT 819 819 I -> V (in Ref. 4; AAH38237).
{ECO:0000305}.
CONFLICT 990 990 H -> L (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 1005 1005 P -> G (in Ref. 2; AAA51620).
{ECO:0000305}.
CONFLICT 1161 1163 SEK -> TPHYPQDNV (in Ref. 4; AAH38237).
{ECO:0000305}.
STRAND 24 26 {ECO:0000244|PDB:4NEH}.
STRAND 28 31 {ECO:0000244|PDB:4NEH}.
TURN 35 38 {ECO:0000244|PDB:4NEH}.
STRAND 39 44 {ECO:0000244|PDB:4NEH}.
TURN 45 47 {ECO:0000244|PDB:4NEH}.
STRAND 48 59 {ECO:0000244|PDB:4NEH}.
STRAND 62 69 {ECO:0000244|PDB:4NEH}.
TURN 71 73 {ECO:0000244|PDB:4NEH}.
STRAND 75 78 {ECO:0000244|PDB:4NEH}.
STRAND 87 89 {ECO:0000244|PDB:5ES4}.
STRAND 94 99 {ECO:0000244|PDB:4NEH}.
TURN 100 103 {ECO:0000244|PDB:4NEH}.
STRAND 104 116 {ECO:0000244|PDB:4NEH}.
STRAND 119 129 {ECO:0000244|PDB:4NEH}.
STRAND 131 133 {ECO:0000244|PDB:4NEN}.
STRAND 136 141 {ECO:0000244|PDB:4NEH}.
STRAND 150 157 {ECO:0000244|PDB:1N3Y}.
HELIX 164 178 {ECO:0000244|PDB:1N3Y}.
TURN 183 185 {ECO:0000244|PDB:1N3Y}.
STRAND 186 201 {ECO:0000244|PDB:1N3Y}.
HELIX 203 208 {ECO:0000244|PDB:1N3Y}.
HELIX 212 216 {ECO:0000244|PDB:1N3Y}.
HELIX 228 236 {ECO:0000244|PDB:1N3Y}.
TURN 237 240 {ECO:0000244|PDB:1N3Y}.
HELIX 242 244 {ECO:0000244|PDB:1N3Y}.
STRAND 250 260 {ECO:0000244|PDB:1N3Y}.
HELIX 269 278 {ECO:0000244|PDB:1N3Y}.
STRAND 282 289 {ECO:0000244|PDB:1N3Y}.
HELIX 290 293 {ECO:0000244|PDB:1N3Y}.
HELIX 298 304 {ECO:0000244|PDB:1N3Y}.
STRAND 307 309 {ECO:0000244|PDB:1N3Y}.
HELIX 310 312 {ECO:0000244|PDB:1N3Y}.
STRAND 313 318 {ECO:0000244|PDB:1N3Y}.
HELIX 319 325 {ECO:0000244|PDB:1N3Y}.
HELIX 326 334 {ECO:0000244|PDB:1N3Y}.
HELIX 336 338 {ECO:0000244|PDB:4NEH}.
TURN 341 343 {ECO:0000244|PDB:4NEH}.
STRAND 348 351 {ECO:0000244|PDB:3K6S}.
STRAND 354 361 {ECO:0000244|PDB:4NEH}.
STRAND 364 369 {ECO:0000244|PDB:4NEH}.
HELIX 372 375 {ECO:0000244|PDB:4NEH}.
STRAND 379 381 {ECO:0000244|PDB:4NEH}.
STRAND 384 386 {ECO:0000244|PDB:3K6S}.
STRAND 389 391 {ECO:0000244|PDB:4NEH}.
HELIX 398 400 {ECO:0000244|PDB:4NEH}.
STRAND 407 424 {ECO:0000244|PDB:4NEH}.
HELIX 427 429 {ECO:0000244|PDB:4NEH}.
STRAND 432 439 {ECO:0000244|PDB:4NEH}.
STRAND 442 450 {ECO:0000244|PDB:4NEH}.
STRAND 460 465 {ECO:0000244|PDB:4NEH}.
STRAND 470 472 {ECO:0000244|PDB:4NEH}.
STRAND 475 484 {ECO:0000244|PDB:4NEH}.
STRAND 489 496 {ECO:0000244|PDB:4NEH}.
STRAND 508 510 {ECO:0000244|PDB:4NEH}.
STRAND 514 521 {ECO:0000244|PDB:4NEN}.
STRAND 523 529 {ECO:0000244|PDB:4NEH}.
STRAND 531 535 {ECO:0000244|PDB:4NEH}.
STRAND 538 543 {ECO:0000244|PDB:4NEH}.
HELIX 546 549 {ECO:0000244|PDB:4NEH}.
STRAND 551 556 {ECO:0000244|PDB:4NEH}.
TURN 560 562 {ECO:0000244|PDB:4NEH}.
STRAND 569 573 {ECO:0000244|PDB:4NEH}.
HELIX 574 577 {ECO:0000244|PDB:4NEH}.
STRAND 586 592 {ECO:0000244|PDB:4NEH}.
STRAND 595 599 {ECO:0000244|PDB:4NEH}.
STRAND 601 606 {ECO:0000244|PDB:4NEH}.
STRAND 609 615 {ECO:0000244|PDB:4NEH}.
STRAND 618 632 {ECO:0000244|PDB:4NEH}.
TURN 634 636 {ECO:0000244|PDB:4NEH}.
STRAND 641 643 {ECO:0000244|PDB:3K6S}.
STRAND 648 661 {ECO:0000244|PDB:4NEH}.
TURN 662 664 {ECO:0000244|PDB:3K6S}.
TURN 668 670 {ECO:0000244|PDB:5ES4}.
STRAND 673 682 {ECO:0000244|PDB:4NEH}.
STRAND 685 687 {ECO:0000244|PDB:3K6S}.
TURN 693 695 {ECO:0000244|PDB:4NEH}.
STRAND 696 706 {ECO:0000244|PDB:4NEH}.
STRAND 708 719 {ECO:0000244|PDB:4NEH}.
STRAND 726 728 {ECO:0000244|PDB:5ES4}.
STRAND 730 740 {ECO:0000244|PDB:4NEH}.
TURN 744 747 {ECO:0000244|PDB:4NEH}.
STRAND 760 765 {ECO:0000244|PDB:4NEH}.
STRAND 772 774 {ECO:0000244|PDB:4NEH}.
STRAND 782 786 {ECO:0000244|PDB:4NEH}.
STRAND 791 795 {ECO:0000244|PDB:4NEH}.
STRAND 800 808 {ECO:0000244|PDB:4NEH}.
STRAND 814 824 {ECO:0000244|PDB:4NEH}.
STRAND 827 829 {ECO:0000244|PDB:4NEH}.
STRAND 838 841 {ECO:0000244|PDB:4NEH}.
STRAND 847 853 {ECO:0000244|PDB:4NEH}.
TURN 854 857 {ECO:0000244|PDB:4NEH}.
STRAND 858 870 {ECO:0000244|PDB:4NEH}.
STRAND 875 884 {ECO:0000244|PDB:4NEH}.
STRAND 892 901 {ECO:0000244|PDB:4NEH}.
STRAND 908 910 {ECO:0000244|PDB:5ES4}.
STRAND 914 924 {ECO:0000244|PDB:4NEH}.
STRAND 926 930 {ECO:0000244|PDB:4NEH}.
STRAND 932 934 {ECO:0000244|PDB:4NEN}.
STRAND 937 941 {ECO:0000244|PDB:4NEH}.
STRAND 948 959 {ECO:0000244|PDB:4NEH}.
STRAND 961 963 {ECO:0000244|PDB:4NEH}.
STRAND 965 977 {ECO:0000244|PDB:4NEH}.
STRAND 980 989 {ECO:0000244|PDB:4NEH}.
STRAND 991 993 {ECO:0000244|PDB:4NEN}.
STRAND 999 1003 {ECO:0000244|PDB:4NEH}.
HELIX 1010 1016 {ECO:0000244|PDB:4NEH}.
STRAND 1019 1021 {ECO:0000244|PDB:4NEN}.
TURN 1022 1024 {ECO:0000244|PDB:4NEH}.
STRAND 1025 1037 {ECO:0000244|PDB:4NEH}.
STRAND 1042 1053 {ECO:0000244|PDB:4NEH}.
HELIX 1054 1058 {ECO:0000244|PDB:4NEH}.
STRAND 1062 1073 {ECO:0000244|PDB:4NEH}.
TURN 1076 1078 {ECO:0000244|PDB:4NEH}.
STRAND 1079 1081 {ECO:0000244|PDB:4NEH}.
HELIX 1086 1089 {ECO:0000244|PDB:4NEH}.
STRAND 1090 1100 {ECO:0000244|PDB:4NEH}.
HELIX 1133 1144 {ECO:0000244|PDB:2LUV}.
STRAND 1147 1149 {ECO:0000244|PDB:2LUV}.
TURN 1150 1154 {ECO:0000244|PDB:2LUV}.
TURN 1160 1162 {ECO:0000244|PDB:2LUV}.
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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