DOCK1_HUMAN
ID DOCK1_HUMAN Reviewed; 1865 AA.
AC Q14185; A9Z1Z5;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Dedicator of cytokinesis protein 1;
DE AltName: Full=180 kDa protein downstream of CRK;
DE Short=DOCK180;
GN Name=DOCK1;
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], FUNCTION, AND INTERACTION WITH CRK.
RC TISSUE=Placenta;
RX PubMed=8657152; DOI=10.1128/mcb.16.4.1770;
RA Hasegawa H., Kiyokawa E., Tanaka S., Nagashima K., Gotoh N., Shibuya M.,
RA Kurata T., Matsuda M.;
RT "DOCK180, a major CRK-binding protein, alters cell morphology upon
RT translocation to the cell membrane.";
RL Mol. Cell. Biol. 16:1770-1776(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP INTERACTION WITH CRK.
RX PubMed=8662907; DOI=10.1074/jbc.271.24.14468;
RA Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T.,
RA Nagashima K., Kurata T.;
RT "Interaction between the amino-terminal SH3 domain of CRK and its natural
RT target proteins.";
RL J. Biol. Chem. 271:14468-14472(1996).
RN [4]
RP GEF ACTIVITY, AND INTERACTION WITH RAC1.
RX PubMed=9808620; DOI=10.1101/gad.12.21.3331;
RA Kiyokawa E., Hashimoto Y., Kobayashi S., Sugimura H., Kurata T.,
RA Matsuda M.;
RT "Activation of Rac1 by a Crk SH3-binding protein, DOCK180.";
RL Genes Dev. 12:3331-3336(1998).
RN [5]
RP INTERACTION WITH NCK2.
RX PubMed=11240126; DOI=10.1016/s0014-5793(01)02195-0;
RA Tu Y., Kucik D.F., Wu C.;
RT "Identification and kinetic analysis of the interaction between Nck-2 and
RT DOCK180.";
RL FEBS Lett. 491:193-199(2001).
RN [6]
RP INTERACTION WITH PTDINS(3,4,5)P3.
RX PubMed=11171081; DOI=10.1042/0264-6021:3540073;
RA Kobayashi S., Shirai T., Kiyokawa E., Mochizuki N., Matsuda M., Fukui Y.;
RT "Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3.";
RL Biochem. J. 354:73-78(2001).
RN [7]
RP GEF ACTIVITY, INTERACTION WITH RAC1; ELMO1 AND ELMO2, SUBUNIT OF A COMPLEX
RP CONTAINING ELMO1 AND DOCK1, AND MUTAGENESIS OF 1401-TYR-ILE-1402 AND
RP 1487-ILE--PRO-1489.
RX PubMed=12134158; DOI=10.1038/ncb824;
RA Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F.,
RA Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R.,
RA Ravichandran K.S.;
RT "Unconventional Rac-GEF activity is mediated through the Dock180-ELMO
RT complex.";
RL Nat. Cell Biol. 4:574-582(2002).
RN [8]
RP NOMENCLATURE, AND GEF ACTIVITY.
RX PubMed=12432077; DOI=10.1242/jcs.00219;
RA Cote J.-F., Vuori K.;
RT "Identification of an evolutionarily conserved superfamily of DOCK180-
RT related proteins with guanine nucleotide exchange activity.";
RL J. Cell Sci. 115:4901-4913(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1751, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION.
RX PubMed=19004829; DOI=10.1074/jbc.m808010200;
RA Sanders M.A., Ampasala D., Basson M.D.;
RT "DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell spreading and
RT migration on collagen IV.";
RL J. Biol. Chem. 284:27-35(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1681, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1681, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Along with DOCK1,
CC mediates CRK/CRKL regulation of epithelial and endothelial cell
CC spreading and migration on type IV collagen (PubMed:19004829).
CC Functions as a guanine nucleotide exchange factor (GEF), which
CC activates Rac Rho small GTPases by exchanging bound GDP for free GTP.
CC Its GEF activity may be enhanced by ELMO1 (PubMed:8657152).
CC {ECO:0000269|PubMed:19004829, ECO:0000269|PubMed:8657152}.
CC -!- SUBUNIT: Interacts with the SH3 domains of CRK and NCK2 via multiple
CC sites (PubMed:8657152, PubMed:8662907, PubMed:11240126). Interacts with
CC nucleotide-free RAC1 via its DOCKER domain (PubMed:9808620,
CC PubMed:12134158). Interacts with ELMO1, ELMO2 and probably ELMO3 via
CC its SH3 domain (PubMed:12134158). Interacts with ADGRB1. Identified in
CC a complex with AUTS2 and ELMO2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BUR4, ECO:0000269|PubMed:11171081,
CC ECO:0000269|PubMed:11240126, ECO:0000269|PubMed:12134158,
CC ECO:0000269|PubMed:8657152, ECO:0000269|PubMed:8662907,
CC ECO:0000269|PubMed:9808620}.
CC -!- INTERACTION:
CC Q14185; O15084: ANKRD28; NbExp=4; IntAct=EBI-446740, EBI-359567;
CC Q14185; P46108: CRK; NbExp=4; IntAct=EBI-446740, EBI-886;
CC Q14185; Q9H7D0-1: DOCK5; NbExp=2; IntAct=EBI-446740, EBI-25409131;
CC Q14185; Q92556: ELMO1; NbExp=17; IntAct=EBI-446740, EBI-346417;
CC Q14185; P62993: GRB2; NbExp=5; IntAct=EBI-446740, EBI-401755;
CC Q14185; P63000: RAC1; NbExp=10; IntAct=EBI-446740, EBI-413628;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}.
CC Note=Recruited to membranes via its interaction with
CC phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, lung, kidney,
CC pancreas and ovary. Expressed at intermediate level in thymus, testes
CC and colon.
CC -!- DOMAIN: The DOCKER domain is necessary and sufficient for the GEF
CC activity.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; D50857; BAA09454.1; -; mRNA.
DR EMBL; AL157711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL607029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS73222.1; -.
DR RefSeq; NP_001371.1; NM_001380.4.
DR PDB; 3L4C; X-ray; 2.37 A; A/B=422-619.
DR PDBsum; 3L4C; -.
DR AlphaFoldDB; Q14185; -.
DR BMRB; Q14185; -.
DR SMR; Q14185; -.
DR BioGRID; 108128; 55.
DR CORUM; Q14185; -.
DR DIP; DIP-29391N; -.
DR IntAct; Q14185; 26.
DR MINT; Q14185; -.
DR STRING; 9606.ENSP00000280333; -.
DR ChEMBL; CHEMBL4523288; -.
DR iPTMnet; Q14185; -.
DR PhosphoSitePlus; Q14185; -.
DR BioMuta; DOCK1; -.
DR DMDM; 209572608; -.
DR EPD; Q14185; -.
DR jPOST; Q14185; -.
DR MassIVE; Q14185; -.
DR MaxQB; Q14185; -.
DR PaxDb; Q14185; -.
DR PeptideAtlas; Q14185; -.
DR PRIDE; Q14185; -.
DR ProteomicsDB; 59903; -.
DR Antibodypedia; 3822; 289 antibodies from 41 providers.
DR DNASU; 1793; -.
DR Ensembl; ENST00000280333.9; ENSP00000280333.6; ENSG00000150760.13.
DR GeneID; 1793; -.
DR KEGG; hsa:1793; -.
DR UCSC; uc001ljt.4; human.
DR CTD; 1793; -.
DR DisGeNET; 1793; -.
DR GeneCards; DOCK1; -.
DR HGNC; HGNC:2987; DOCK1.
DR HPA; ENSG00000150760; Low tissue specificity.
DR MIM; 601403; gene.
DR neXtProt; NX_Q14185; -.
DR OpenTargets; ENSG00000150760; -.
DR PharmGKB; PA27453; -.
DR VEuPathDB; HostDB:ENSG00000150760; -.
DR eggNOG; KOG1998; Eukaryota.
DR GeneTree; ENSGT00940000154974; -.
DR HOGENOM; CLU_000595_2_1_1; -.
DR InParanoid; Q14185; -.
DR OrthoDB; 102580at2759; -.
DR PhylomeDB; Q14185; -.
DR TreeFam; TF300423; -.
DR PathwayCommons; Q14185; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q14185; -.
DR SIGNOR; Q14185; -.
DR BioGRID-ORCS; 1793; 14 hits in 316 CRISPR screens.
DR ChiTaRS; DOCK1; human.
DR EvolutionaryTrace; Q14185; -.
DR GeneWiki; Dock180; -.
DR GenomeRNAi; 1793; -.
DR Pharos; Q14185; Tbio.
DR PRO; PR:Q14185; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14185; protein.
DR Bgee; ENSG00000150760; Expressed in corpus callosum and 189 other tissues.
DR ExpressionAtlas; Q14185; baseline and differential.
DR Genevisible; Q14185; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:WormBase.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc.
DR GO; GO:0007520; P:myoblast fusion; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; TAS:ProtInc.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1270.350; -; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
DR InterPro; IPR027357; DOCKER_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; PTHR45653; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Guanine-nucleotide releasing factor;
KW Membrane; Phagocytosis; Phosphoprotein; Reference proteome; SH3 domain;
KW SH3-binding.
FT CHAIN 1..1865
FT /note="Dedicator of cytokinesis protein 1"
FT /id="PRO_0000189984"
FT DOMAIN 9..70
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 425..609
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1207..1617
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1619..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1695
FT /note="Phosphoinositide-binding"
FT /evidence="ECO:0000255"
FT REGION 1732..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1819
FT /note="Interaction with NCK2 second and third SH3 domain
FT (minor)"
FT REGION 1820..1836
FT /note="Interaction with NCK2 third SH3 domain (major)"
FT REGION 1837..1852
FT /note="Interaction with NCK2 (minor)"
FT MOTIF 1799..1805
FT /note="SH3-binding; interaction with CRK"
FT /evidence="ECO:0000255"
FT MOTIF 1838..1843
FT /note="SH3-binding; interaction with CRK"
FT /evidence="ECO:0000255"
FT COMPBIAS 1633..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1767
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1772
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT MOD_RES 1858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUR4"
FT VARIANT 1793
FT /note="A -> T (in dbSNP:rs869801)"
FT /id="VAR_059971"
FT MUTAGEN 1401..1402
FT /note="YI->AA: Abolishes Rac GEF activity."
FT /evidence="ECO:0000269|PubMed:12134158"
FT MUTAGEN 1487..1489
FT /note="ISP->AAA: Abolishes Rac GEF activity."
FT /evidence="ECO:0000269|PubMed:12134158"
FT CONFLICT 1857
FT /note="A -> T (in Ref. 1; BAA09454)"
FT /evidence="ECO:0000305"
FT STRAND 426..436
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 528..537
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 546..555
FT /evidence="ECO:0007829|PDB:3L4C"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:3L4C"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:3L4C"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:3L4C"
FT STRAND 595..608
FT /evidence="ECO:0007829|PDB:3L4C"
SQ SEQUENCE 1865 AA; 215346 MW; 940C5AFD047EBEDE CRC64;
MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF
PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS TIWRQLYVQD NREMFRSVRH
MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS
TISLFRAHEI ASKQVEERLQ EEKSQKQNID INRQAKFAAT PSLALFVNLK NVVCKIGEDA
EVLMSLYDPV ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
IVRVGRMELR DNNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQPVAGENDF
LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP HLVDRTTAVA RKTGFPEIIM
PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS
VIYYQVKQPR WFETVKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD
GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKAELEEK GHSATGKSMQ SLGSCTISKD
SFQISTLVCS TKLTQNVDLL GLLKWRSNTS LLQQNLRQLM KVDGGEVVKF LQDTLDALFN
IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLK
NYVDGAEKPG VNEQLYKAMK ALESIFKFIV RSRILFNQLY ENKGEADFVE SLLQLFRSIN
DMMSSMSDQT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTEFILNVPM GLLTIQKLYC
LIEIVHSDLF TQHDCREILL PMMTDQLKYH LERQEDLEAC CQLLSHILEV LYRKDVGPTQ
RHVQIIMEKL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD
VVDFLMETFI MFKNLIGKNV YPFDWVIMNM VQNKVFLRAI NQYADMLNKK FLDQANFELQ
LWNNYFHLAV AFLTQESLQL ENFSSAKRAK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF
IPEMVGPILE MTLIPETELR KATIPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR
GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKENRMSCT
VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS EDVCVAHLTQ
RDGYQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYENEMFD YEQLSELLKK
QAQFYENIVK VIRPKPDYFA VGYYGQGFPT FLRGKVFIYR GKEYERREDF EARLLTQFPN
AEKMKTTSPP GDDIKNSPGQ YIQCFTVKPK LDLPPKFHRP VSEQIVSFYR VNEVQRFEYS
RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
NDKINSMVQQ HLDDPSLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY LQEHPEAHEK
IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLKEKVEK EYGVRIMPSS
LDDRRGSRPR SMVRSFTMPS SSRPLSVASV SSLSSDSTPS RPGSDGFALE PLLPKKMHSR
SQDKLDKDDL EKEKKDKKKE KRNSKHQEIF EKEFKPTDIS LQQSEAVILS ETISPLRPQR
PKSQVMNVIG SERRFSVSPS SPSSQQTPPP VTPRAKLSFS MQSSLELNGM TGADVADVPP
PLPLKGSVAD YGNLMENQDL LGSPTPPPPP PHQRHLPPPL PSKTPPPPPP KTTRKQASVD
SGIVQ
