DOK1_HUMAN
ID DOK1_HUMAN Reviewed; 481 AA.
AC Q99704; O43204; Q53TY2; Q9UHG6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Docking protein 1;
DE AltName: Full=Downstream of tyrosine kinase 1;
DE AltName: Full=p62(dok);
DE AltName: Full=pp62;
GN Name=DOK1;
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] (ISOFORM 1), AND PHOSPHORYLATION AT TYROSINE
RP RESIDUES.
RX PubMed=9008160; DOI=10.1016/s0092-8674(00)81840-1;
RA Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R.,
RA Stillman B., Clarkson B.;
RT "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein
RT in chronic myelogenous leukemia progenitor cells.";
RL Cell 88:197-204(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10940083; DOI=10.1046/j.1365-2370.2000.00203.x;
RA Hubert P., Ferreira V., Debre P., Bismuth G.;
RT "Molecular cloning of a truncated p62Dok1 isoform, p22Dokdel.";
RL Eur. J. Immunogenet. 27:145-148(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PHOSPHORYLATION AT TYR-362 AND TYR-398, AND MUTAGENESIS OF TYR-362 AND
RP TYR-398.
RX PubMed=11551902; DOI=10.1074/jbc.m102116200;
RA Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.;
RT "Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362
RT and 398 plays distinct roles for binding GTPase-activating protein and Nck
RT and is essential for inhibiting insulin-stimulated activation of Ras and
RT Akt.";
RL J. Biol. Chem. 276:42843-42850(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12595900; DOI=10.1038/sj.gene.6363891;
RA Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.;
RT "DOK4 and DOK5: new Dok-related genes expressed in human T cells.";
RL Genes Immun. 4:40-45(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-362; TYR-377; TYR-398 AND
RP TYR-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, 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 [11]
RP SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), AND ACETYLATION
RP AT MET-1 (ISOFORM 3).
RX PubMed=19481542; DOI=10.1016/j.febslet.2009.05.042;
RA Kobayashi R., Patenia R., Ashizawa S., Vykoukal J.;
RT "Targeted mass spectrometric analysis of N-terminally truncated isoforms
RT generated via alternative translation initiation.";
RL FEBS Lett. 583:2441-2445(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-341 AND TYR-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRMS.
RX PubMed=23822091; DOI=10.1111/febs.12420;
RA Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.;
RT "The unique N-terminal region of SRMS regulates enzymatic activity and
RT phosphorylation of its novel substrate Dok1.";
RL FEBS J. 280:4539-4559(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-269 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 152-256, FUNCTION, AND INTERACTION
RP WITH ITGB3.
RX PubMed=18156175; DOI=10.1074/jbc.m709435200;
RA Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D.,
RA Wegener K.L.;
RT "An integrin phosphorylation switch: the effect of beta3 integrin tail
RT phosphorylation on Dok1 and talin binding.";
RL J. Biol. Chem. 283:5420-5426(2008).
CC -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding
CC proteins. They provide a docking platform for the assembly of
CC multimolecular signaling complexes. DOK1 appears to be a negative
CC regulator of the insulin signaling pathway. Modulates integrin
CC activation by competing with talin for the same binding site on ITGB3.
CC {ECO:0000269|PubMed:18156175}.
CC -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with RasGAP and
CC INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3. Interacts
CC with SRMS (via the SH2 and SH3 domains). {ECO:0000250,
CC ECO:0000269|PubMed:18156175, ECO:0000269|PubMed:23822091}.
CC -!- INTERACTION:
CC Q99704; P04626: ERBB2; NbExp=2; IntAct=EBI-1384360, EBI-641062;
CC Q99704; Q9H3Y6: SRMS; NbExp=7; IntAct=EBI-1384360, EBI-8541270;
CC Q99704; Q9JIY2: Cbll1; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-7644904;
CC Q99704; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=p62Dok1;
CC IsoId=Q99704-1; Sequence=Displayed;
CC Name=2; Synonyms=p22Dokdel;
CC IsoId=Q99704-2; Sequence=VSP_003852, VSP_003853;
CC Name=3; Synonyms=p44Dok;
CC IsoId=Q99704-3; Sequence=VSP_038224;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, heart, leukocyte and spleen.
CC Expressed in both resting and activated peripheral blood T-cells.
CC Expressed in breast cancer. {ECO:0000269|PubMed:12595900}.
CC -!- DOMAIN: The PTB domain mediates receptor interaction.
CC -!- PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC (By
CC similarity). Phosphorylated by LYN (By similarity). Phosphorylated on
CC tyrosine residues by the insulin receptor kinase. Results in the
CC negative regulation of the insulin signaling pathway. Phosphorylated on
CC tyrosine residues by SRMS. {ECO:0000250, ECO:0000269|PubMed:11551902,
CC ECO:0000269|PubMed:23822091, ECO:0000269|PubMed:9008160}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met-
CC 140 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR EMBL; U70987; AAC51127.1; -; mRNA.
DR EMBL; AF180527; AAF19167.1; -; mRNA.
DR EMBL; AF035299; AAB88182.1; -; mRNA.
DR EMBL; AC005033; AAX93224.1; -; Genomic_DNA.
DR EMBL; BC114440; AAI14441.1; -; mRNA.
DR CCDS; CCDS1954.1; -. [Q99704-1]
DR CCDS; CCDS56125.1; -. [Q99704-3]
DR CCDS; CCDS82474.1; -. [Q99704-2]
DR RefSeq; NP_001184189.1; NM_001197260.1. [Q99704-3]
DR RefSeq; NP_001305797.1; NM_001318868.1. [Q99704-2]
DR RefSeq; NP_001372.1; NM_001381.4. [Q99704-1]
DR PDB; 2V76; X-ray; 1.60 A; A/B/C/D=152-256.
DR PDBsum; 2V76; -.
DR AlphaFoldDB; Q99704; -.
DR BMRB; Q99704; -.
DR SMR; Q99704; -.
DR BioGRID; 108131; 42.
DR ELM; Q99704; -.
DR IntAct; Q99704; 30.
DR MINT; Q99704; -.
DR STRING; 9606.ENSP00000233668; -.
DR iPTMnet; Q99704; -.
DR PhosphoSitePlus; Q99704; -.
DR BioMuta; DOK1; -.
DR DMDM; 17366642; -.
DR EPD; Q99704; -.
DR jPOST; Q99704; -.
DR MassIVE; Q99704; -.
DR MaxQB; Q99704; -.
DR PaxDb; Q99704; -.
DR PeptideAtlas; Q99704; -.
DR PRIDE; Q99704; -.
DR ProteomicsDB; 78413; -. [Q99704-1]
DR ProteomicsDB; 78414; -. [Q99704-2]
DR ProteomicsDB; 78415; -. [Q99704-3]
DR Antibodypedia; 3784; 892 antibodies from 42 providers.
DR DNASU; 1796; -.
DR Ensembl; ENST00000233668.10; ENSP00000233668.5; ENSG00000115325.14. [Q99704-1]
DR Ensembl; ENST00000340004.6; ENSP00000344330.6; ENSG00000115325.14. [Q99704-2]
DR Ensembl; ENST00000409429.5; ENSP00000387016.1; ENSG00000115325.14. [Q99704-3]
DR GeneID; 1796; -.
DR KEGG; hsa:1796; -.
DR MANE-Select; ENST00000233668.10; ENSP00000233668.5; NM_001381.5; NP_001372.1.
DR UCSC; uc002smr.4; human. [Q99704-1]
DR CTD; 1796; -.
DR DisGeNET; 1796; -.
DR GeneCards; DOK1; -.
DR HGNC; HGNC:2990; DOK1.
DR HPA; ENSG00000115325; Low tissue specificity.
DR MIM; 602919; gene.
DR neXtProt; NX_Q99704; -.
DR OpenTargets; ENSG00000115325; -.
DR PharmGKB; PA27456; -.
DR VEuPathDB; HostDB:ENSG00000115325; -.
DR eggNOG; KOG4047; Eukaryota.
DR GeneTree; ENSGT00940000155980; -.
DR HOGENOM; CLU_056741_0_0_1; -.
DR InParanoid; Q99704; -.
DR OMA; ALYSQVH; -.
DR PhylomeDB; Q99704; -.
DR TreeFam; TF324994; -.
DR PathwayCommons; Q99704; -.
DR Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-HSA-8853659; RET signaling.
DR SignaLink; Q99704; -.
DR SIGNOR; Q99704; -.
DR BioGRID-ORCS; 1796; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; DOK1; human.
DR EvolutionaryTrace; Q99704; -.
DR GeneWiki; DOK1; -.
DR GenomeRNAi; 1796; -.
DR Pharos; Q99704; Tbio.
DR PRO; PR:Q99704; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q99704; protein.
DR Bgee; ENSG00000115325; Expressed in tendon of biceps brachii and 203 other tissues.
DR ExpressionAtlas; Q99704; baseline and differential.
DR Genevisible; Q99704; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR037751; Dok1/2/3_PTB.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..481
FT /note="Docking protein 1"
FT /id="PRO_0000187268"
FT DOMAIN 4..119
FT /note="PH"
FT DOMAIN 151..259
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 270..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 296
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 341
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 362
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000269|PubMed:11551902,
FT ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332"
FT MOD_RES 377
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 398
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000269|PubMed:11551902,
FT ECO:0007744|PubMed:15592455"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 449
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038224"
FT VAR_SEQ 153..177
FT /note="SQFWVTVQRTEAAERCGLHGSYVLR -> HVLFRGRPPLPLRPWNLHLPDGT
FT GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10940083"
FT /id="VSP_003852"
FT VAR_SEQ 178..481
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10940083"
FT /id="VSP_003853"
FT MUTAGEN 362
FT /note="Y->F: No association with NCK. No association with
FT GAP; when associated with F-398."
FT /evidence="ECO:0000269|PubMed:11551902"
FT MUTAGEN 398
FT /note="Y->F: No association with GAP; when associated with
FT F-362."
FT /evidence="ECO:0000269|PubMed:11551902"
FT CONFLICT 1..20
FT /note="MDGAVMEGPLFLQSQRFGTK -> RLPAQASATREREPRWSPFQ (in
FT Ref. 3; AAB88182)"
FT /evidence="ECO:0000305"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2V76"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:2V76"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:2V76"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2V76"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:2V76"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:2V76"
FT MOD_RES Q99704-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:19481542"
SQ SEQUENCE 481 AA; 52392 MW; E9D947831244BA6C CRC64;
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS GGGRGSSRRL
DCKVIRLAEC VSVAPVTVET PPEPGATAFR LDTAQRSHLL AADAPSSAAW VQTLCRNAFP
KGSWTLAPTD NPPKLSALEM LENSLYSPTW EGSQFWVTVQ RTEAAERCGL HGSYVLRVEA
ERLTLLTVGA QSQILEPLLS WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND
IFQAVETAIH RQKAQGKAGQ GHDVLRADSH EGEVAEGKLP SPPGPQELLD SPPALYAEPL
DSLRIAPCPS QDSLYSDPLD STSAQAGEGV QRKKPLYWDL YEHAQQQLLK AKLTDPKEDP
IYDEPEGLAP VPPQGLYDLP REPKDAWWCQ ARVKEEGYEL PYNPATDDYA VPPPRSTKPL
LAPKPQGPAF PEPGTATGSG IKSHNSALYS QVQKSGASGS WDCGLSRVGT DKTGVKSEGS
T
