COBL1_HUMAN
ID COBL1_HUMAN Reviewed; 1128 AA.
AC Q53SF7; A6NMZ3; Q6IQ33; Q7Z3I6; Q9BRH4; Q9UG88; Q9Y2I3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cordon-bleu protein-like 1 {ECO:0000305};
GN Name=COBLL1 {ECO:0000312|HGNC:HGNC:23571}; Synonyms=KIAA0977;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Ovary, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1128 (ISOFORM 4).
RC TISSUE=Fetal brain, and Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND THR-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; THR-260; SER-441;
RP SER-821; SER-911 AND SER-917, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-1121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; THR-284; SER-344;
RP SER-356 AND SER-917, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-222; SER-256;
RP THR-260; SER-344; SER-438; SER-441; SER-786; SER-814; SER-821; SER-911 AND
RP SER-917, AND IDENTIFICATION BY 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).
RN [13]
RP STRUCTURE BY NMR OF 144-222.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the novel identified ubiquitin-like domain in the
RT human COBL-like 1 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=4;
CC IsoId=Q53SF7-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53SF7-2; Sequence=VSP_060296;
CC Name=3;
CC IsoId=Q53SF7-3; Sequence=VSP_060297, VSP_060298;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06264.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAA76821.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023194; BAA76821.2; ALT_INIT; mRNA.
DR EMBL; AK225849; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC019181; AAX93068.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11340.1; -; Genomic_DNA.
DR EMBL; BC006264; AAH06264.1; ALT_SEQ; mRNA.
DR EMBL; BC071588; AAH71588.1; -; mRNA.
DR EMBL; AL049939; CAB43215.1; -; mRNA.
DR EMBL; BX537877; CAD97877.2; -; mRNA.
DR CCDS; CCDS2223.2; -. [Q53SF7-3]
DR CCDS; CCDS63045.1; -. [Q53SF7-4]
DR PIR; T08673; T08673.
DR RefSeq; NP_001265387.1; NM_001278458.1.
DR RefSeq; NP_001265389.1; NM_001278460.1.
DR RefSeq; NP_001265390.1; NM_001278461.1. [Q53SF7-4]
DR RefSeq; NP_055715.3; NM_014900.4. [Q53SF7-3]
DR PDB; 2DAJ; NMR; -; A=144-221.
DR PDBsum; 2DAJ; -.
DR AlphaFoldDB; Q53SF7; -.
DR BMRB; Q53SF7; -.
DR SMR; Q53SF7; -.
DR BioGRID; 116511; 45.
DR CORUM; Q53SF7; -.
DR IntAct; Q53SF7; 28.
DR MINT; Q53SF7; -.
DR STRING; 9606.ENSP00000341360; -.
DR iPTMnet; Q53SF7; -.
DR PhosphoSitePlus; Q53SF7; -.
DR BioMuta; COBLL1; -.
DR EPD; Q53SF7; -.
DR jPOST; Q53SF7; -.
DR MassIVE; Q53SF7; -.
DR MaxQB; Q53SF7; -.
DR PaxDb; Q53SF7; -.
DR PeptideAtlas; Q53SF7; -.
DR PRIDE; Q53SF7; -.
DR ProteomicsDB; 62537; -. [Q53SF7-2]
DR ProteomicsDB; 62538; -. [Q53SF7-3]
DR ProteomicsDB; 62539; -. [Q53SF7-4]
DR Antibodypedia; 33758; 159 antibodies from 18 providers.
DR DNASU; 22837; -.
DR Ensembl; ENST00000342193.8; ENSP00000341360.4; ENSG00000082438.18. [Q53SF7-3]
DR Ensembl; ENST00000375458.6; ENSP00000364607.2; ENSG00000082438.18. [Q53SF7-4]
DR Ensembl; ENST00000652658.2; ENSP00000498242.1; ENSG00000082438.18. [Q53SF7-4]
DR GeneID; 22837; -.
DR KEGG; hsa:22837; -.
DR MANE-Select; ENST00000652658.2; ENSP00000498242.1; NM_001365672.2; NP_001352601.1.
DR UCSC; uc002ucp.5; human. [Q53SF7-4]
DR CTD; 22837; -.
DR DisGeNET; 22837; -.
DR GeneCards; COBLL1; -.
DR HGNC; HGNC:23571; COBLL1.
DR HPA; ENSG00000082438; Tissue enhanced (liver).
DR MIM; 610318; gene.
DR neXtProt; NX_Q53SF7; -.
DR OpenTargets; ENSG00000082438; -.
DR PharmGKB; PA134990267; -.
DR VEuPathDB; HostDB:ENSG00000082438; -.
DR eggNOG; KOG3751; Eukaryota.
DR GeneTree; ENSGT00530000063608; -.
DR HOGENOM; CLU_003305_0_0_1; -.
DR InParanoid; Q53SF7; -.
DR OrthoDB; 986623at2759; -.
DR PhylomeDB; Q53SF7; -.
DR TreeFam; TF333490; -.
DR PathwayCommons; Q53SF7; -.
DR SignaLink; Q53SF7; -.
DR BioGRID-ORCS; 22837; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; COBLL1; human.
DR EvolutionaryTrace; Q53SF7; -.
DR GeneWiki; COBLL1; -.
DR GenomeRNAi; 22837; -.
DR Pharos; Q53SF7; Tbio.
DR PRO; PR:Q53SF7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53SF7; protein.
DR Bgee; ENSG00000082438; Expressed in sural nerve and 195 other tissues.
DR ExpressionAtlas; Q53SF7; baseline and differential.
DR Genevisible; Q53SF7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR InterPro; IPR039895; COBL-like.
DR InterPro; IPR019025; Cordon-bleu_ubiquitin_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR21557; PTHR21557; 1.
DR Pfam; PF09469; Cobl; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1128
FT /note="Cordon-bleu protein-like 1"
FT /id="PRO_0000260493"
FT DOMAIN 1081..1101
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 291..296
FT /note="KKRRAP 1"
FT MOTIF 360..365
FT /note="KKRRAP 2"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMF0"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1
FT /note="M -> MCGRAAEAAASSRTPGREMGQAVTRRLGAGARAAPRRAM (in
FT isoform 2)"
FT /id="VSP_060296"
FT VAR_SEQ 409
FT /note="A -> ETFHPGLSSQEQCTAPKLMEETSVFECPGTPEAAITSLTS (in
FT isoform 3)"
FT /id="VSP_060297"
FT VAR_SEQ 519
FT /note="Missing (in isoform 3)"
FT /id="VSP_060298"
FT CONFLICT 330
FT /note="T -> A (in Ref. 5; AAH71588)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="T -> G (in Ref. 6; CAB43215)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="M -> T (in Ref. 6; CAD97877)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="K -> E (in Ref. 5; AAH71588)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="T -> A (in Ref. 6; CAD97877)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="S -> G (in Ref. 6; CAB43215)"
FT /evidence="ECO:0000305"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2DAJ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2DAJ"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2DAJ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2DAJ"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:2DAJ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2DAJ"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:2DAJ"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2DAJ"
SQ SEQUENCE 1128 AA; 123868 MW; B0BC3812F4BA93E8 CRC64;
MDGRTPRPQD APARRKPKAK APLPPAETKY TDVSSAADSV ESTAFIMEQK ENMIDKDVEL
SVVLPGDIIK STTVHGSKPM MDLLIFLCAQ YHLNPSSYTI DLLSAEQNHI KFKPNTPIGM
LEVEKVILKP KMLDKKKPTP IIPEKTVRVV INFKKTQKTI VRVSPHASLQ ELAPIICSKC
EFDPLHTLLL KDYQSQEPLD LTKSLNDLGL RELYAMDVNR ESCQISQNLD IMKEKENKGF
FSFFQRSKKK RDQTASAPAT PLVNKHRPTF TRSNTISKPY ISNTLPSDAP KKRRAPLPPM
PASQSVPQDL AHIQERPASC IVKSMSVDET DKSPCEAGRV RAGSLQLSSM SAGNSSLRRT
KRKAPSPPSK IPPHQSDENS RVTALQPVDG VPPDSASEAN SPEELSSPAG ISSDYSLEEI
DEKEELSEVP KVEAENISPK SQDIPFVSTD IINTLKNDPD SALGNGSGEF SQNSMEEKQE
TKSTDGQEPH SVVYDTSNGK KVVDSIRNLK SLGPNQENVV QNEIIVYPEN TEDNMKNGVK
KTEINVEGVA KNNNIDMEVE RPSNSEAHET DTAISYKENH LAASSVPDQK LNQPSAEKTK
DAAIQTTPSC NSFDGKHQDH NLSDSKVEEC VQTSNNNIST QHSCLSSQDS VNTSREFRSQ
GTLIIHSEDP LTVKDPICAH GNDDLLPPVD RIDKNSTASY LKNYPLYRQD YNPKPKPSNE
ITREYIPKIG MTTYKIVPPK SLEISKDWQS ETIEYKDDQD MHALGKKHTH ENVKETAIQT
EDSAISESPE EPLPNLKPKP NLRTEHQVPS SVSSPDDAMV SPLKPAPKMT RDTGTAPFAP
NLEEINNILE SKFKSRASNA QAKPSSFFLQ MQKRVSGHYV TSAAAKSVHA APNPAPKELT
NKEAERDMLP SPEQTLSPLS KMPHSVPQPL VEKTDDDVIG QAPAEASPPP IAPKPVTIPA
SQVSTQNLKT LKTFGAPRPY SSSGPSPFAL AVVKRSQSFS KERTESPSAS ALVQPPANTE
EGKTHSVNKF VDIPQLGVSD KENNSAHNEQ NSQIPTPTDG PSFTVMRQSS LTFQSSDPEQ
MRQSLLTAIR SGEAAAKLKR VTIPSNTISV NGRSRLSHSM SPDAQDGH
