MTA1_HUMAN
ID MTA1_HUMAN Reviewed; 715 AA.
AC Q13330; A5PLK4; Q86SW2; Q8NFI8; Q96GI8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Metastasis-associated protein MTA1;
GN Name=MTA1;
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 LONG), AND VARIANT THR-612.
RX PubMed=8083195; DOI=10.1016/s0021-9258(17)31603-4;
RA Toh Y., Pencil S.D., Nicolson G.L.;
RT "A novel candidate metastasis-associated gene, mta1, differentially
RT expressed in highly metastatic mammary adenocarcinoma cell lines. cDNA
RT cloning, expression, and protein analyses.";
RL J. Biol. Chem. 269:22958-22963(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT THR-612.
RX PubMed=7607577; DOI=10.1016/0378-1119(94)00410-t;
RA Toh Y., Pencil S.D., Nicolson G.L.;
RT "Analysis of the complete sequence of the novel metastasis-associated
RT candidate gene, mta1, differentially expressed in mammary adenocarcinoma
RT and breast cancer cell lines.";
RL Gene 159:97-104(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND SUBCELLULAR LOCATION.
RC TISSUE=Mammary gland;
RX PubMed=12167865; DOI=10.1038/nature00889;
RA Kumar R., Wang R.-A., Mazumdar A., Talukder A.H., Mandal M., Yang Z.,
RA Bagheri-Yarmand R., Sahin A., Hortobagyi G., Adam L., Barnes C.J.,
RA Vadlamudi R.K.;
RT "A naturally occurring MTA1 variant sequesters oestrogen receptor-alpha in
RT the cytoplasm.";
RL Nature 418:654-657(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT THR-612.
RC TISSUE=Brain;
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 10-299 (ISOFORM 3).
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION IN NURD COMPLEX.
RX PubMed=9885572; DOI=10.1016/s1097-2765(00)80299-3;
RA Xue Y., Wong J., Moreno G.T., Young M.K., Cote J., Wang W.;
RT "NURD, a novel complex with both ATP-dependent chromatin-remodeling and
RT histone deacetylase activities.";
RL Mol. Cell 2:851-861(1998).
RN [8]
RP INTERACTION WITH ITGB3BP.
RX PubMed=15254226; DOI=10.1128/mcb.24.15.6581-6591.2004;
RA Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R.;
RT "Metastasis-associated protein 1 interacts with NRIF3, an estrogen-
RT inducible nuclear receptor coregulator.";
RL Mol. Cell. Biol. 24:6581-6591(2004).
RN [9]
RP PHOSPHORYLATION BY CSNK1G2/CK1, INTERACTION WITH CSNK1G2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15077195; DOI=10.1038/sj.onc.1207569;
RA Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.;
RT "Metastatic tumor antigen 1 short form (MTA1s) associates with casein
RT kinase I-gamma2, an estrogen-responsive kinase.";
RL Oncogene 23:4422-4429(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND THR-564, 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT LYS-626,
RP MUTAGENESIS OF LYS-626, AND INTERACTION WITH EP300.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [13]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [14]
RP FUNCTION, INTERACTION WITH HDAC2, ACETYLATION AT LYS-626, AND MUTAGENESIS
RP OF LYS-626.
RX PubMed=17671180; DOI=10.1158/0008-5472.can-07-0750;
RA Balasenthil S., Gururaj A.E., Talukder A.H., Bagheri-Yarmand R.,
RA Arrington T., Haas B.J., Braisted J.C., Kim I., Lee N.H., Kumar R.;
RT "Identification of Pax5 as a target of MTA1 in B-cell lymphomas.";
RL Cancer Res. 67:7132-7138(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP FUNCTION.
RX PubMed=17922032; DOI=10.1038/sj.onc.1210839;
RA Molli P.R., Singh R.R., Lee S.W., Kumar R.;
RT "MTA1-mediated transcriptional repression of BRCA1 tumor suppressor gene.";
RL Oncogene 27:1971-1980(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; SER-522;
RP THR-564 AND SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP FUNCTION, AND INTERACTION WITH MDM2 AND TP53.
RX PubMed=19837670; DOI=10.1074/jbc.m109.056499;
RA Li D.Q., Divijendra Natha Reddy S., Pakala S.B., Wu X., Zhang Y.,
RA Rayala S.K., Kumar R.;
RT "MTA1 coregulator regulates p53 stability and function.";
RL J. Biol. Chem. 284:34545-34552(2009).
RN [21]
RP UBIQUITINATION AT LYS-182 AND LYS-626, ACETYLATION AT LYS-626, MUTAGENESIS
RP OF LYS-182 AND LYS-626, AND INTERACTION WITH COP1 AND HDAC2.
RX PubMed=19805145; DOI=10.1073/pnas.0908027106;
RA Li D.Q., Ohshiro K., Reddy S.D., Pakala S.B., Lee M.H., Zhang Y.,
RA Rayala S.K., Kumar R.;
RT "E3 ubiquitin ligase COP1 regulates the stability and functions of MTA1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17493-17498(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-522; THR-564;
RP SER-576 AND THR-578, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP INTERACTION WITH SIX3.
RX PubMed=20682799; DOI=10.1158/0008-5472.can-10-0909;
RA Kumar R., Balasenthil S., Manavathi B., Rayala S.K., Pakala S.B.;
RT "Metastasis-associated protein 1 and its short form variant stimulates Wnt1
RT transcription through promoting its derepression from Six3 corepressor.";
RL Cancer Res. 70:6649-6658(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449;
RP SER-522; SER-576 AND THR-578, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [25]
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 [26]
RP FUNCTION, SUMOYLATION AT LYS-509, SUBCELLULAR LOCATION, INTERACTION WITH
RP HDAC2; UBE2I; PIAS1; PIAS3; PIAS4; SUMO1; SUMO2; SENP1 AND SENP2, SUMO
RP INTERACTION MOTIF, AND MUTAGENESIS OF LYS-509 AND 711-ILE--ILE-713.
RX PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449;
RP SER-522; SER-576; THR-578 AND SER-639, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP REVIEW.
RX PubMed=22253283; DOI=10.1158/0008-5472.can-11-2345;
RA Li D.Q., Pakala S.B., Nair S.S., Eswaran J., Kumar R.;
RT "Metastasis-associated protein 1/nucleosome remodeling and histone
RT deacetylase complex in cancer.";
RL Cancer Res. 72:387-394(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; SER-522;
RP THR-564 AND SER-576, 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 [30]
RP INTERACTION WITH NACC2.
RX PubMed=22926524; DOI=10.1038/onc.2012.386;
RA Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z.,
RA Shang Y.;
RT "RBB, a novel transcription repressor, represses the transcription of HDM2
RT oncogene.";
RL Oncogene 32:3711-3721(2013).
RN [31]
RP FUNCTION, INTERACTION WITH TFAP2C AND IFI16, AND SUBCELLULAR LOCATION.
RX PubMed=24413532; DOI=10.1158/0008-5472.can-13-2020;
RA Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA Kim Y.N., Seong J.K., Lee M.O.;
RT "Differential regulation of estrogen receptor alpha expression in breast
RT cancer cells by metastasis-associated protein 1.";
RL Cancer Res. 74:1484-1494(2014).
RN [32]
RP 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 [33]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TPR AND
RP HDAC2.
RX PubMed=24970816; DOI=10.18632/oncotarget.2095;
RA Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
RA Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
RT "The subcellular distribution and function of MTA1 in cancer
RT differentiation.";
RL Oncotarget 5:5153-5164(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-549, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [35]
RP INTERACTION WITH PWWP2A.
RX PubMed=30327463; DOI=10.1038/s41467-018-06665-5;
RA Link S., Spitzer R.M.M., Sana M., Torrado M., Voelker-Albert M.C.,
RA Keilhauer E.C., Burgold T., Puenzeler S., Low J.K.K., Lindstroem I.,
RA Nist A., Regnard C., Stiewe T., Hendrich B., Imhof A., Mann M.,
RA Mackay J.P., Bartkuhn M., Hake S.B.;
RT "PWWP2A binds distinct chromatin moieties and interacts with an MTA1-
RT specific core NuRD complex.";
RL Nat. Commun. 9:4300-4300(2018).
CC -!- FUNCTION: Transcriptional coregulator which can act as both a
CC transcriptional corepressor and coactivator. As a part of the histone-
CC deacetylase multiprotein complex (NuRD), regulates transcription of its
CC targets by modifying the acetylation status of the target chromatin and
CC cofactor accessibility to the target DNA. In conjunction with other
CC components of NuRD, acts as a transcriptional corepressor of BRCA1,
CC ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3,
CC PAX5 and SUMO2, independent of the NuRD complex. Stimulates the
CC expression of WNT1 by inhibiting the expression of its transcriptional
CC corepressor SIX3. Regulates p53-dependent and -independent DNA repair
CC processes following genotoxic stress. Regulates the stability and
CC function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2
CC thereby regulating the p53-dependent DNA repair. Plays an important
CC role in tumorigenesis, tumor invasion, and metastasis. Involved in the
CC epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C,
CC IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of
CC the circadian clock and is essential for the generation and maintenance
CC of circadian rhythms under constant light and for normal entrainment of
CC behavior to light-dark (LD) cycles. Positively regulates the CLOCK-
CC ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own
CC transcription and the transcription of CRY1. Regulates deacetylation of
CC ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing
CC CRY1-mediated transcription repression. Isoform Short binds to ESR1 and
CC sequesters it in the cytoplasm and enhances its non-genomic responses.
CC With TFCP2L1, promotes establishment and maintenance of pluripotency in
CC embryonic stem cells (ESCs) and inhibits endoderm differentiation (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4B0,
CC ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180,
CC ECO:0000269|PubMed:17922032, ECO:0000269|PubMed:19837670,
CC ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24413532}.
CC -!- SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase
CC multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR.
CC Binds to CSNK1G2 in the cytoplasm. Interacts with NACC2. Interacts with
CC ARNTL/BMAL1 and CLOCK. Interacts with EP300, TFAP2C, IFI16, TPR, HDAC2,
CC UBE2I/UBC9, PIAS1, PIAS3, PIAS4, p53/TP53, MDM2, COP1, SUMO1, SUMO2,
CC SENP1 and SENP2. Interacts with SIX3; facilitates the binding of SIX3
CC to the core DNA motif of SIX3 promoter (By similarity). Interacts with
CC TFCP2L1; which is indispensable for TFCP2L1-mediated self-renewal-
CC promoting effect and endoderm-inhibiting action (By similarity).
CC Interacts with PWWP2A (PubMed:30327463). Interacts with PWWP2B (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4B0,
CC ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:15254226,
CC ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180,
CC ECO:0000269|PubMed:19805145, ECO:0000269|PubMed:19837670,
CC ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:22926524, ECO:0000269|PubMed:24413532,
CC ECO:0000269|PubMed:24970816, ECO:0000269|PubMed:30327463,
CC ECO:0000269|PubMed:9885572}.
CC -!- INTERACTION:
CC Q13330; Q8N726: CDKN2A; NbExp=2; IntAct=EBI-714236, EBI-625922;
CC Q13330; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-714236, EBI-3867333;
CC Q13330; Q96KQ7: EHMT2; NbExp=9; IntAct=EBI-714236, EBI-744366;
CC Q13330; Q13547: HDAC1; NbExp=12; IntAct=EBI-714236, EBI-301834;
CC Q13330; Q92769: HDAC2; NbExp=6; IntAct=EBI-714236, EBI-301821;
CC Q13330; Q16665: HIF1A; NbExp=6; IntAct=EBI-714236, EBI-447269;
CC Q13330; Q13422: IKZF1; NbExp=3; IntAct=EBI-714236, EBI-745305;
CC Q13330; P05412: JUN; NbExp=4; IntAct=EBI-714236, EBI-852823;
CC Q13330; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-714236, EBI-742808;
CC Q13330; O00505: KPNA3; NbExp=3; IntAct=EBI-714236, EBI-358297;
CC Q13330; O00629: KPNA4; NbExp=4; IntAct=EBI-714236, EBI-396343;
CC Q13330; Q15323: KRT31; NbExp=3; IntAct=EBI-714236, EBI-948001;
CC Q13330; Q6A162: KRT40; NbExp=4; IntAct=EBI-714236, EBI-10171697;
CC Q13330; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-714236, EBI-10171774;
CC Q13330; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-714236, EBI-741037;
CC Q13330; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-714236, EBI-10178634;
CC Q13330; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-714236, EBI-945833;
CC Q13330; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-714236, EBI-22310682;
CC Q13330; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-714236, EBI-79165;
CC Q13330; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-714236, EBI-949255;
CC Q13330; Q09028: RBBP4; NbExp=10; IntAct=EBI-714236, EBI-620823;
CC Q13330; P21673: SAT1; NbExp=3; IntAct=EBI-714236, EBI-711613;
CC Q13330; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-714236, EBI-10173690;
CC Q13330; Q99961: SH3GL1; NbExp=3; IntAct=EBI-714236, EBI-697911;
CC Q13330; O60315: ZEB2; NbExp=12; IntAct=EBI-714236, EBI-717614;
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Nucleus. Nucleus envelope.
CC Cytoplasm. Cytoplasm, cytoskeleton. Note=Associated with microtubules.
CC Localization at the nuclear envelope is TPR-dependent.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=Q13330-1; Sequence=Displayed;
CC Name=Short; Synonyms=MTA1S;
CC IsoId=Q13330-2; Sequence=VSP_001601, VSP_001602;
CC Name=3;
CC IsoId=Q13330-3; Sequence=VSP_042207;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in brain, liver,
CC kidney, and cardiac muscle, ovaries, adrenal glands and virgin mammary
CC glands. Higher in tumors than in adjacent normal tissue from the same
CC individual. Up-regulated in a wide variety of cancers including breast,
CC liver, ovarian, and colorectal cancer and its expression levels are
CC closely correlated with tumor aggressiveness and metastasis.
CC {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:24970816}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in metastatic cells.
CC -!- DOMAIN: Isoform Short contains a Leu-Arg-Ile-Leu-Leu motif (ER binding
CC motif).
CC -!- PTM: Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances
CC corepression of estrogen receptor (ER). {ECO:0000269|PubMed:15077195}.
CC -!- PTM: Acetylation is essential for its transcriptional coactivator
CC activity. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17671180,
CC ECO:0000269|PubMed:19805145}.
CC -!- PTM: Sumoylation positively regulates its transcriptional corepressor
CC activity but does not affect the protein stability. Sumoylated
CC preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by
CC PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of
CC PIAS1/3/4. Desumoylated by SENP1. {ECO:0000269|PubMed:21965678}.
CC -!- PTM: Ubiquitinated by COP1, which leads to proteasomal degradation.
CC {ECO:0000269|PubMed:19805145}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MTA1ID41443ch14q32.html";
CC ---------------------------------------------------------------------------
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DR EMBL; U35113; AAA78935.1; -; mRNA.
DR EMBL; AF508978; AAN01613.1; -; mRNA.
DR EMBL; AL928654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009443; AAH09443.2; -; mRNA.
DR EMBL; BC142941; AAI42942.1; -; mRNA.
DR EMBL; BX248776; CAD66583.1; -; mRNA.
DR CCDS; CCDS32169.1; -. [Q13330-1]
DR CCDS; CCDS55954.1; -. [Q13330-2]
DR RefSeq; NP_001190187.1; NM_001203258.1. [Q13330-2]
DR RefSeq; NP_004680.2; NM_004689.3. [Q13330-1]
DR PDB; 4BKX; X-ray; 3.00 A; A=162-335.
DR PDB; 4PBY; X-ray; 2.50 A; C/D=656-686.
DR PDB; 4PBZ; X-ray; 2.15 A; B=670-695.
DR PDB; 4PC0; X-ray; 2.50 A; C/D=670-711.
DR PDB; 5FXY; X-ray; 3.20 A; B/D/F/H=464-546.
DR PDB; 5ICN; X-ray; 3.30 A; A=162-354.
DR PDB; 6G16; X-ray; 2.80 A; B/D/F/H=464-546.
DR PDB; 6ZRC; X-ray; 2.60 A; P/Q=677-689.
DR PDB; 6ZRD; X-ray; 2.50 A; P/Q=677-689.
DR PDB; 7AO8; EM; 4.50 A; A/D=1-715.
DR PDB; 7AO9; EM; 6.10 A; A/D=1-715.
DR PDB; 7AOA; EM; 19.40 A; A/D=1-715.
DR PDBsum; 4BKX; -.
DR PDBsum; 4PBY; -.
DR PDBsum; 4PBZ; -.
DR PDBsum; 4PC0; -.
DR PDBsum; 5FXY; -.
DR PDBsum; 5ICN; -.
DR PDBsum; 6G16; -.
DR PDBsum; 6ZRC; -.
DR PDBsum; 6ZRD; -.
DR PDBsum; 7AO8; -.
DR PDBsum; 7AO9; -.
DR PDBsum; 7AOA; -.
DR AlphaFoldDB; Q13330; -.
DR SMR; Q13330; -.
DR BioGRID; 114562; 223.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q13330; -.
DR DIP; DIP-41751N; -.
DR IntAct; Q13330; 101.
DR MINT; Q13330; -.
DR STRING; 9606.ENSP00000333633; -.
DR GlyGen; Q13330; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13330; -.
DR PhosphoSitePlus; Q13330; -.
DR BioMuta; MTA1; -.
DR DMDM; 259016275; -.
DR CPTAC; CPTAC-1619; -.
DR EPD; Q13330; -.
DR jPOST; Q13330; -.
DR MassIVE; Q13330; -.
DR MaxQB; Q13330; -.
DR PaxDb; Q13330; -.
DR PeptideAtlas; Q13330; -.
DR PRIDE; Q13330; -.
DR ProteomicsDB; 59317; -. [Q13330-1]
DR ProteomicsDB; 59318; -. [Q13330-2]
DR ProteomicsDB; 59319; -. [Q13330-3]
DR ABCD; Q13330; 1 sequenced antibody.
DR Antibodypedia; 90; 437 antibodies from 37 providers.
DR DNASU; 9112; -.
DR Ensembl; ENST00000331320.12; ENSP00000333633.7; ENSG00000182979.18. [Q13330-1]
DR Ensembl; ENST00000405646.5; ENSP00000384180.1; ENSG00000182979.18. [Q13330-3]
DR Ensembl; ENST00000438610.5; ENSP00000393438.1; ENSG00000182979.18. [Q13330-2]
DR GeneID; 9112; -.
DR KEGG; hsa:9112; -.
DR MANE-Select; ENST00000331320.12; ENSP00000333633.7; NM_004689.4; NP_004680.2.
DR UCSC; uc001yqx.4; human. [Q13330-1]
DR CTD; 9112; -.
DR DisGeNET; 9112; -.
DR GeneCards; MTA1; -.
DR HGNC; HGNC:7410; MTA1.
DR HPA; ENSG00000182979; Low tissue specificity.
DR MIM; 603526; gene.
DR neXtProt; NX_Q13330; -.
DR OpenTargets; ENSG00000182979; -.
DR PharmGKB; PA31218; -.
DR VEuPathDB; HostDB:ENSG00000182979; -.
DR eggNOG; KOG3554; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR HOGENOM; CLU_006585_2_1_1; -.
DR InParanoid; Q13330; -.
DR OMA; HEWLILT; -.
DR OrthoDB; 802091at2759; -.
DR PhylomeDB; Q13330; -.
DR TreeFam; TF106444; -.
DR PathwayCommons; Q13330; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q13330; -.
DR SIGNOR; Q13330; -.
DR BioGRID-ORCS; 9112; 17 hits in 1100 CRISPR screens.
DR ChiTaRS; MTA1; human.
DR GeneWiki; MTA1; -.
DR GenomeRNAi; 9112; -.
DR Pharos; Q13330; Tbio.
DR PRO; PR:Q13330; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13330; protein.
DR Bgee; ENSG00000182979; Expressed in right uterine tube and 203 other tissues.
DR ExpressionAtlas; Q13330; baseline and differential.
DR Genevisible; Q13330; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR IDEAL; IID00563; -.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR035170; MTA1_R1.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF17226; MTA_R1; 2.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Biological rhythms; Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..715
FT /note="Metastasis-associated protein MTA1"
FT /id="PRO_0000083493"
FT DOMAIN 1..164
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 165..276
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 283..335
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 393..420
FT /note="GATA-type; atypical"
FT REGION 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 545..552
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 696..705
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 711..715
FT /note="SUMO interaction motif 1 (SIM); crucial for
FT efficient sumoylation"
FT COMPBIAS 694..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 626
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16617102,
FT ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19805145"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2 and SUMO3)"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:19805145"
FT VAR_SEQ 64..81
FT /note="TLSVCYKAGPGADNGEEG -> R (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_042207"
FT VAR_SEQ 398..430
FT /note="TTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGL -> MSSLRILLDILEEIW
FT WLENANPVRWREARTKPQ (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12167865"
FT /id="VSP_001601"
FT VAR_SEQ 431..715
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12167865"
FT /id="VSP_001602"
FT VARIANT 372
FT /note="V -> I (in dbSNP:rs4983413)"
FT /id="VAR_055847"
FT VARIANT 612
FT /note="A -> T (in dbSNP:rs13707)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7607577, ECO:0000269|PubMed:8083195"
FT /id="VAR_058965"
FT MUTAGEN 182
FT /note="K->A: Reduced ubiquitination. Significant reduction
FT in ubiquitination; when associated with A-626."
FT /evidence="ECO:0000269|PubMed:19805145"
FT MUTAGEN 509
FT /note="K->R: Reduced sumoylation and transcriptional
FT corepressor activity."
FT /evidence="ECO:0000269|PubMed:21965678"
FT MUTAGEN 626
FT /note="K->A: Loss of acetylation and transcriptional
FT coactivator activity. Reduced ubiquitination. Significant
FT reduction in ubiquitination; when associated with A-182."
FT /evidence="ECO:0000269|PubMed:16617102,
FT ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145"
FT MUTAGEN 711..713
FT /note="IVI->AAA: Significant loss of interaction with SUMO1
FT and SUMO2 and reduced transcriptional corepressor
FT activity."
FT /evidence="ECO:0000269|PubMed:21965678"
FT CONFLICT 498
FT /note="H -> N (in Ref. 1; AAA78935)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="P -> R (in Ref. 5; AAI42942)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="D -> G (in Ref. 1; AAA78935)"
FT /evidence="ECO:0000305"
FT CONFLICT 661..662
FT /note="AT -> PK (in Ref. 1; AAA78935)"
FT /evidence="ECO:0000305"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 505..514
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:6G16"
FT HELIX 674..680
FT /evidence="ECO:0007829|PDB:4PBZ"
SQ SEQUENCE 715 AA; 80786 MW; 2D5330F0489AE62E CRC64;
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD ISSTLIALAD
KHATLSVCYK AGPGADNGEE GEIEEEMENP EMVDLPEKLK HQLRHRELFL SRQLESLPAT
HIRGKCSVTL LNETESLKSY LEREDFFFYS LVYDPQQKTL LADKGEIRVG NRYQADITDL
LKEGEEDGRD QSRLETQVWE AHNPLTDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM
SAAAASRDIT LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL
EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK LKQVYIPNYN
KPNPNQISVN NVKAGVVNGT GAPGQSPGAG RACESCYTTQ SYQWYSWGPP NMQCRLCASC
WTYWKKYGGL KMPTRLDGER PGPNRSNMSP HGLPARSSGS PKFAMKTRQA FYLHTTKLTR
IARRLCREIL RPWHAARHPY LPINSAAIKA ECTARLPEAS QSPLVLKQAV RKPLEAVLRY
LETHPRPPKP DPVKSVSSVL SSLTPAKVAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL
MPSRGLANHG QARHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW IDAPDDVFYM
ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPPRP PPPAPVNDEP IVIED
