SIN3B_MOUSE
ID SIN3B_MOUSE Reviewed; 1098 AA.
AC Q62141; O54976; Q6A013; Q8VCB8; Q8VDZ5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Paired amphipathic helix protein Sin3b;
DE AltName: Full=Histone deacetylase complex subunit Sin3b;
DE AltName: Full=Transcriptional corepressor Sin3b;
GN Name=Sin3b; Synonyms=Kiaa0700;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryonic kidney;
RX PubMed=7889570; DOI=10.1016/0092-8674(95)90355-0;
RA Ayer D.E., Lawrence Q.A., Eisenman R.N.;
RT "Mad-Max transcriptional repression is mediated by ternary complex
RT formation with mammalian homologs of yeast repressor Sin3.";
RL Cell 80:767-776(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP FOXK1.
RC TISSUE=Heart;
RX PubMed=10620510; DOI=10.1042/bj3450335;
RA Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S.;
RT "The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta)
RT forms a co-repressor complex with mammalian Sin3B.";
RL Biochem. J. 345:335-343(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Mammary gland, and Salivary gland;
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 [5]
RP INTERACTION WITH MAD3 AND MAD4.
RX PubMed=8521822; DOI=10.1002/j.1460-2075.1995.tb00252.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RT "Mad3 and Mad4: novel Max-interacting transcriptional repressors that
RT suppress c-myc dependent transformation and are expressed during neural and
RT epidermal differentiation.";
RL EMBO J. 14:5646-5659(1995).
RN [6]
RP ERRATUM OF PUBMED:8521822.
RX PubMed=8617250; DOI=10.1002/j.1460-2075.1996.tb00555.x;
RA Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
RA Copeland N.G., Jenkins N.A., Eisenman R.N.;
RL EMBO J. 15:2030-2030(1996).
RN [7]
RP INTERACTION WITH NCOR1.
RX PubMed=9139820; DOI=10.1038/387043a0;
RA Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D.,
RA Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E.,
RA Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.;
RT "A complex containing N-CoR, mSin3 and histone deacetylase mediates
RT transcriptional repression.";
RL Nature 387:43-48(1997).
RN [8]
RP INTERACTION WITH SAP30.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [9]
RP INTERACTION WITH SUDS3 AND HDAC1.
RX PubMed=11909966; DOI=10.1128/mcb.22.8.2743-2750.2002;
RA Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr.,
RA Chen K., DePinho R.A.;
RT "Identification of mammalian Sds3 as an integral component of the
RT Sin3/histone deacetylase corepressor complex.";
RL Mol. Cell. Biol. 22:2743-2750(2002).
RN [10]
RP INTERACTION WITH SETDB1.
RX PubMed=12398767; DOI=10.1042/bj20020854;
RA Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT "An ERG (ets-related gene)-associated histone methyltransferase interacts
RT with histone deacetylases 1/2 and transcription co-repressors mSin3A/B.";
RL Biochem. J. 369:651-657(2003).
RN [11]
RP INTERACTION WITH CRY1.
RX PubMed=15226430; DOI=10.1128/mcb.24.14.6278-6287.2004;
RA Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.;
RT "Circadian and light-induced transcription of clock gene Per1 depends on
RT histone acetylation and deacetylation.";
RL Mol. Cell. Biol. 24:6278-6287(2004).
RN [12]
RP INTERACTION WITH MAEL.
RX PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A.,
RA Cooke H.J.;
RT "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT chromatin and microRNA pathway?";
RL Hum. Mol. Genet. 15:2324-2334(2006).
RN [13]
RP INTERACTION WITH RNF220, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=20170641; DOI=10.1016/j.bbrc.2010.02.066;
RA Kong Q., Zeng W., Wu J., Hu W., Li C., Mao B.;
RT "RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination.";
RL Biochem. Biophys. Res. Commun. 393:708-713(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-670, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION, AND INTERACTION WITH FOXK1.
RX PubMed=22476904; DOI=10.1007/s11010-012-1302-2;
RA Shi X., Garry D.J.;
RT "Sin3 interacts with Foxk1 and regulates myogenic progenitors.";
RL Mol. Cell. Biochem. 366:251-258(2012).
RN [16]
RP INTERACTION WITH MYT1L.
RX PubMed=28379941; DOI=10.1038/nature21722;
RA Mall M., Kareta M.S., Chanda S., Ahlenius H., Perotti N., Zhou B.,
RA Grieder S.D., Ge X., Drake S., Euong Ang C., Walker B.M., Vierbuchen T.,
RA Fuentes D.R., Brennecke P., Nitta K.R., Jolma A., Steinmetz L.M.,
RA Taipale J., Suedhof T.C., Wernig M.;
RT "Myt1l safeguards neuronal identity by actively repressing many non-
RT neuronal fates.";
RL Nature 544:245-249(2017).
RN [17]
RP STRUCTURE BY NMR OF 148-232 IN COMPLEX WITH MAD1.
RX PubMed=11101889; DOI=10.1038/81944;
RA Spronk C.A.E., Tessari M., Kaan A.M., Jansen J.F.A., Vermeulen M.,
RA Stunnenberg H.G., Vuister G.W.;
RT "The Mad1-Sin3B interaction involves a novel helical fold.";
RL Nat. Struct. Biol. 7:1100-1104(2000).
RN [18]
RP STRUCTURE BY NMR OF 31-107 IN COMPLEX WITH REST, AND INTERACTION WITH REST.
RX PubMed=16288918; DOI=10.1016/j.jmb.2005.10.008;
RA Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.;
RT "The neural repressor NRSF/REST binds the PAH1 domain of the Sin3
RT corepressor by using its distinct short hydrophobic helix.";
RL J. Mol. Biol. 354:903-915(2005).
RN [19]
RP STRUCTURE BY NMR OF 32-100.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first PAH domain of the mouse transcriptional
RT repressor SIN3B.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to
CC repress MYC responsive genes and antagonize MYC oncogenic activities.
CC Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer
CC then represses transcription by tethering SIN3B to DNA. Also forms a
CC complex with FOXK1 which represses transcription. With FOXK1, regulates
CC cell cycle progression probably by repressing cell cycle inhibitor
CC genes expression (PubMed:22476904). {ECO:0000269|PubMed:10620510,
CC ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:7889570}.
CC -!- SUBUNIT: Interacts with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30.
CC Interaction with SUDS3 enhances the interaction with HDAC1 to form a
CC complex. Interacts with CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and
CC SETDB1. Interacts with MYT1L (PubMed:28379941). Interacts with C6orf89
CC (By similarity). {ECO:0000250|UniProtKB:O75182,
CC ECO:0000269|PubMed:10620510, ECO:0000269|PubMed:11101889,
CC ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12398767,
CC ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:16288918,
CC ECO:0000269|PubMed:16787967, ECO:0000269|PubMed:20170641,
CC ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:28379941,
CC ECO:0000269|PubMed:7889570, ECO:0000269|PubMed:8521822,
CC ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9702189}.
CC -!- INTERACTION:
CC Q62141; Q6PDX6: Rnf220; NbExp=5; IntAct=EBI-591450, EBI-2795840;
CC Q62141; Q8BR65: Suds3; NbExp=5; IntAct=EBI-591450, EBI-591431;
CC Q62141; P01106: MYC; Xeno; NbExp=8; IntAct=EBI-591450, EBI-447544;
CC Q62141-2; P42128: Foxk1; NbExp=11; IntAct=EBI-591466, EBI-878270;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810,
CC ECO:0000269|PubMed:20170641, ECO:0000269|PubMed:7889570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q62141-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q62141-1; Sequence=VSP_014187;
CC Name=2;
CC IsoId=Q62141-2; Sequence=VSP_008225, VSP_008226, VSP_014187;
CC Name=3;
CC IsoId=Q62141-3; Sequence=VSP_008227, VSP_008228, VSP_014187;
CC -!- PTM: Ubiquitinated by RNF220 that leads to proteasomal degradation.
CC {ECO:0000269|PubMed:20170641}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32283.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L38622; AAA69774.1; -; mRNA.
DR EMBL; AF038848; AAC04821.1; -; mRNA.
DR EMBL; AK173005; BAD32283.1; ALT_INIT; mRNA.
DR EMBL; BC020049; AAH20049.1; -; mRNA.
DR EMBL; BC021160; AAH21160.1; -; mRNA.
DR CCDS; CCDS52598.1; -. [Q62141-2]
DR CCDS; CCDS52599.1; -. [Q62141-4]
DR PIR; I61714; I61714.
DR RefSeq; NP_001106719.1; NM_001113248.2. [Q62141-2]
DR RefSeq; NP_033214.2; NM_009188.4. [Q62141-4]
DR PDB; 1E91; NMR; -; A=148-232.
DR PDB; 1PD7; NMR; -; A=148-232.
DR PDB; 2CR7; NMR; -; A=32-98.
DR PDB; 2CZY; NMR; -; A=31-107.
DR PDB; 2F05; NMR; -; A=148-252.
DR PDB; 5Y95; NMR; -; A=32-98.
DR PDBsum; 1E91; -.
DR PDBsum; 1PD7; -.
DR PDBsum; 2CR7; -.
DR PDBsum; 2CZY; -.
DR PDBsum; 2F05; -.
DR PDBsum; 5Y95; -.
DR AlphaFoldDB; Q62141; -.
DR SMR; Q62141; -.
DR BioGRID; 203257; 22.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR CORUM; Q62141; -.
DR DIP; DIP-470N; -.
DR IntAct; Q62141; 8.
DR MINT; Q62141; -.
DR STRING; 10090.ENSMUSP00000004494; -.
DR ChEMBL; CHEMBL4105761; -.
DR iPTMnet; Q62141; -.
DR PhosphoSitePlus; Q62141; -.
DR MaxQB; Q62141; -.
DR PaxDb; Q62141; -.
DR PeptideAtlas; Q62141; -.
DR PRIDE; Q62141; -.
DR ProteomicsDB; 261368; -. [Q62141-4]
DR ProteomicsDB; 261369; -. [Q62141-1]
DR ProteomicsDB; 261370; -. [Q62141-2]
DR ProteomicsDB; 261371; -. [Q62141-3]
DR Antibodypedia; 27459; 245 antibodies from 26 providers.
DR DNASU; 20467; -.
DR Ensembl; ENSMUST00000004494; ENSMUSP00000004494; ENSMUSG00000031622. [Q62141-4]
DR Ensembl; ENSMUST00000109950; ENSMUSP00000105576; ENSMUSG00000031622. [Q62141-2]
DR Ensembl; ENSMUST00000212095; ENSMUSP00000148407; ENSMUSG00000031622. [Q62141-3]
DR GeneID; 20467; -.
DR KEGG; mmu:20467; -.
DR UCSC; uc009mgp.3; mouse. [Q62141-4]
DR CTD; 23309; -.
DR MGI; MGI:107158; Sin3b.
DR VEuPathDB; HostDB:ENSMUSG00000031622; -.
DR eggNOG; KOG4204; Eukaryota.
DR GeneTree; ENSGT00940000159560; -.
DR HOGENOM; CLU_001360_0_1_1; -.
DR InParanoid; Q62141; -.
DR OMA; MRWFFGT; -.
DR OrthoDB; 253485at2759; -.
DR PhylomeDB; Q62141; -.
DR TreeFam; TF106187; -.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 20467; 12 hits in 79 CRISPR screens.
DR ChiTaRS; Sin3b; mouse.
DR EvolutionaryTrace; Q62141; -.
DR PRO; PR:Q62141; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q62141; protein.
DR Bgee; ENSMUSG00000031622; Expressed in placenta labyrinth and 267 other tissues.
DR ExpressionAtlas; Q62141; baseline and differential.
DR Genevisible; Q62141; MM.
DR GO; GO:0030849; C:autosome; IDA:MGI.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IBA:GO_Central.
DR GO; GO:0000805; C:X chromosome; IDA:MGI.
DR GO; GO:0001741; C:XY body; IDA:UniProtKB.
DR GO; GO:0000806; C:Y chromosome; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0048738; P:cardiac muscle tissue development; IDA:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
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; IDA:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IDA:UniProtKB.
DR Gene3D; 1.20.1160.11; -; 3.
DR IDEAL; IID50092; -.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1098
FT /note="Paired amphipathic helix protein Sin3b"
FT /id="PRO_0000121540"
FT DOMAIN 30..100
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 145..230
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 283..360
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..299
FT /note="Interaction with CRY1"
FT /evidence="ECO:0000269|PubMed:15226430"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..98
FT /note="Interaction with REST"
FT /evidence="ECO:0000269|PubMed:16288918"
FT REGION 238..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..499
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000269|PubMed:9139820"
FT REGION 383..550
FT /note="Interaction with SUDS3 and HDAC1"
FT /evidence="ECO:0000269|PubMed:11909966"
FT REGION 661..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 275..302
FT /note="KKMKLRGTKDLSIAAVGKYGTLQEFSFF -> VLVHVWVLPAHGRSGVEAQA
FT AGEPEARA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008227"
FT VAR_SEQ 275..293
FT /note="KKMKLRGTKDLSIAAVGKY -> VGLQLKCAVVWFGYCTAEE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10620510,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008225"
FT VAR_SEQ 294..954
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10620510,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008226"
FT VAR_SEQ 303..954
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008228"
FT VAR_SEQ 955..1098
FT /note="Missing (in isoform 1, isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10620510,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7889570"
FT /id="VSP_014187"
FT CONFLICT 230
FT /note="A -> G (in Ref. 2; AAC04821)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="S -> P (in Ref. 2; AAC04821)"
FT /evidence="ECO:0000305"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:2CR7"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2CZY"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:2CR7"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2CR7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2CR7"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2CR7"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2CZY"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:1E91"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2F05"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:1E91"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1E91"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:1E91"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2F05"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1E91"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2F05"
SQ SEQUENCE 1098 AA; 126405 MW; A73F6DFC11EBA256 CRC64;
MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE
IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ
DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE
ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS
CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKKKMKLR GTKDLSIAAV GKYGTLQEFS
FFDKVRRVLK SQEVYENFLR CIALFNQELV SGSELLQLVS PFLGKFPELF AQFKSFLGVK
ELSFAPPMSD RSGDGISREI DYASCKRIGS SYRALPKTYQ QPKCSGRTAI CKEVLNDTWV
SFPSWSEDST FVSSKKTPYE EQLHRCEDER FELDVVLETN LATIRVLESV QKKLSRMAPE
DQEKLRLDDC LGGTSEVIQR RAIHRIYGDK APEVIESLKR NPATAVPVVL KRLKAKEEEW
REAQQGFNKI WREQYEKAYL KSLDHQAVNF KQNDTKALRS KSLLNEIESV YDEHQEQHSE
GRSAPSSEPH LIFVYEDRQI LEDAAALISY YVKRQPAIQK EDQGTIRQLL HRFLPSLFFS
QQCPGTSDDS ADERDRDRDS AEPERRRPTD EKPPADASPE PPKVLDDVYS LFFANNNWYF
FLRLHQTLCA RLLKIYRQAQ KQLLEHRREQ EREQLLCEGR REKAADPAME LRLKQPSEVE
LEEYYPAFLD MVRSLLEGSI DPTQYEDTLR EMFTIHAYIG FTMDKLVQNI ARQLHHLVSD
DVCLKVVELY LNEQQRGAAG GNLSSRCVRA ARETSYQWKA ERCMADENCF KVMFLQRRGQ
VIMTIELLDT EEAQTEDPVE VQHLARYVEQ YVGSEGASSS STEGFLLKPV FLQRNLKKFR
RWQCEQVRAM RGEAKSSWKR LMGVESACDV DCRFRLGTHK MVFIVNSEDY MYRRGTLCRA
KQVQPLVLLR HHRHFEEWHG RWLEDNVTVA AAGLVQDWLM GEEEEDMVPC KTLCETAHVH
GLPVTRYRVQ YSRRPASP
