ID   SIN3B_HUMAN             Reviewed;        1162 AA.
AC   O75182; Q2NL91; Q68GC2; Q6P4B8; Q8TB34; Q9BSC8;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 192.
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 {ECO:0000312|HGNC:HGNC:19354}; Synonyms=KIAA0700;
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] {ECO:0000305, ECO:0000312|EMBL:AAU01916.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ali M., Batra H., Saluja D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAU01916.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAH05113.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 743-1162 (ISOFORMS 1/2).
RC   TISSUE=Duodenum {ECO:0000312|EMBL:AAH63531.1}, Lung
RC   {ECO:0000312|EMBL:AAH05113.1}, Lymph, and Skin
RC   {ECO:0000312|EMBL:AAH25026.1};
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   [5] {ECO:0000305}
RP   INTERACTION WITH HCFC1.
RX   PubMed=12670868; DOI=10.1101/gad.252103;
RA   Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT   "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT   methyltransferase are tethered together selectively by the cell-
RT   proliferation factor HCF-1.";
RL   Genes Dev. 17:896-911(2003).
RN   [6]
RP   IDENTIFICATION BY 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   [7]
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   [8]
RP   FUNCTION, AND IDENTIFICATION IN THE SIN3B COMPLEX.
RX   PubMed=21041482; DOI=10.1128/mcb.00840-10;
RA   Jelinic P., Pellegrino J., David G.;
RT   "A novel mammalian complex containing Sin3B mitigates histone acetylation
RT   and RNA polymerase II progression within transcribed loci.";
RL   Mol. Cell. Biol. 31:54-62(2011).
RN   [9]
RP   INTERACTION WITH C6ORF89.
RC   TISSUE=Adipocyte;
RX   PubMed=23460338; DOI=10.1002/jcp.24355;
RA   Lalioti V.S., Vergarajauregui S., Villasante A., Pulido D., Sandoval I.V.;
RT   "C6orf89 encodes three distinct HDAC enhancers that function in the
RT   nucleolus, the Golgi and the midbody.";
RL   J. Cell. Physiol. 228:1907-1921(2013).
RN   [10] {ECO:0007744|PDB:8BPA, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC, ECO:0007744|PDB:8C60}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH HDAC2;
RP   PHF12 AND MORF4L1, IDENTIFICATION IN THE SIN3B COMPLEX, AND FUNCTION.
RX   PubMed=37137925; DOI=10.1038/s41467-023-38276-0;
RA   Wan M.S.M., Muhammad R., Koliopoulos M.G., Roumeliotis T.I.,
RA   Choudhary J.S., Alfieri C.;
RT   "Mechanism of assembly, activation and lysine selection by the SIN3B
RT   histone deacetylase complex.";
RL   Nat. Commun. 14:2556-2556(2023).
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. As part of the SIN3B complex represses transcription
CC       and counteracts the histone acetyltransferase activity of EP300 through
CC       the recognition H3K27ac marks by PHF12 and the activity of the histone
CC       deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited
CC       downstream of the constitutively active genes transcriptional start
CC       sites through interaction with histones and mitigates histone
CC       acetylation and RNA polymerase II progression within transcribed
CC       regions contributing to the regulation of transcription
CC       (PubMed:21041482). {ECO:0000250|UniProtKB:Q62141,
CC       ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:37137925}.
CC   -!- SUBUNIT: Component of the SIN3B complex, which includes SIN3B, HDAC2 or
CC       HDAC1, PHF12 and MORF4L1 (PubMed:37137925, PubMed:21041482). Interacts
CC       with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30. Interaction with SUDS3
CC       enhances the interaction with HDAC1 to form a complex. Interacts with
CC       CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and SETDB1. Interacts with
CC       C6orf89 (PubMed:23460338). Interacts with MYT1L (By similarity).
CC       {ECO:0000250|UniProtKB:Q62141, ECO:0000269|PubMed:12670868,
CC       ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:23460338,
CC       ECO:0000269|PubMed:37137925}.
CC   -!- INTERACTION:
CC       O75182; P01106: MYC; NbExp=7; IntAct=EBI-540462, EBI-447544;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long;
CC         IsoId=O75182-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:9734811};
CC         IsoId=O75182-2; Sequence=VSP_014186;
CC       Name=3 {ECO:0000269|PubMed:15489334};
CC         IsoId=O75182-3; Sequence=VSP_014185;
CC   -!- PTM: Ubiquitinated by RNF220 that leads to proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31675.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY706204; AAU01916.1; -; mRNA.
DR   EMBL; AB014600; BAA31675.2; ALT_INIT; mRNA.
DR   EMBL; CH471106; EAW84565.1; -; Genomic_DNA.
DR   EMBL; BC005113; AAH05113.1; -; mRNA.
DR   EMBL; BC025026; AAH25026.1; -; mRNA.
DR   EMBL; BC063531; AAH63531.1; -; mRNA.
DR   EMBL; BC110821; AAI10822.1; -; mRNA.
DR   CCDS; CCDS32946.1; -. [O75182-1]
DR   CCDS; CCDS74308.1; -. [O75182-2]
DR   RefSeq; NP_001284524.1; NM_001297595.1. [O75182-2]
DR   RefSeq; NP_001284526.1; NM_001297597.1.
DR   RefSeq; NP_056075.1; NM_015260.3. [O75182-1]
DR   PDB; 8BPA; EM; 3.70 A; A=1-1162.
DR   PDB; 8BPB; EM; 2.80 A; A=1-1162.
DR   PDB; 8BPC; EM; 2.80 A; A=1-1162.
DR   PDB; 8C60; EM; 3.40 A; A=1-1162.
DR   PDBsum; 8BPA; -.
DR   PDBsum; 8BPB; -.
DR   PDBsum; 8BPC; -.
DR   PDBsum; 8C60; -.
DR   AlphaFoldDB; O75182; -.
DR   EMDB; EMD-16147; -.
DR   EMDB; EMD-16148; -.
DR   EMDB; EMD-16149; -.
DR   EMDB; EMD-16449; -.
DR   SMR; O75182; -.
DR   BioGRID; 116901; 139.
DR   ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR   CORUM; O75182; -.
DR   IntAct; O75182; 42.
DR   MINT; O75182; -.
DR   STRING; 9606.ENSP00000369131; -.
DR   GlyGen; O75182; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O75182; -.
DR   PhosphoSitePlus; O75182; -.
DR   BioMuta; SIN3B; -.
DR   EPD; O75182; -.
DR   jPOST; O75182; -.
DR   MassIVE; O75182; -.
DR   MaxQB; O75182; -.
DR   PaxDb; 9606-ENSP00000369131; -.
DR   PeptideAtlas; O75182; -.
DR   ProteomicsDB; 49855; -. [O75182-1]
DR   ProteomicsDB; 49856; -. [O75182-2]
DR   ProteomicsDB; 49857; -. [O75182-3]
DR   Pumba; O75182; -.
DR   Antibodypedia; 27459; 264 antibodies from 26 providers.
DR   DNASU; 23309; -.
DR   Ensembl; ENST00000248054.10; ENSP00000248054.4; ENSG00000127511.10. [O75182-2]
DR   Ensembl; ENST00000379803.5; ENSP00000369131.1; ENSG00000127511.10. [O75182-1]
DR   Ensembl; ENST00000596802.5; ENSP00000473039.1; ENSG00000127511.10. [O75182-3]
DR   GeneID; 23309; -.
DR   KEGG; hsa:23309; -.
DR   MANE-Select; ENST00000248054.10; ENSP00000248054.4; NM_001297595.2; NP_001284524.1. [O75182-2]
DR   UCSC; uc002new.4; human. [O75182-1]
DR   AGR; HGNC:19354; -.
DR   CTD; 23309; -.
DR   DisGeNET; 23309; -.
DR   GeneCards; SIN3B; -.
DR   HGNC; HGNC:19354; SIN3B.
DR   HPA; ENSG00000127511; Low tissue specificity.
DR   MalaCards; SIN3B; -.
DR   MIM; 607777; gene.
DR   neXtProt; NX_O75182; -.
DR   OpenTargets; ENSG00000127511; -.
DR   Orphanet; 500166; SIN3A-related intellectual disability syndrome due to a point mutation.
DR   PharmGKB; PA134909030; -.
DR   VEuPathDB; HostDB:ENSG00000127511; -.
DR   eggNOG; KOG4204; Eukaryota.
DR   GeneTree; ENSGT00940000159560; -.
DR   HOGENOM; CLU_001360_0_1_1; -.
DR   InParanoid; O75182; -.
DR   OMA; DHAIHYV; -.
DR   OrthoDB; 199155at2759; -.
DR   PhylomeDB; O75182; -.
DR   TreeFam; TF106187; -.
DR   PathwayCommons; O75182; -.
DR   Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha. [O75182-1]
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-HSA-9707564; Cytoprotection by HMOX1. [O75182-1]
DR   SignaLink; O75182; -.
DR   SIGNOR; O75182; -.
DR   BioGRID-ORCS; 23309; 46 hits in 1175 CRISPR screens.
DR   ChiTaRS; SIN3B; human.
DR   GeneWiki; SIN3B; -.
DR   GenomeRNAi; 23309; -.
DR   Pharos; O75182; Tbio.
DR   PRO; PR:O75182; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O75182; Protein.
DR   Bgee; ENSG00000127511; Expressed in body of uterus and 176 other cell types or tissues.
DR   ExpressionAtlas; O75182; baseline and differential.
DR   GO; GO:0030849; C:autosome; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0000805; C:X chromosome; IEA:Ensembl.
DR   GO; GO:0001741; C:XY body; IEA:Ensembl.
DR   GO; GO:0000806; C:Y chromosome; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.20.1160.11; Paired amphipathic helix; 3.
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:SF1; PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B; 1.
DR   PANTHER; PTHR12346; SIN3B-RELATED; 1.
DR   Pfam; PF02671; PAH; 3.
DR   Pfam; PF08295; Sin3_corepress; 2.
DR   Pfam; PF16879; Sin3a_C; 1.
DR   SMART; SM00761; HDAC_interact; 1.
DR   SUPFAM; SSF47762; PAH2 domain; 3.
DR   PROSITE; PS51477; PAH; 3.
DR   Genevisible; O75182; HS.
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..1162
FT                   /note="Paired amphipathic helix protein Sin3b"
FT                   /id="PRO_0000121539"
FT   DOMAIN          37..107
FT                   /note="PAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT   DOMAIN          153..238
FT                   /note="PAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT   DOMAIN          292..369
FT                   /note="PAH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT   REGION          1..308
FT                   /note="Interaction with CRY1"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..105
FT                   /note="Interaction with REST"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   REGION          246..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..540
FT                   /note="Interaction with NCOR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   REGION          392..591
FT                   /note="Interaction with SUDS3 and HDAC1"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   REGION          394..430
FT                   /note="Middle-domain"
FT                   /evidence="ECO:0000269|PubMed:37137925"
FT   REGION          430..446
FT                   /note="Gate loop"
FT                   /evidence="ECO:0000269|PubMed:37137925"
FT   REGION          446..572
FT                   /note="HDAC-interacting domain"
FT                   /evidence="ECO:0000269|PubMed:37137925"
FT   REGION          706..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         709
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62141"
FT   VAR_SEQ         354..1162
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014185"
FT   VAR_SEQ         423..454
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9734811"
FT                   /id="VSP_014186"
FT   HELIX           305..318
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           322..335
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   TURN            336..338
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           341..348
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   TURN            349..351
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           356..366
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   TURN            398..400
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           418..422
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          459..461
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           474..476
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           479..515
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           520..523
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   TURN            530..533
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           539..548
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           549..551
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           552..561
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           563..592
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   TURN            593..595
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           596..604
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           608..618
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           621..641
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          651..656
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           659..674
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          677..679
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           681..692
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           694..698
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          771..777
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           779..817
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           821..823
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           841..860
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           865..876
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           877..883
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           886..902
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           904..918
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          922..926
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   HELIX           929..946
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          953..960
FT                   /evidence="ECO:0007829|PDB:8BPC"
FT   STRAND          963..970
FT                   /evidence="ECO:0007829|PDB:8BPC"
SQ   SEQUENCE   1162 AA;  133066 MW;  03D3B24AF1CF40B6 CRC64;
     MAHAGGGSGG SGAGGPAGRG LSGARWGRSG SAGHEKLPVH VEDALTYLDQ VKIRFGSDPA
     TYNGFLEIMK EFKSQSIDTP GVIRRVSQLF HEHPDLIVGF NAFLPLGYRI DIPKNGKLNI
     QSPLTSQENS HNHGDGAEDF KQQVPYKEDK PQVPLESDSV EFNNAISYVN KIKTRFLDHP
     EIYRSFLEIL HTYQKEQLNT RGRPFRGMSE EEVFTEVANL FRGQEDLLSE FGQFLPEAKR
     SLFTGNGPCE MHSVQKNEHD KTPEHSRKRS RPSLLRPVSA PAKKKMKLRG TKDLSIAAVG
     KYGTLQEFSF FDKVRRVLKS QEVYENFLRC IALFNQELVS GSELLQLVSP FLGKFPELFA
     QFKSFLGVKE LSFAPPMSDR SGDGISREID YASCKRIGSS YRALPKTYQQ PKCSGRTAIC
     KELDHWTLLQ GSWTDDYCMS KFKNTCWIPG YSAGVLNDTW VSFPSWSEDS TFVSSKKTPY
     EEQLHRCEDE RFELDVVLET NLATIRVLES VQKKLSRMAP EDQEKFRLDD SLGGTSEVIQ
     RRAIYRIYGD KAPEIIESLK KNPVTAVPVV LKRLKAKEEE WREAQQGFNK IWREQYEKAY
     LKSLDHQAVN FKQNDTKALR SKSLLNEIES VYDEHQEQHS EGRSAPSSEP HLIFVYEDRQ
     ILEDAAALIS YYVKRQPAIQ KEDQGTIHQL LHQFVPSLFF SQQLDLGASE ESADEDRDSP
     QGQTTDPSER KKPAPGPHSS PPEEKGAFGD APATEQPPLP PPAPHKPLDD VYSLFFANNN
     WYFFLRLHQT LCSRLLKIYR QAQKQLLEYR TEKEREKLLC EGRREKGSDP AMELRLKQPS
     EVELEEYYPA FLDMVRSLLE GSIDPTQYED TLREMFTIHA YVGFTMDKLV QNIARQLHHL
     VSDDVCLKVV ELYLNEKKRG AAGGNLSSRC VRAARETSYQ WKAERCMADE NCFKVMFLQR
     KGQVIMTIEL LDTEEAQTED PVEVQHLARY VEQYVGTEGA SSSPTEGFLL KPVFLQRNLK
     KFRRRWQSEQ ARALRGEARS SWKRLVGVES ACDVDCRFKL STHKMVFIVN SEDYMYRRGT
     LCRAKQVQPL VLLRHHQHFE EWHSRWLEDN VTVEAASLVQ DWLMGEEDED MVPCKTLCET
     VHVHGLPVTR YRVQYSRRPA SP
//