GenomeNet

Database: UniProt
Entry: Q08024
LinkDB: Q08024
Original site: Q08024 
ID   PEBB_MOUSE              Reviewed;         187 AA.
AC   Q08024; Q08025; Q62050; Q62051; Q8C282; Q8CGD5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   17-JUN-2020, entry version 160.
DE   RecName: Full=Core-binding factor subunit beta;
DE            Short=CBF-beta;
DE   AltName: Full=Polyomavirus enhancer-binding protein 2 beta subunit;
DE            Short=PEA2-beta;
DE            Short=PEBP2-beta;
DE   AltName: Full=SL3-3 enhancer factor 1 subunit beta;
DE   AltName: Full=SL3/AKV core-binding factor beta subunit;
GN   Name=Cbfb; Synonyms=Pebp2b, Pebpb2;
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] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 1-26, AND PROTEIN SEQUENCE OF 12-28 AND 95-98.
RX   PubMed=8386878; DOI=10.1006/viro.1993.1262;
RA   Ogawa E., Inuzuka M., Maruyama M., Satake M., Naito-Fujimoto M., Ito Y.,
RA   Shigesada K.;
RT   "Molecular cloning and characterization of PEBP2 beta, the heterodimeric
RT   partner of a novel Drosophila runt-related DNA binding protein PEBP2
RT   alpha.";
RL   Virology 194:314-331(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4).
RC   TISSUE=Thymus;
RX   PubMed=8497254; DOI=10.1128/mcb.13.6.3324;
RA   Wang S., Wang Q., Crute B.E., Melnikova I.N., Keller S.R., Speck N.A.;
RT   "Cloning and characterization of subunits of the T-cell receptor and murine
RT   leukemia virus enhancer core-binding factor.";
RL   Mol. Cell. Biol. 13:3324-3339(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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   [6]
RP   INTERACTION WITH COPRS, AND IDENTIFICATION IN A COMPLEX WITH PRMT5 AND
RP   RUNX1.
RX   PubMed=22193545; DOI=10.1038/cdd.2011.193;
RA   Paul C., Sardet C., Fabbrizio E.;
RT   "The histone- and PRMT5-associated protein COPR5 is required for myogenic
RT   differentiation.";
RL   Cell Death Differ. 19:900-908(2012).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-141 IN COMPLEX WITH CEBPB;
RP   RUNX1 AND DNA, AND MUTAGENESIS OF VAL-5; ASN-63 AND ASN-104.
RX   PubMed=11257229; DOI=10.1016/s0092-8674(01)00271-9;
RA   Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K.,
RA   Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.;
RT   "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and
RT   its allosteric control by CBFbeta.";
RL   Cell 104:755-767(2001).
RN   [8]
RP   STRUCTURE BY NMR OF 1-141.
RX   PubMed=10404216; DOI=10.1038/10670;
RA   Huang X., Peng J.W., Speck N.A., Bushweller J.H.;
RT   "Solution structure of core binding factor beta and map of the CBF alpha
RT   binding site.";
RL   Nat. Struct. Biol. 6:624-627(1999).
RN   [9]
RP   STRUCTURE BY NMR OF 1-141.
RX   PubMed=11560490; DOI=10.1021/bi010713+;
RA   Wolf-Watz M., Grundstroem T., Haerd T.;
RT   "Structure and backbone dynamics of Apo-CBFbeta in solution.";
RL   Biochemistry 40:11423-11432(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=18258917; DOI=10.1126/science.1151844;
RA   Setoguchi R., Tachibana M., Naoe Y., Muroi S., Akiyama K., Tezuka C.,
RA   Okuda T., Taniuchi I.;
RT   "Repression of the transcription factor Th-POK by Runx complexes in
RT   cytotoxic T cell development.";
RL   Science 319:822-825(2008).
CC   -!- FUNCTION: Forms the heterodimeric complex core-binding factor (CBF)
CC       with RUNX family proteins (RUNX1, RUNX2, and RUNX3). RUNX members
CC       modulate the transcription of their target genes through recognizing
CC       the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-
CC       TGCGGT-3', within their regulatory regions via their runt domain, while
CC       CBFB is a non-DNA-binding regulatory subunit that allosterically
CC       enhances the sequence-specific DNA-binding capacity of RUNX. The
CC       heterodimers bind to the core site of a number of enhancers and
CC       promoters, including murine leukemia virus, polyomavirus enhancer, T-
CC       cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). CBF
CC       complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T
CC       cell development. They bind to RUNX-binding sequence within the ZBTB7B
CC       locus acting as transcriptional silencer and allowing for cytotoxic T
CC       cell differentiation (PubMed:18258917). {ECO:0000269|PubMed:18258917,
CC       ECO:0000305|PubMed:11257229, ECO:0000305|PubMed:8386878,
CC       ECO:0000305|PubMed:8497254}.
CC   -!- SUBUNIT: Heterodimer with RUNX1, RUNX2 and RUNX3 (Probable). Interacts
CC       with COPRS. Found in a complex with PRMT5 and RUNX1 (PubMed:22193545).
CC       {ECO:0000269|PubMed:22193545, ECO:0000305|PubMed:11257229}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q08024-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08024-2; Sequence=VSP_004360;
CC       Name=3;
CC         IsoId=Q08024-3; Sequence=VSP_004359;
CC       Name=4;
CC         IsoId=Q08024-4; Sequence=VSP_004358;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest level in
CC       thymus, but also abundantly expressed in muscle, lung and brain.
CC   -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Does not dimerize with the alpha subunit.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Does not dimerize with the alpha subunit.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CBF-beta family. {ECO:0000305}.
DR   EMBL; D14572; BAA03426.1; -; mRNA.
DR   EMBL; D14571; BAA03425.1; -; mRNA.
DR   EMBL; D14570; BAA03424.1; -; mRNA.
DR   EMBL; D14569; BAA03423.1; -; Genomic_DNA.
DR   EMBL; L03305; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L03306; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L03279; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK089094; BAC40748.1; -; mRNA.
DR   EMBL; BC006763; AAH06763.1; -; mRNA.
DR   EMBL; BC026749; AAH26749.1; -; mRNA.
DR   EMBL; BC040752; AAH40752.2; -; mRNA.
DR   CCDS; CCDS22592.1; -. [Q08024-1]
DR   CCDS; CCDS52654.1; -. [Q08024-2]
DR   CCDS; CCDS52655.1; -. [Q08024-3]
DR   CCDS; CCDS52656.1; -. [Q08024-4]
DR   PIR; A46107; A46107.
DR   PIR; B48124; B48124.
DR   RefSeq; NP_001154928.1; NM_001161456.1. [Q08024-4]
DR   RefSeq; NP_001154929.1; NM_001161457.1. [Q08024-3]
DR   RefSeq; NP_001154930.1; NM_001161458.1. [Q08024-2]
DR   RefSeq; NP_071704.3; NM_022309.4. [Q08024-1]
DR   PDB; 1ILF; NMR; -; A=1-141.
DR   PDB; 1IO4; X-ray; 3.00 A; D=1-141.
DR   PDB; 2JHB; NMR; -; A=1-141.
DR   PDB; 3WTS; X-ray; 2.35 A; B/G=1-142.
DR   PDB; 3WTT; X-ray; 2.35 A; B/G=1-142.
DR   PDB; 3WTU; X-ray; 2.70 A; B/G=1-142.
DR   PDB; 3WTV; X-ray; 2.70 A; B/G=1-142.
DR   PDB; 3WTW; X-ray; 2.90 A; B/G=1-142.
DR   PDB; 3WTX; X-ray; 2.80 A; B/G=1-142.
DR   PDB; 3WTY; X-ray; 2.70 A; B/G=1-142.
DR   PDBsum; 1ILF; -.
DR   PDBsum; 1IO4; -.
DR   PDBsum; 2JHB; -.
DR   PDBsum; 3WTS; -.
DR   PDBsum; 3WTT; -.
DR   PDBsum; 3WTU; -.
DR   PDBsum; 3WTV; -.
DR   PDBsum; 3WTW; -.
DR   PDBsum; 3WTX; -.
DR   PDBsum; 3WTY; -.
DR   SMR; Q08024; -.
DR   BioGRID; 198525; 7.
DR   IntAct; Q08024; 3.
DR   STRING; 10090.ENSMUSP00000059382; -.
DR   iPTMnet; Q08024; -.
DR   PhosphoSitePlus; Q08024; -.
DR   EPD; Q08024; -.
DR   jPOST; Q08024; -.
DR   MaxQB; Q08024; -.
DR   PaxDb; Q08024; -.
DR   PeptideAtlas; Q08024; -.
DR   PRIDE; Q08024; -.
DR   Antibodypedia; 15619; 390 antibodies.
DR   Ensembl; ENSMUST00000052209; ENSMUSP00000059382; ENSMUSG00000031885. [Q08024-1]
DR   Ensembl; ENSMUST00000109392; ENSMUSP00000105019; ENSMUSG00000031885. [Q08024-2]
DR   Ensembl; ENSMUST00000109394; ENSMUSP00000105021; ENSMUSG00000031885. [Q08024-4]
DR   Ensembl; ENSMUST00000109395; ENSMUSP00000105022; ENSMUSG00000031885. [Q08024-3]
DR   GeneID; 12400; -.
DR   KEGG; mmu:12400; -.
DR   UCSC; uc009nbp.2; mouse. [Q08024-1]
DR   UCSC; uc009nbq.2; mouse. [Q08024-2]
DR   UCSC; uc009nbr.2; mouse. [Q08024-4]
DR   UCSC; uc012gjd.1; mouse. [Q08024-3]
DR   CTD; 865; -.
DR   MGI; MGI:99851; Cbfb.
DR   eggNOG; KOG4785; Eukaryota.
DR   eggNOG; ENOG410Z04Q; LUCA.
DR   GeneTree; ENSGT00390000018132; -.
DR   HOGENOM; CLU_074992_1_0_1; -.
DR   InParanoid; Q08024; -.
DR   OMA; PGKVHIK; -.
DR   OrthoDB; 1254153at2759; -.
DR   PhylomeDB; Q08024; -.
DR   TreeFam; TF314675; -.
DR   Reactome; R-MMU-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR   Reactome; R-MMU-8878166; Transcriptional regulation by RUNX2.
DR   Reactome; R-MMU-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR   Reactome; R-MMU-8934593; Regulation of RUNX1 Expression and Activity.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   Reactome; R-MMU-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR   Reactome; R-MMU-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR   Reactome; R-MMU-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR   Reactome; R-MMU-8941326; RUNX2 regulates bone development.
DR   Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 12400; 8 hits in 14 CRISPR screens.
DR   ChiTaRS; Cbfb; mouse.
DR   EvolutionaryTrace; Q08024; -.
DR   PRO; PR:Q08024; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q08024; protein.
DR   Bgee; ENSMUSG00000031885; Expressed in trigeminal ganglion and 316 other tissues.
DR   Genevisible; Q08024; MM.
DR   GO; GO:0016513; C:core-binding factor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR   GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI.
DR   GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR   GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0001503; P:ossification; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.40.250.10; -; 1.
DR   InterPro; IPR003417; CBF_beta.
DR   InterPro; IPR036552; CBF_bsu_sf.
DR   PANTHER; PTHR10276; PTHR10276; 1.
DR   Pfam; PF02312; CBF_beta; 1.
DR   SUPFAM; SSF50723; SSF50723; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..187
FT                   /note="Core-binding factor subunit beta"
FT                   /id="PRO_0000058302"
FT   MOD_RES         10
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         159
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         56..94
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:8497254"
FT                   /id="VSP_004358"
FT   VAR_SEQ         134..165
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8386878"
FT                   /id="VSP_004359"
FT   VAR_SEQ         166..187
FT                   /note="ARRQQDPSPGSNLGGGDDLKLR -> VRVSQLLAVTGKKTARP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8386878,
FT                   ECO:0000303|PubMed:8497254"
FT                   /id="VSP_004360"
FT   MUTAGEN         5
FT                   /note="V->A: Interferes with heterodimerization."
FT                   /evidence="ECO:0000269|PubMed:11257229"
FT   MUTAGEN         63
FT                   /note="N->A: Interferes with heterodimerization."
FT                   /evidence="ECO:0000269|PubMed:11257229"
FT   MUTAGEN         104
FT                   /note="N->A: Interferes with heterodimerization."
FT                   /evidence="ECO:0000269|PubMed:11257229"
FT   CONFLICT        2
FT                   /note="P -> S (in Ref. 3; BAC40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="R -> P (in Ref. 3; BAC40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="D -> N (in Ref. 2; L03279)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..12
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   HELIX           16..19
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   TURN            20..22
FT                   /evidence="ECO:0000244|PDB:3WTT"
FT   STRAND          25..29
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   TURN            31..34
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   HELIX           37..49
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          52..57
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   TURN            58..61
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          62..67
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          83..86
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          88..103
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          106..115
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   TURN            116..118
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   STRAND          120..127
FT                   /evidence="ECO:0000244|PDB:3WTS"
FT   HELIX           129..139
FT                   /evidence="ECO:0000244|PDB:3WTS"
SQ   SEQUENCE   187 AA;  22030 MW;  0B2E6101A35D0FD8 CRC64;
     MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QTRFQNACRD GRSEIAFVAT
     GTNLSLQFFP ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLHRLD
     GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH REEMEARRQQ DPSPGSNLGG
     GDDLKLR
//
DBGET integrated database retrieval system