PEBB_MOUSE
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 03-AUG-2022, entry version 169.
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.13.6.3324-3339.1993;
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}.
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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 AlphaFoldDB; Q08024; -.
DR BMRB; Q08024; -.
DR SMR; Q08024; -.
DR BioGRID; 198525; 10.
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 ProteomicsDB; 289339; -. [Q08024-1]
DR ProteomicsDB; 289340; -. [Q08024-2]
DR ProteomicsDB; 289341; -. [Q08024-3]
DR ProteomicsDB; 289342; -. [Q08024-4]
DR Antibodypedia; 15619; 427 antibodies from 40 providers.
DR DNASU; 12400; -.
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 VEuPathDB; HostDB:ENSMUSG00000031885; -.
DR eggNOG; KOG4785; Eukaryota.
DR GeneTree; ENSGT00390000018132; -.
DR HOGENOM; CLU_074992_1_0_1; -.
DR InParanoid; Q08024; -.
DR OMA; CCEGHTE; -.
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; 18 hits in 79 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 267 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: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 REGION 139..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:3WTS"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:3WTS"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3WTT"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3WTS"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:3WTS"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3WTS"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 88..103
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:3WTS"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3WTS"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3WTS"
FT HELIX 129..139
FT /evidence="ECO:0007829|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
