CENPB_HUMAN
ID CENPB_HUMAN Reviewed; 599 AA.
AC P07199; Q96EI4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Major centromere autoantigen B;
DE AltName: Full=Centromere protein B;
DE Short=CENP-B;
GN Name=CENPB;
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 [GENOMIC DNA].
RX PubMed=1893793; DOI=10.1007/bf00337514;
RA Sullivan K.F., Glass C.A.;
RT "CENP-B is a highly conserved mammalian centromere protein with homology to
RT the helix-loop-helix family of proteins.";
RL Chromosoma 100:360-370(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-599.
RX PubMed=2435739; DOI=10.1083/jcb.104.4.817;
RA Earnshaw W.C., Sullivan K.F., Machlin P.S., Cooke C.A., Kaiser D.A.,
RA Pollard T.D., Rothfield N.F., Cleveland D.W.;
RT "Molecular cloning of cDNA for CENP-B, the major human centromere
RT autoantigen.";
RL J. Cell Biol. 104:817-829(1987).
RN [5]
RP SUBUNIT, AND DOMAINS.
RX PubMed=1469042; DOI=10.1083/jcb.119.6.1413;
RA Yoda K., Kitagawa K., Masumoto H., Muro Y., Okazaki T.;
RT "A human centromere protein, CENP-B, has a DNA binding domain containing
RT four potential alpha helices at the NH2 terminus, which is separable from
RT dimerizing activity.";
RL J. Cell Biol. 119:1413-1427(1992).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18072184; DOI=10.1002/cbic.200700358;
RA Orthaus S., Biskup C., Hoffmann B., Hoischen C., Ohndorf S., Benndorf K.,
RA Diekmann S.;
RT "Assembly of the inner kinetochore proteins CENP-A and CENP-B in living
RT human cells.";
RL ChemBioChem 9:77-92(2008).
RN [7]
RP INTERACTION WITH CENPT.
RX PubMed=19412974; DOI=10.1002/jbio.200810014;
RA Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.;
RT "Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-
RT A and CENP-B.";
RL J. Biophotonics 1:245-254(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-165 AND THR-398, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND THR-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT GLY-2, AND MUTAGENESIS OF
RP LYS-4.
RX PubMed=23978223; DOI=10.1021/pr400498y;
RA Dai X., Otake K., You C., Cai Q., Wang Z., Masumoto H., Wang Y.;
RT "Identification of novel alpha-n-methylation of CENP-B that regulates its
RT binding to the centromeric DNA.";
RL J. Proteome Res. 12:4167-4175(2013).
RN [13]
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 [14]
RP DEVELOPMENTAL STAGE.
RX PubMed=24522885; DOI=10.1098/rsob.130229;
RA Dornblut C., Quinn N., Monajambashi S., Prendergast L., van Vuuren C.,
RA Muench S., Deng W., Leonhardt H., Cardoso M.C., Hoischen C., Diekmann S.,
RA Sullivan K.F.;
RT "A CENP-S/X complex assembles at the centromere in S and G2 phases of the
RT human cell cycle.";
RL Open Biol. 4:130229-130229(2014).
RN [15]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246, 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 [17]
RP STRUCTURE BY NMR OF 1-56.
RX PubMed=9451007; DOI=10.1093/emboj/17.3.827;
RA Iwahara J., Kigawa T., Kitagawa K., Masumoto H., Okazaki T., Yokoyama S.;
RT "A helix-turn-helix structure unit in human centromere protein B (CENP-
RT B).";
RL EMBO J. 17:827-837(1998).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-129 IN COMPLEX WITH DNA, H-T-H
RP MOTIF, AND FUNCTION.
RX PubMed=11726497; DOI=10.1093/emboj/20.23.6612;
RA Tanaka Y., Nureki O., Kurumizaka H., Fukai S., Kawaguchi S., Ikuta M.,
RA Iwahara J., Okazaki T., Yokoyama S.;
RT "Crystal structure of the CENP-B protein-DNA complex: the DNA-binding
RT domains of CENP-B induce kinks in the CENP-B box DNA.";
RL EMBO J. 20:6612-6618(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 536-599, AND SUBUNIT.
RX PubMed=14522975; DOI=10.1074/jbc.m310388200;
RA Tawaramoto M.S., Park S.Y., Tanaka Y., Nureki O., Kurumizaka H.,
RA Yokoyama S.;
RT "Crystal structure of the human centromere protein B (CENP-B) dimerization
RT domain at 1.65-A resolution.";
RL J. Biol. Chem. 278:51454-51461(2003).
CC -!- FUNCTION: Interacts with centromeric heterochromatin in chromosomes and
CC binds to a specific 17 bp subset of alphoid satellite DNA, called the
CC CENP-B box (PubMed:11726497). May organize arrays of centromere
CC satellite DNA into a higher-order structure which then directs
CC centromere formation and kinetochore assembly in mammalian chromosomes
CC (Probable). {ECO:0000269|PubMed:11726497, ECO:0000305}.
CC -!- SUBUNIT: Antiparallel homodimer (PubMed:1469042, PubMed:14522975).
CC Interacts with CENPT (PubMed:19412974). Identified in a centromere
CC complex containing histones H2A, H2B and H4, and at least CENPA, CENPB,
CC CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 (PubMed:27499292).
CC {ECO:0000269|PubMed:14522975, ECO:0000269|PubMed:1469042,
CC ECO:0000269|PubMed:19412974, ECO:0000269|PubMed:27499292}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320,
CC ECO:0000255|PROSITE-ProRule:PRU00583, ECO:0000269|PubMed:18072184}.
CC Chromosome, centromere {ECO:0000269|PubMed:18072184}.
CC -!- DEVELOPMENTAL STAGE: Expression varies across the cell cycle, with high
CC levels in G2 phase (at the mRNA level). {ECO:0000269|PubMed:24522885}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:P27790}.
CC -!- PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is
CC stimulated in response to extracellular stimuli, including increased
CC cell density and heat shock, and seems to facilitate binding to CENP-B
CC boxes. Chromatin-bound CENP-B is primarily trimethylated.
CC {ECO:0000269|PubMed:23978223}.
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DR EMBL; X55039; CAA38879.1; -; Genomic_DNA.
DR EMBL; AL109804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012297; AAH12297.1; -; mRNA.
DR EMBL; BC053847; AAH53847.1; -; mRNA.
DR EMBL; X05299; CAA28918.1; -; mRNA.
DR CCDS; CCDS13064.1; -.
DR PIR; S18735; S18735.
DR RefSeq; NP_001801.1; NM_001810.5.
DR PDB; 1BW6; NMR; -; A=1-56.
DR PDB; 1HLV; X-ray; 2.50 A; A=1-129.
DR PDB; 1UFI; X-ray; 1.65 A; A/B/C/D=540-599.
DR PDB; 6KDR; X-ray; 2.11 A; D/E=2-10.
DR PDBsum; 1BW6; -.
DR PDBsum; 1HLV; -.
DR PDBsum; 1UFI; -.
DR PDBsum; 6KDR; -.
DR AlphaFoldDB; P07199; -.
DR SMR; P07199; -.
DR BioGRID; 107488; 114.
DR CORUM; P07199; -.
DR IntAct; P07199; 64.
DR MINT; P07199; -.
DR STRING; 9606.ENSP00000369075; -.
DR iPTMnet; P07199; -.
DR PhosphoSitePlus; P07199; -.
DR BioMuta; CENPB; -.
DR DMDM; 116109; -.
DR EPD; P07199; -.
DR jPOST; P07199; -.
DR MassIVE; P07199; -.
DR MaxQB; P07199; -.
DR PaxDb; P07199; -.
DR PeptideAtlas; P07199; -.
DR PRIDE; P07199; -.
DR ProteomicsDB; 51963; -.
DR ProteomicsDB; 76410; -.
DR Antibodypedia; 23700; 138 antibodies from 20 providers.
DR DNASU; 1059; -.
DR Ensembl; ENST00000379751.5; ENSP00000369075.4; ENSG00000125817.8.
DR GeneID; 1059; -.
DR KEGG; hsa:1059; -.
DR MANE-Select; ENST00000379751.5; ENSP00000369075.4; NM_001810.6; NP_001801.1.
DR UCSC; uc002wjk.3; human.
DR CTD; 1059; -.
DR DisGeNET; 1059; -.
DR GeneCards; CENPB; -.
DR HGNC; HGNC:1852; CENPB.
DR HPA; ENSG00000125817; Low tissue specificity.
DR MIM; 117140; gene.
DR neXtProt; NX_P07199; -.
DR OpenTargets; ENSG00000125817; -.
DR PharmGKB; PA26397; -.
DR VEuPathDB; HostDB:ENSG00000125817; -.
DR eggNOG; KOG3105; Eukaryota.
DR GeneTree; ENSGT00940000162810; -.
DR HOGENOM; CLU_018294_10_0_1; -.
DR InParanoid; P07199; -.
DR OMA; GGLPCDY; -.
DR OrthoDB; 1343623at2759; -.
DR PhylomeDB; P07199; -.
DR TreeFam; TF101131; -.
DR PathwayCommons; P07199; -.
DR SignaLink; P07199; -.
DR BioGRID-ORCS; 1059; 24 hits in 1083 CRISPR screens.
DR ChiTaRS; CENPB; human.
DR EvolutionaryTrace; P07199; -.
DR GeneWiki; Centromere_protein_B; -.
DR GenomeRNAi; 1059; -.
DR Pharos; P07199; Tbio.
DR PRO; PR:P07199; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P07199; protein.
DR Bgee; ENSG00000125817; Expressed in C1 segment of cervical spinal cord and 182 other tissues.
DR Genevisible; P07199; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0019237; F:centromeric DNA binding; IC:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003696; F:satellite DNA binding; NAS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; TAS:BHF-UCL.
DR Gene3D; 1.10.287.1090; -; 1.
DR InterPro; IPR033062; CENP-B.
DR InterPro; IPR015115; CenpB_C.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR034882; Dimerisation_CENP-B_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR007889; HTH_Psq.
DR PANTHER; PTHR19303:SF25; PTHR19303:SF25; 1.
DR Pfam; PF09026; CENP-B_dimeris; 1.
DR Pfam; PF04218; CENP-B_N; 1.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR SMART; SM00674; CENPB; 1.
DR SUPFAM; SSF101160; SSF101160; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51253; HTH_CENPB; 1.
DR PROSITE; PS50960; HTH_PSQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Centromere; Chromosome; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23978223"
FT CHAIN 2..599
FT /note="Major centromere autoantigen B"
FT /id="PRO_0000126125"
FT DOMAIN 2..52
FT /note="HTH psq-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DOMAIN 65..136
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT DNA_BIND 97..129
FT /note="H-T-H motif"
FT REGION 143..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..599
FT /note="Homodimerization"
FT COMPBIAS 404..471
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine; alternate"
FT /evidence="ECO:0000269|PubMed:23978223"
FT MOD_RES 2
FT /note="N,N-dimethylglycine; alternate"
FT /evidence="ECO:0000269|PubMed:23978223"
FT MOD_RES 2
FT /note="N-methylglycine; alternate"
FT /evidence="ECO:0000269|PubMed:23978223"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 4
FT /note="K->Q: Abolishes N-terminal methylation."
FT /evidence="ECO:0000269|PubMed:23978223"
FT CONFLICT 583
FT /note="R -> M (in Ref. 4; CAA28918)"
FT /evidence="ECO:0000305"
FT CONFLICT 592..593
FT /note="VR -> LL (in Ref. 4; CAA28918)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1BW6"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1HLV"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1BW6"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:1HLV"
FT HELIX 544..558
FT /evidence="ECO:0007829|PDB:1UFI"
FT HELIX 565..584
FT /evidence="ECO:0007829|PDB:1UFI"
SQ SEQUENCE 599 AA; 65171 MW; 9B4B7DB957A914AA CRC64;
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG
VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN
GWLDRFRRRH GVVSCSGVAR ARARNAAPRT PAAPASPAAV PSEGSGGSTT GWRAREEQPP
SVAEGYASQD VFSATETSLW YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP
PLVAGKSAKP RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG
LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS LKSEGEEEEE EEEEEEEEEG
EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE EGDVDSDEEE EEDEESSSEG LEAEDWAQGV
VEAGGSFGAY GAQEEAQCPT LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP
VPSFGEAMAY FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS
