CAF1B_HUMAN
ID CAF1B_HUMAN Reviewed; 559 AA.
AC Q13112; Q99548;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Chromatin assembly factor 1 subunit B {ECO:0000305};
DE Short=CAF-1 subunit B;
DE AltName: Full=Chromatin assembly factor I p60 subunit;
DE Short=CAF-I 60 kDa subunit;
DE Short=CAF-I p60;
DE AltName: Full=M-phase phosphoprotein 7;
GN Name=CHAF1B {ECO:0000312|HGNC:HGNC:1911};
GN Synonyms=CAF1A, CAF1P60, MPHOSPH7, MPP7;
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 [MRNA], AND PROTEIN SEQUENCE OF 100-123.
RX PubMed=7600578; DOI=10.1016/s0092-8674(05)80015-7;
RA Kaufman P.D., Kobayashi R., Kessler N., Stillman B.;
RT "The p150 and p60 subunits of chromatin assembly factor I: a molecular link
RT between newly synthesized histones and DNA replication.";
RL Cell 81:1105-1114(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A.,
RA Asakawa S., Shimizu N.;
RT "Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 474-559, AND PHOSPHORYLATION.
RC TISSUE=Lymphoblast;
RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455;
RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression cloning.";
RL Mol. Biol. Cell 7:1455-1469(1996).
RN [6]
RP FUNCTION.
RX PubMed=9813080; DOI=10.1083/jcb.143.3.563;
RA Martini E., Roche D.M., Marheineke K., Verreault A., Almouzni G.;
RT "Recruitment of phosphorylated chromatin assembly factor 1 to chromatin
RT after UV irradiation of human cells.";
RL J. Cell Biol. 143:563-575(1998).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9614144; DOI=10.1074/jbc.273.24.15279;
RA Marheineke K., Krude T.;
RT "Nucleosome assembly activity and intracellular localization of human CAF-1
RT changes during the cell division cycle.";
RL J. Biol. Chem. 273:15279-15286(1998).
RN [8]
RP REVIEW.
RX PubMed=10893180; DOI=10.1242/jcs.113.15.2647;
RA Ridgway P., Almouzni G.;
RT "CAF-1 and the inheritance of chromatin states: at the crossroads of DNA
RT replication and repair.";
RL J. Cell Sci. 113:2647-2658(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419; SER-429; THR-433 AND
RP SER-538, AND 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-458, 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394; THR-419; SER-429;
RP THR-433 AND SER-458, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP INTERACTION WITH HISTONES H3.1; H3.2 AND H3.1T.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Complex that is thought to mediate chromatin assembly in DNA
CC replication and DNA repair. Assembles histone octamers onto replicating
CC DNA in vitro. CAF-1 performs the first step of the nucleosome assembly
CC process, bringing newly synthesized histones H3 and H4 to replicating
CC DNA; histones H2A/H2B can bind to this chromatin precursor subsequent
CC to DNA replication to complete the histone octamer.
CC {ECO:0000269|PubMed:9813080}.
CC -!- SUBUNIT: Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and
CC CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4
CC are complexed with CHAF1A and CHAF1B in G1 phase. In G2 and S phase
CC also monomeric CHAF1B is detected. Interacts with histones H3.1, H3.2
CC and H3.1t (PubMed:33857403). {ECO:0000250|UniProtKB:Q5R1S9,
CC ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC Q13112; Q9Y294: ASF1A; NbExp=3; IntAct=EBI-1052944, EBI-749553;
CC Q13112; Q9NVP2: ASF1B; NbExp=3; IntAct=EBI-1052944, EBI-1055650;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9614144}. Cytoplasm
CC {ECO:0000269|PubMed:9614144}. Note=DNA replication foci. Cytoplasmic in
CC M phase.
CC -!- DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2 phases.
CC -!- PTM: Differentially phosphorylated during cell cycle. During mitosis
CC the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced
CC into the cytosol. Progressivly dephosphorylated from G1 to S and G2
CC phase. Phosphorylated p60 is recruited to chromatin undergoing DNA
CC repair after UV irradiation in G1, S or G2 phases.
CC {ECO:0000269|PubMed:8885239, ECO:0000269|PubMed:9614144}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
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DR EMBL; U20980; AAA76737.1; -; mRNA.
DR EMBL; AP000694; BAA89426.1; -; Genomic_DNA.
DR EMBL; AP001725; BAA95549.1; -; Genomic_DNA.
DR EMBL; BC021218; AAH21218.1; -; mRNA.
DR EMBL; X98262; CAA66915.1; -; mRNA.
DR CCDS; CCDS13644.1; -.
DR PIR; B56731; B56731.
DR RefSeq; NP_005432.1; NM_005441.2.
DR RefSeq; XP_016883966.1; XM_017028477.1.
DR RefSeq; XP_016883967.1; XM_017028478.1.
DR AlphaFoldDB; Q13112; -.
DR SMR; Q13112; -.
DR BioGRID; 113846; 150.
DR ComplexPortal; CPX-569; Chromatin assembly factor 1 complex.
DR CORUM; Q13112; -.
DR DIP; DIP-29243N; -.
DR IntAct; Q13112; 40.
DR MINT; Q13112; -.
DR STRING; 9606.ENSP00000315700; -.
DR GlyGen; Q13112; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13112; -.
DR MetOSite; Q13112; -.
DR PhosphoSitePlus; Q13112; -.
DR SwissPalm; Q13112; -.
DR BioMuta; CHAF1B; -.
DR DMDM; 3121829; -.
DR EPD; Q13112; -.
DR jPOST; Q13112; -.
DR MassIVE; Q13112; -.
DR MaxQB; Q13112; -.
DR PaxDb; Q13112; -.
DR PeptideAtlas; Q13112; -.
DR PRIDE; Q13112; -.
DR ProteomicsDB; 59163; -.
DR Antibodypedia; 8327; 318 antibodies from 35 providers.
DR DNASU; 8208; -.
DR Ensembl; ENST00000314103.6; ENSP00000315700.4; ENSG00000159259.8.
DR GeneID; 8208; -.
DR KEGG; hsa:8208; -.
DR MANE-Select; ENST00000314103.6; ENSP00000315700.4; NM_005441.3; NP_005432.1.
DR UCSC; uc002yvj.4; human.
DR CTD; 8208; -.
DR DisGeNET; 8208; -.
DR GeneCards; CHAF1B; -.
DR HGNC; HGNC:1911; CHAF1B.
DR HPA; ENSG00000159259; Tissue enhanced (skeletal).
DR MIM; 601245; gene.
DR neXtProt; NX_Q13112; -.
DR OpenTargets; ENSG00000159259; -.
DR PharmGKB; PA26447; -.
DR VEuPathDB; HostDB:ENSG00000159259; -.
DR eggNOG; KOG1009; Eukaryota.
DR GeneTree; ENSGT00550000074968; -.
DR HOGENOM; CLU_010127_5_2_1; -.
DR InParanoid; Q13112; -.
DR OMA; CTIAVRC; -.
DR OrthoDB; 685536at2759; -.
DR PhylomeDB; Q13112; -.
DR TreeFam; TF313062; -.
DR PathwayCommons; Q13112; -.
DR SignaLink; Q13112; -.
DR SIGNOR; Q13112; -.
DR BioGRID-ORCS; 8208; 786 hits in 1066 CRISPR screens.
DR ChiTaRS; CHAF1B; human.
DR GeneWiki; CHAF1B; -.
DR GenomeRNAi; 8208; -.
DR Pharos; Q13112; Tbio.
DR PRO; PR:Q13112; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q13112; protein.
DR Bgee; ENSG00000159259; Expressed in secondary oocyte and 110 other tissues.
DR Genevisible; Q13112; HS.
DR GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
DR GO; GO:0042393; F:histone binding; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR029129; CAF1_p60_C.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR045145; PTHR15271.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15271; PTHR15271; 1.
DR Pfam; PF15512; CAF-1_p60_C; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00319; GPROTEINB.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA repair; DNA replication; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..559
FT /note="Chromatin assembly factor 1 subunit B"
FT /id="PRO_0000050896"
FT REPEAT 11..54
FT /note="WD 1"
FT REPEAT 64..103
FT /note="WD 2"
FT REPEAT 127..166
FT /note="WD 3"
FT REPEAT 169..208
FT /note="WD 4"
FT REPEAT 228..279
FT /note="WD 5"
FT REPEAT 299..340
FT /note="WD 6"
FT REPEAT 344..385
FT /note="WD 7"
FT REGION 386..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 495
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 531
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 506
FT /note="K -> Q (in dbSNP:rs74900401)"
FT /id="VAR_053387"
FT CONFLICT 494
FT /note="K -> N (in Ref. 5; CAA66915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61493 MW; AD1846CC81B8DC9F CRC64;
MKVITCEIAW HNKEPVYSLD FQHGTAGRIH RLASAGVDTN VRIWKVEKGP DGKAIVEFLS
NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKVNDNKE PEQIAFQDED EAQLNKENWT
VVKTLRGHLE DVYDICWATD GNLMASASVD NTAIIWDVSK GQKISIFNEH KSYVQGVTWD
PLGQYVATLS CDRVLRVYSI QKKRVAFNVS KMLSGIGAEG EARSYRMFHD DSMKSFFRRL
SFTPDGSLLL TPAGCVESGE NVMNTTYVFS RKNLKRPIAH LPCPGKATLA VRCCPVYFEL
RPVVETGVEL MSLPYRLVFA VASEDSVLLY DTQQSFPFGY VSNIHYHTLS DISWSSDGAF
LAISSTDGYC SFVTFEKDEL GIPLKEKPVL NMRTPDTAKK TKSQTHRGSS PGPRPVEGTP
ASRTQDPSSP GTTPPQARQA PAPTVIRDPP SITPAVKSPL PGPSEEKTLQ PSSQNTKAHP
SRRVTLNTLQ AWSKTTPRRI NLTPLKTDTP PSSVPTSVIS TPSTEEIQSE TPGDAQGSPP
ELKRPRLDEN KGGTESLDP
