CSR2B_HUMAN
ID CSR2B_HUMAN Reviewed; 782 AA.
AC Q9H8E8; A2A2I5; Q96GW6; Q96IH3; Q9HBF0; Q9UIY5;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cysteine-rich protein 2-binding protein;
DE Short=CSRP2-binding protein;
DE AltName: Full=ADA2A-containing complex subunit 2;
DE Short=ATAC2;
DE AltName: Full=CRP2-binding partner;
DE Short=CRP2BP;
DE AltName: Full=Lysine acetyltransferase 14 {ECO:0000312|HGNC:HGNC:15904};
GN Name=KAT14 {ECO:0000312|HGNC:HGNC:15904}; Synonyms=CSRP2BP;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-400.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-400.
RC TISSUE=Eye, and Placenta;
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 546-782, AND INTERACTION WITH CSRP2.
RC TISSUE=Kidney;
RX PubMed=10924333; DOI=10.1006/bbrc.2000.3187;
RA Weiskirchen R., Gressner A.M.;
RT "The cysteine- and glycine-rich LIM domain protein CRP2 specifically
RT interacts with a novel human protein.";
RL Biochem. Biophys. Res. Commun. 274:655-663(2000).
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 FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-292, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-285 AND SER-416, 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).
CC -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4. May function as a
CC scaffold for the ATAC complex to promote ATAC complex stability. Has
CC also weak histone acetyltransferase activity toward histone H4.
CC Required for the normal progression through G1 and G2/M phases of the
CC cell cycle. {ECO:0000269|PubMed:19103755}.
CC -!- SUBUNIT: Interacts with the LIM 1 domain of CSRP2. Component of the
CC ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L,
CC TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it
CC probably interacts directly with KAT2A, MBIP and WDR5.
CC {ECO:0000269|PubMed:10924333, ECO:0000269|PubMed:19103755}.
CC -!- INTERACTION:
CC Q9H8E8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-750907, EBI-739624;
CC Q9H8E8; Q7L190: DPPA4; NbExp=3; IntAct=EBI-750907, EBI-710457;
CC Q9H8E8; Q9NS73: MBIP; NbExp=6; IntAct=EBI-750907, EBI-741953;
CC Q9H8E8; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-750907, EBI-10182361;
CC Q9H8E8; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-750907, EBI-748601;
CC Q9H8E8; P14373: TRIM27; NbExp=6; IntAct=EBI-750907, EBI-719493;
CC Q9H8E8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-750907, EBI-2130429;
CC Q9H8E8; P08048: ZFY; NbExp=3; IntAct=EBI-750907, EBI-12239601;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8E8-2; Sequence=VSP_000070;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung,
CC placenta, brain, liver, pancreas and kidney. High expression in
CC skeletal muscle and heart. Lower expression in lung.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; AK023759; BAB14669.1; -; mRNA.
DR EMBL; AL050321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10255.1; -; Genomic_DNA.
DR EMBL; BC007537; AAH07537.1; -; mRNA.
DR EMBL; BC009174; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF252257; AAG10249.1; -; mRNA.
DR CCDS; CCDS13133.1; -. [Q9H8E8-1]
DR RefSeq; NP_065397.3; NM_020536.4. [Q9H8E8-1]
DR AlphaFoldDB; Q9H8E8; -.
DR SMR; Q9H8E8; -.
DR BioGRID; 121485; 103.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; Q9H8E8; -.
DR IntAct; Q9H8E8; 39.
DR MINT; Q9H8E8; -.
DR STRING; 9606.ENSP00000392318; -.
DR GlyGen; Q9H8E8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H8E8; -.
DR PhosphoSitePlus; Q9H8E8; -.
DR BioMuta; KAT14; -.
DR DMDM; 308153608; -.
DR EPD; Q9H8E8; -.
DR jPOST; Q9H8E8; -.
DR MassIVE; Q9H8E8; -.
DR MaxQB; Q9H8E8; -.
DR PaxDb; Q9H8E8; -.
DR PeptideAtlas; Q9H8E8; -.
DR PRIDE; Q9H8E8; -.
DR ProteomicsDB; 81203; -. [Q9H8E8-1]
DR ProteomicsDB; 81204; -. [Q9H8E8-2]
DR Antibodypedia; 24530; 161 antibodies from 23 providers.
DR DNASU; 57325; -.
DR Ensembl; ENST00000377681.8; ENSP00000366909.3; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000435364.8; ENSP00000392318.2; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000464792.2; ENSP00000424752.2; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000489634.2; ENSP00000425909.2; ENSG00000149474.15. [Q9H8E8-2]
DR Ensembl; ENST00000676935.1; ENSP00000503493.1; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000677174.1; ENSP00000503109.1; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000677266.1; ENSP00000504050.1; ENSG00000149474.15. [Q9H8E8-1]
DR Ensembl; ENST00000678772.1; ENSP00000504276.1; ENSG00000149474.15. [Q9H8E8-1]
DR GeneID; 57325; -.
DR KEGG; hsa:57325; -.
DR UCSC; uc002wqk.3; human. [Q9H8E8-1]
DR CTD; 57325; -.
DR DisGeNET; 57325; -.
DR GeneCards; KAT14; -.
DR HGNC; HGNC:15904; KAT14.
DR HPA; ENSG00000149474; Low tissue specificity.
DR MIM; 617501; gene.
DR neXtProt; NX_Q9H8E8; -.
DR OpenTargets; ENSG00000149474; -.
DR PharmGKB; PA26969; -.
DR VEuPathDB; HostDB:ENSG00000149474; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000001146; -.
DR HOGENOM; CLU_022855_0_0_1; -.
DR InParanoid; Q9H8E8; -.
DR OMA; RNWPWLQ; -.
DR OrthoDB; 1404086at2759; -.
DR PhylomeDB; Q9H8E8; -.
DR TreeFam; TF324809; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q9H8E8; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9H8E8; -.
DR BioGRID-ORCS; 57325; 31 hits in 1072 CRISPR screens.
DR ChiTaRS; KAT14; human.
DR GeneWiki; CSRP2BP; -.
DR GenomeRNAi; 57325; -.
DR Pharos; Q9H8E8; Tbio.
DR PRO; PR:Q9H8E8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H8E8; protein.
DR Bgee; ENSG00000149474; Expressed in deltoid and 183 other tissues.
DR ExpressionAtlas; Q9H8E8; baseline and differential.
DR Genevisible; Q9H8E8; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IPI:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0030274; F:LIM domain binding; NAS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR037829; KAT14.
DR PANTHER; PTHR20916:SF0; PTHR20916:SF0; 1.
DR Pfam; PF13673; Acetyltransf_10; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..782
FT /note="Cysteine-rich protein 2-binding protein"
FT /id="PRO_0000074603"
FT DOMAIN 638..782
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CID0"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000070"
FT VARIANT 214
FT /note="P -> L (in dbSNP:rs6081011)"
FT /id="VAR_028034"
FT VARIANT 400
FT /note="V -> G (in dbSNP:rs1205193)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_028035"
FT VARIANT 442
FT /note="R -> T (in dbSNP:rs2295182)"
FT /id="VAR_020466"
FT VARIANT 600
FT /note="P -> R (in dbSNP:rs11557577)"
FT /id="VAR_033839"
FT VARIANT 738
FT /note="A -> S (in dbSNP:rs6081027)"
FT /id="VAR_048166"
FT CONFLICT 535
FT /note="R -> G (in Ref. 1; BAB14669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 88844 MW; E84FAEF06412EA77 CRC64;
MDSSIHLSSL ISRHDDEATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN
SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCSDCS ADGKEQYERL
KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC
LSVGSPMYFR SGAQEFGEPG WWKLVHNKPP TMKPEGEKLS ASTLKIKAAS KPTLDPIITV
EGLRKRASRN PVESAMELKE KRSRTQEAKD IRRAQKEAAG FLDRSTSSTP VKFISRGRRP
DVILEKGEVI DFSSLSSSDR TPLTSPSPSP SLDFSAPGTP ASHSATPSLL SEADLIPDVM
PPQALFHDDD EMEGDGVIDP GMEYVPPPAG SVASGPVVGV RKKVRGPEQI KQEVESEEEK
PDRMDIDSED TDSNTSLQTR AREKRKPQLE KDTKPKEPRY TPVSIYEEKL LLKRLEACPG
AVAMTPEARR LKRKLIVRQA KRDRGLPLFD LDQVVNAALL LVDGIYGAKE GGISRLPAGQ
ATYRTTCQDF RILDRYQTSL PSRKGFRHQT TKFLYRLVGS EDMAVDQSIV SPYTSRILKP
YIRRDYETKP PKLQLLSQIR SHLHRSDPHW TPEPDAPLDY CYVRPNHIPT INSMCQEFFW
PGIDLSECLQ YPDFSVVVLY KKVIIAFGFM VPDVKYNEAY ISFLFVHPEW RRAGIATFMI
YHLIQTCMGK DVTLHVSASN PAMLLYQKFG FKTEEYVLDF YDKYYPLEST ECKHAFFLRL
RR
