CCAR1_MOUSE
ID CCAR1_MOUSE Reviewed; 1146 AA.
AC Q8CH18; Q05BR1; Q05DK6; Q6AXC9; Q6PAR2; Q80XE4; Q8BJY0; Q8BVN2; Q8CGG1;
AC Q9CSR5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cell division cycle and apoptosis regulator protein 1;
DE AltName: Full=Cell cycle and apoptosis regulatory protein 1;
DE Short=CARP-1;
GN Name=Ccar1; Synonyms=Carp1;
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] (ISOFORM 1).
RC STRAIN=Swiss Webster;
RA Tian Y., Li D., Benjamin T.;
RT "TAZ binding partners identified by mass spectrometry.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-833 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-797 (ISOFORM 3).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Kidney, and Mammary tumor;
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 FUNCTION, AND INTERACTION WITH CALCOCO1; ESR1; NR3C AND TP53.
RX PubMed=18722177; DOI=10.1016/j.molcel.2008.08.001;
RA Kim J.H., Yang C.K., Heo K., Roeder R.G., An W., Stallcup M.R.;
RT "CCAR1, a key regulator of mediator complex recruitment to nuclear receptor
RT transcription complexes.";
RL Mol. Cell 31:510-519(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Pancreas, Spleen, and
RC 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 FUNCTION.
RX PubMed=23887938; DOI=10.1093/nar/gkt644;
RA Seo W.Y., Jeong B.C., Yu E.J., Kim H.J., Kim S.H., Lim J.E., Kwon G.Y.,
RA Lee H.M., Kim J.H.;
RT "CCAR1 promotes chromatin loading of androgen receptor (AR) transcription
RT complex by stabilizing the association between AR and GATA2.";
RL Nucleic Acids Res. 41:8526-8536(2013).
RN [7]
RP FUNCTION, AND INTERACTION WITH MED1; GATA1 AND CALCOCO1.
RX PubMed=24245781; DOI=10.1111/gtc.12104;
RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
RT pathway for GATA1 function.";
RL Genes Cells 19:28-51(2014).
CC -!- FUNCTION: Associates with components of the Mediator and p160
CC coactivator complexes that play a role as intermediaries transducing
CC regulatory signals from upstream transcriptional activator proteins to
CC basal transcription machinery at the core promoter. Recruited to
CC endogenous nuclear receptor target genes in response to the appropriate
CC hormone. Also functions as a p53 coactivator. May thus play an
CC important role in transcriptional regulation. May be involved in
CC apoptosis signaling in the presence of the retinoid CD437. Apoptosis
CC induction involves sequestration of 14-3-3 protein(s) and mediated
CC altered expression of multiple cell cycle regulatory genes including
CC MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or
CC cell proliferation (By similarity). In association with CALCOCO1
CC enhances GATA1- and MED1-mediated transcriptional activation from the
CC gamma-globin promoter during erythroid differentiation of K562
CC erythroleukemia cells (PubMed:24245781). Can act as a both a
CC coactivator and corepressor of AR-mediated transcription. Contributes
CC to chromatin looping and AR transcription complex assembly by
CC stabilizing AR-GATA2 association on chromatin and facilitating MED1 and
CC RNA polymerase II recruitment to AR-binding sites. May play an
CC important role in the growth and tumorigenesis of prostate cancer cells
CC (PubMed:23887938). {ECO:0000250|UniProtKB:Q8IX12,
CC ECO:0000269|PubMed:23887938, ECO:0000269|PubMed:24245781}.
CC -!- SUBUNIT: Directly interacts with ESR1, NR3C1 and p53/TP53. Interacts
CC (via N-terminus) with CALCOCO1. Interacts with MED1 and GATA1.
CC Interacts with AR and GATA2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IX12, ECO:0000269|PubMed:18722177,
CC ECO:0000269|PubMed:24245781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CH18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CH18-2; Sequence=VSP_018054, VSP_018055;
CC Name=3;
CC IsoId=Q8CH18-3; Sequence=VSP_037737;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10199.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH34174.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH39939.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH51052.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH60130.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH79652.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF465615; AAO17318.1; -; mRNA.
DR EMBL; AK012111; BAB28040.2; -; mRNA.
DR EMBL; AK077151; BAC36646.1; -; mRNA.
DR EMBL; AK078424; BAC37267.1; -; mRNA.
DR EMBL; BC010199; AAH10199.1; ALT_SEQ; mRNA.
DR EMBL; BC034174; AAH34174.1; ALT_SEQ; mRNA.
DR EMBL; BC039939; AAH39939.1; ALT_SEQ; mRNA.
DR EMBL; BC051052; AAH51052.1; ALT_SEQ; mRNA.
DR EMBL; BC060130; AAH60130.1; ALT_SEQ; mRNA.
DR EMBL; BC079652; AAH79652.1; ALT_SEQ; mRNA.
DR CCDS; CCDS35922.1; -. [Q8CH18-1]
DR RefSeq; NP_080477.1; NM_026201.3. [Q8CH18-1]
DR RefSeq; XP_006514057.1; XM_006513994.3. [Q8CH18-1]
DR RefSeq; XP_006514058.1; XM_006513995.3. [Q8CH18-1]
DR RefSeq; XP_006514059.1; XM_006513996.3. [Q8CH18-1]
DR RefSeq; XP_006514060.1; XM_006513997.2. [Q8CH18-3]
DR RefSeq; XP_011241839.1; XM_011243537.2. [Q8CH18-1]
DR AlphaFoldDB; Q8CH18; -.
DR SMR; Q8CH18; -.
DR BioGRID; 212231; 10.
DR IntAct; Q8CH18; 6.
DR MINT; Q8CH18; -.
DR STRING; 10090.ENSMUSP00000020268; -.
DR iPTMnet; Q8CH18; -.
DR PhosphoSitePlus; Q8CH18; -.
DR EPD; Q8CH18; -.
DR jPOST; Q8CH18; -.
DR MaxQB; Q8CH18; -.
DR PaxDb; Q8CH18; -.
DR PeptideAtlas; Q8CH18; -.
DR PRIDE; Q8CH18; -.
DR ProteomicsDB; 265357; -. [Q8CH18-1]
DR ProteomicsDB; 265358; -. [Q8CH18-2]
DR ProteomicsDB; 265359; -. [Q8CH18-3]
DR Antibodypedia; 2118; 218 antibodies from 31 providers.
DR DNASU; 67500; -.
DR Ensembl; ENSMUST00000020268; ENSMUSP00000020268; ENSMUSG00000020074. [Q8CH18-1]
DR Ensembl; ENSMUST00000219527; ENSMUSP00000151895; ENSMUSG00000020074. [Q8CH18-1]
DR GeneID; 67500; -.
DR KEGG; mmu:67500; -.
DR UCSC; uc007fja.2; mouse. [Q8CH18-1]
DR UCSC; uc007fjc.2; mouse. [Q8CH18-2]
DR UCSC; uc011xff.1; mouse. [Q8CH18-3]
DR CTD; 55749; -.
DR MGI; MGI:1914750; Ccar1.
DR VEuPathDB; HostDB:ENSMUSG00000020074; -.
DR eggNOG; KOG4246; Eukaryota.
DR GeneTree; ENSGT00530000063672; -.
DR HOGENOM; CLU_008030_0_0_1; -.
DR InParanoid; Q8CH18; -.
DR OMA; LRYSDMH; -.
DR OrthoDB; 614048at2759; -.
DR PhylomeDB; Q8CH18; -.
DR TreeFam; TF316387; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 67500; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Ccar1; mouse.
DR PRO; PR:Q8CH18; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8CH18; protein.
DR Bgee; ENSMUSG00000020074; Expressed in undifferentiated genital tubercle and 237 other tissues.
DR ExpressionAtlas; Q8CH18; baseline and differential.
DR Genevisible; Q8CH18; MM.
DR GO; GO:0005641; C:nuclear envelope lumen; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR045354; BURAN.
DR InterPro; IPR025224; CCAR1/CCAR2.
DR InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR045353; LAIKA.
DR InterPro; IPR025223; S1-like_RNA-bd_dom.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR14304; PTHR14304; 1.
DR Pfam; PF19257; BURAN; 1.
DR Pfam; PF14443; DBC1; 1.
DR Pfam; PF19256; LAIKA; 1.
DR Pfam; PF14444; S1-like; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM01122; DBC1; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Apoptosis; Cell cycle; Coiled coil;
KW Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1146
FT /note="Cell division cycle and apoptosis regulator protein
FT 1"
FT /id="PRO_0000233149"
FT DOMAIN 633..667
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..246
FT /note="Interaction with AR"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT REGION 200..657
FT /note="Interaction with GATA2"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT REGION 282..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..1146
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 671..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..615
FT /evidence="ECO:0000255"
FT COILED 1029..1110
FT /evidence="ECO:0000255"
FT COMPBIAS 296..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..696
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..885
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT MOD_RES 624
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT MOD_RES 664
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT MOD_RES 858
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT CROSSLNK 1008
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT CROSSLNK 1008
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT CROSSLNK 1063
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT CROSSLNK 1131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IX12"
FT VAR_SEQ 316..327
FT /note="SRERDRERRRSR -> RYVLRQCGGLEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018054"
FT VAR_SEQ 328..1146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018055"
FT VAR_SEQ 638..699
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037737"
FT CONFLICT 279
FT /note="P -> L (in Ref. 3; AAH79652)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="T -> A (in Ref. 3; AAH39939)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="K -> E (in Ref. 2; BAC37267)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="E -> G (in Ref. 2; BAC37267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1146 AA; 132060 MW; 6005A057B4F0BFF0 CRC64;
MAQFGGQKNP PWATQFTATA VSQPAALGVQ QPSLLGASPT IYTQQTALAA AGLTTQTPAN
YQLTQTAALQ QQAAAVLQQQ YSQPQQALYS VQQQLQQPQQ TILTQPAVAL PTSLSLSTPQ
PAAQITVSYP TPRSSQQQTQ PQKQRVFTGV VTKLHDTFGF VDEDVFFQLG AVKGKTPQVG
DRVLVEATYN PNMPFKWNAQ RIQTLPNQNQ SQTQPLLKTP TAVIQPIVPQ TTFGVQAQPQ
PQSLLQAQIS AASITPLLQT QPQPLLQQPQ QKAGLLQPPV RIVSQPQPAR RLDPPSRFSG
RNDRGDQVPN RKDDRSRERD RERRRSRERS PQRKRSRERS PRRERERSPR RVRRVVPRYT
VQFSKFSLDC PSCDMMELRR RYQNLYIPSD FFDAQFTWVD AFPLSRPFQL GNYCNFYVMH
REVESLEKNM AVLDPPDADH LYSAKVMLMA SPSMEDLYHK SCALAEDPQD LRDGFQHPAR
LVKFLVGMKG KDEAMAIGGH WSPSLDGPNP EKDPSVLIKT AIRCCKALTG IDLSVCTQWY
RFAEIRYHRP EETHKGRTVP AHVETVVLFF PDVWHCLPTR SEWETLSRGY KQQLVEKLQG
ERKKADGEQD EEEKDDGEVK EIATPTHWSK LDPKAMKVND LRKELESRAL SSKGLKSQLI
ARLTKQLKIE EQKEEQKELE KSEKEEEDED DKKSEDDKEE EERKRQEEVE RQRQERRYIL
PDEPAIIVHP NWAAKSGKFD CSIMSLSVLL DYRLEDNKEH SFEVSLFAEL FNEMLQRDFG
VRIYKSLLSL PEKEDKKDKE KKSKKEERKD KKEEREDDID EPKPKRRKSG DDKDKKEDRD
ERKKEEKRKD DSKDDDETEE DNNQDEYDPM EAEEAEDEDD DREEEEVKRD DKRDVSRYCK
DRPAKDKEKE KPQMVTVNRD LLMAFVYFDQ SHCGYLLEKD LEEILYTLGL HLSRAQVKKL
LNKVVLRESC FYRKLTDTSK DDENHEESEA LQEDMLGNRL LLPTPTIKQE SKDGEENVGL
IVYNGAMVDV GSLLQKLEKS EKVRAEVEQK LQLLEEKTDE DGKTILNLEN SNKSLSGELR
EVKKDLGQLQ ENLEVSENMN LQFENQLNKT LRNLSTVMDD IHTVLKKDNV KSEDRDEKSK
ENGSGV
