ID   CCAR1_HUMAN             Reviewed;        1150 AA.
AC   Q8IX12; A0JLT7; A1L4P7; A8K9D4; B4DNP8; B4DRK8; Q32NE3; Q5EBM3;
AC   Q5VUP6; Q6PIZ0; Q6X935; Q9H8N4; Q9NVA7; Q9NVQ0; Q9NWM6;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   05-OCT-2010, entry version 64.
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;
DE   AltName: Full=Death inducer with SAP domain;
GN   Name=CCAR1; Synonyms=CARP1, DIS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RX   MEDLINE=22817892; PubMed=12816952; DOI=10.1074/jbc.M303173200;
RA   Rishi A.K., Zhang L., Boyanapalli M., Wali A., Mohammad R.M., Yu Y.,
RA   Fontana J.A., Hatfield J.S., Dawson M.I., Majumdar A.P.N.,
RA   Reichert U.;
RT   "Identification and characterization of a cell cycle and apoptosis
RT   regulatory protein-1 as a novel mediator of apoptosis signaling by
RT   retinoid CD437.";
RL   J. Biol. Chem. 278:33422-33435(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 2).
RC   TISSUE=Hepatoma, Lung, Placenta, Teratocarcinoma, and Thymus;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-818 (ISOFORM 1).
RC   TISSUE=Cerebellum, Lung, Lymph, Muscle, and Skin;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-333; SER-339
RP   AND SER-343, AND MASS SPECTROMETRY.
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [10]
RP   INTERACTION WITH CALCOCO1.
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
RT   receptor transcription complexes.";
RL   Mol. Cell 31:510-519(2008).
RN   [11]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18655026; DOI=10.1002/pmic.200700887;
RA   Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,
RA   Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT   "Proteomic analysis of ubiquitinated proteins in normal hepatocyte
RT   cell line Chang liver cells.";
RL   Proteomics 8:2885-2896(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-607.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Associates with components of the Mediator and p160
CC       coactivator complexes that play a role as intermediaries
CC       transducing regulatory signals from upstream transcriptional
CC       activator proteins to basal transcription machinery at the core
CC       promoter. Recruited to endogenous nuclear receptor target genes in
CC       response to the appropriate hormone. Also functions as a p53
CC       coactivator. May thus play an important role in transcriptional
CC       regulation (By similarity). May be involved in apoptosis signaling
CC       in the presence of the reinoid CD437. Apoptosis induction involves
CC       sequestration of 14-3-3 protein(s) and mediated altered expression
CC       of multiple cell cycle regulatory genes including MYC, CCNB1 and
CC       CDKN1A. Plays a role in cell cycle progression and/or cell
CC       proliferation.
CC   -!- SUBUNIT: Directly interacts with CALCOCO1, ESR1, NR3C1 and TP53
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IX12-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IX12-2; Sequence=VSP_037736;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in various epithelial cancer cell
CC       lines, including breast, colon, prostate, pancreatic and leukemia.
CC       Expression is regulated by growth factors.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 1 SAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26036.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAI08683.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAA91354.1; Type=Erroneous initiation;
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DR   EMBL; AY249140; AAP82002.1; -; mRNA.
DR   EMBL; AF465616; AAO17319.1; -; mRNA.
DR   EMBL; AK000741; BAA91354.1; ALT_INIT; mRNA.
DR   EMBL; AK001452; BAA91700.1; -; mRNA.
DR   EMBL; AK001701; BAA91847.1; -; mRNA.
DR   EMBL; AK023438; BAB14574.1; -; mRNA.
DR   EMBL; AK298004; BAG60310.1; -; mRNA.
DR   EMBL; AK299307; BAG61320.1; -; mRNA.
DR   EMBL; AK292649; BAF85338.1; -; mRNA.
DR   EMBL; AL513534; CAH70221.1; -; Genomic_DNA.
DR   EMBL; AL391539; CAH70221.1; JOINED; Genomic_DNA.
DR   EMBL; AL391539; CAH73835.1; -; Genomic_DNA.
DR   EMBL; AL513534; CAH73835.1; JOINED; Genomic_DNA.
DR   EMBL; CH471083; EAW54302.1; -; Genomic_DNA.
DR   EMBL; BC015475; AAH15475.1; -; mRNA.
DR   EMBL; BC026036; AAH26036.1; ALT_SEQ; mRNA.
DR   EMBL; BC089420; AAH89420.1; -; mRNA.
DR   EMBL; BC130626; AAI30627.1; -; mRNA.
DR   EMBL; BC132725; AAI32726.1; -; mRNA.
DR   EMBL; BC108682; AAI08683.1; ALT_SEQ; mRNA.
DR   IPI; IPI00217357; -.
DR   IPI; IPI00939119; -.
DR   RefSeq; NP_060707.2; -.
DR   UniGene; Hs.49853; -.
DR   ProteinModelPortal; Q8IX12; -.
DR   SMR; Q8IX12; 145-212, 628-673.
DR   IntAct; Q8IX12; 8.
DR   MINT; MINT-1139760; -.
DR   STRING; Q8IX12; -.
DR   PhosphoSite; Q8IX12; -.
DR   PeptideAtlas; Q8IX12; -.
DR   PRIDE; Q8IX12; -.
DR   Ensembl; ENST00000265872; ENSP00000265872; ENSG00000060339.
DR   GeneID; 55749; -.
DR   KEGG; hsa:55749; -.
DR   UCSC; uc001joo.1; human.
DR   CTD; 55749; -.
DR   GeneCards; GC10P070480; -.
DR   H-InvDB; HIX0008877; -.
DR   HGNC; HGNC:24236; CCAR1.
DR   HPA; HPA007856; -.
DR   MIM; 612569; gene.
DR   PharmGKB; PA134920227; -.
DR   HOVERGEN; HBG079908; -.
DR   InParanoid; Q8IX12; -.
DR   OMA; NTAVLDP; -.
DR   OrthoDB; EOG9Z91G5; -.
DR   PhylomeDB; Q8IX12; -.
DR   Reactome; REACT_1675; mRNA Processing.
DR   Reactome; REACT_71; Gene Expression.
DR   NextBio; 60733; -.
DR   ArrayExpress; Q8IX12; -.
DR   Bgee; Q8IX12; -.
DR   CleanEx; HS_CCAR1; -.
DR   Genevestigator; Q8IX12; -.
DR   GermOnline; ENSG00000060339; Homo sapiens.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; EXP:Reactome.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell cycle; Coiled coil;
KW   Complete proteome; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Polymorphism; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1   1150       Cell division cycle and apoptosis
FT                                regulator protein 1.
FT                                /FTId=PRO_0000233148.
FT   DOMAIN      636    670       SAP.
FT   COILED      594    618       Potential.
FT   COILED     1033   1114       Potential.
FT   COMPBIAS     73     79       Poly-Ala.
FT   COMPBIAS    293    361       Arg-rich.
FT   COMPBIAS    673    889       Glu-rich.
FT   MOD_RES     214    214       Phosphoserine.
FT   MOD_RES     329    329       Phosphoserine.
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES    1149   1149       Phosphoserine.
FT   CROSSLNK    637    637       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   VAR_SEQ      83     97       Missing (in isoform 2).
FT                                /FTId=VSP_037736.
FT   VARIANT     588    588       T -> I (in dbSNP:rs1782338).
FT                                /FTId=VAR_058330.
FT   VARIANT     607    607       E -> K (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035497.
FT   VARIANT     681    681       E -> G (in dbSNP:rs1060145).
FT                                /FTId=VAR_058331.
FT   VARIANT     747    747       M -> V (in dbSNP:rs11542602).
FT                                /FTId=VAR_058332.
FT   CONFLICT    296    296       D -> Y (in Ref. 3; BAA91354).
FT   CONFLICT    305    305       N -> S (in Ref. 3; BAG60310).
FT   CONFLICT    492    492       K -> E (in Ref. 3; BAA91847).
FT   CONFLICT    618    618       D -> Y (in Ref. 6; AAH15475).
FT   CONFLICT    650    650       S -> G (in Ref. 2; AAO17319 and 3;
FT                                BAA91700).
FT   CONFLICT    723    723       L -> S (in Ref. 3; BAF85338).
FT   CONFLICT    801    803       EKD -> KKK (in Ref. 6; AAH89420).
FT   CONFLICT    816    818       EER -> KKK (in Ref. 6; AAH15475).
FT   CONFLICT    853    853       D -> G (in Ref. 1, 2 and 3; BAA91700).
FT   CONFLICT   1104   1104       N -> S (in Ref. 1, 2 and 3; BAA91700).
SQ   SEQUENCE   1150 AA;  132821 MW;  30618DCC8097F552 CRC64;
     MAQFGGQKNP PWATQFTATA VSQPAALGVQ QPSLLGASPT IYTQQTALAA AGLTTQTPAN
     YQLTQTAALQ QQAAAAAAAL QQQYSQPQQA LYSVQQQLQQ PQQTLLTQPA VALPTSLSLS
     TPQPTAQITV SYPTPRSSQQ QTQPQKQRVF TGVVTKLHDT FGFVDEDVFF QLSAVKGKTP
     QVGDRVLVEA TYNPNMPFKW NAQRIQTLPN QNQSQTQPLL KTPPAVLQPI APQTTFGVQT
     QPQPQSLLQA QISAASITPL LQTQPQPLLQ QPQQKAGLLQ PPVRIVSQPQ PARRLDPPSR
     FSGRNDRGDQ VPNRKDDRSR ERERERRRSR ERSPQRKRSR ERSPRRERER SPRRVRRVVP
     RYTVQFSKFS LDCPSCDMME LRRRYQNLYI PSDFFDAQFT WVDAFPLSRP FQLGNYCNFY
     VMHREVESLE KNMAILDPPD ADHLYSAKVM LMASPSMEDL YHKSCALAED PQELRDGFQH
     PARLVKFLVG MKGKDEAMAI GGHWSPSLDG PDPEKDPSVL IKTAIRCCKA LTGIDLSVCT
     QWYRFAEIRY HRPEETHKGR TVPAHVETVV LFFPDVWHCL PTRSEWETLS RGYKQQLVEK
     LQGERKEADG EQDEEEKDDG EAKEISTPTH WSKLDPKTMK VNDLRKELES RALSSKGLKS
     QLIARLTKQL KVEEQKEEQK ELEKSEKEED EDDDRKSEDD KEEEERKRQE EIERQRRERR
     YILPDEPAII VHPNWAAKSG KFDCSIMSLS VLLDYRLEDN KEHSFEVSLF AELFNEMLQR
     DFGVRIYKSL LSLPEKEDKK EKDKKSKKDE RKDKKEERDD ETDEPKPKRR KSGDDKDKKE
     DRDERKKEDK RKDDSKDDDE TEEDNNQDEY DPMEAEEAED EEDDRDEEEM TKRDDKRDIN
     RYCKERPSKD KEKEKTQMIT INRDLLMAFV YFDQSHCGYL LEKDLEEILY TLGLHLSRAQ
     VKKLLNKVVL RESCFYRKLT DTSKDEENHE ESESLQEDML GNRLLLPTPT VKQESKDVEE
     NVGLIVYNGA MVDVGSLLQK LEKSEKVRAE VEQKLQLLEE KTDEDEKTIL NLENSNKSLS
     GELREVKKDL SQLQENLKIS ENMNLQFENQ MNKTIRNLST VMDEIHTVLK KDNVKNEDKD
     QKSKENGASV
//