PPRC1_HUMAN
ID PPRC1_HUMAN Reviewed; 1664 AA.
AC Q5VV67; Q5VV66; Q6P3U5; Q6P3W1; Q76N31; Q9BUJ3; Q9BZE5; Q9Y4E0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator-related protein 1;
DE AltName: Full=PGC-1-related coactivator;
DE Short=PRC;
GN Name=PPRC1; Synonyms=KIAA0595;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH NRF1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11340167; DOI=10.1128/mcb.21.11.3738-3749.2001;
RA Andersson U., Scarpulla R.C.;
RT "Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear
RT respiratory factor 1-dependent transcription in mammalian cells.";
RL Mol. Cell. Biol. 21:3738-3749(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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 MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 998-1664 (ISOFORM 1), AND VARIANT ARG-834.
RC TISSUE=Placenta, and 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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=14550271; DOI=10.1016/j.bbrc.2003.09.076;
RA Savagner F., Mirebeau D., Jacques C., Guyetant S., Morgan C., Franc B.,
RA Reynier P., Malthiery Y.;
RT "PGC-1-related coactivator and targets are upregulated in thyroid
RT oncocytoma.";
RL Biochem. Biophys. Res. Commun. 310:779-784(2003).
RN [7]
RP FUNCTION, INTERACTION WITH CREB1 AND NRF1, AND INDUCTION.
RX PubMed=16908542; DOI=10.1128/mcb.00585-06;
RA Vercauteren K., Pasko R.A., Gleyzer N., Marino V.M., Scarpulla R.C.;
RT "PGC-1-related coactivator: immediate early expression and characterization
RT of a CREB/NRF-1 binding domain associated with cytochrome c promoter
RT occupancy and respiratory growth.";
RL Mol. Cell. Biol. 26:7409-7419(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1411 AND SER-1413, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-548 AND SER-1076,
RP AND 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 [11]
RP VARIANT GLN-1288.
RX PubMed=25676728; DOI=10.1002/humu.22764;
RA Jonsson F., Bystroem B., Davidson A.E., Backman L.J., Kellgren T.G.,
RA Tuft S.J., Koskela T., Ryden P., Sandgren O., Danielson P.,
RA Hardcastle A.J., Golovleva I.;
RT "Mutations in collagen, type XVII, alpha 1 (COL17A1) cause epithelial
RT recurrent erosion dystrophy (ERED).";
RL Hum. Mutat. 36:463-473(2015).
CC -!- FUNCTION: Acts as a coactivator during transcriptional activation of
CC nuclear genes related to mitochondrial biogenesis and cell growth.
CC Involved in the transcription coactivation of CREB and NRF1 target
CC genes. {ECO:0000269|PubMed:11340167, ECO:0000269|PubMed:16908542}.
CC -!- SUBUNIT: Interacts with CREB1 and NRF1. {ECO:0000269|PubMed:11340167,
CC ECO:0000269|PubMed:16908542}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11340167}.
CC Note=Colocalizes with NRF1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VV67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VV67-2; Sequence=VSP_027229, VSP_027230, VSP_027231;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart and skeletal muscle,
CC moderately in lung, placenta, intestine, liver, kidney, spleen, thymus,
CC colon and brain. Also expressed in several oncocytic thyroid tumors.
CC {ECO:0000269|PubMed:11340167, ECO:0000269|PubMed:14550271}.
CC -!- INDUCTION: Up-regulated by serum (at protein level).
CC {ECO:0000269|PubMed:16908542}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02561.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA25521.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF325193; AAK11573.1; -; mRNA.
DR EMBL; AB011167; BAA25521.2; ALT_INIT; mRNA.
DR EMBL; AL500527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002561; AAH02561.2; ALT_FRAME; mRNA.
DR EMBL; BC063806; AAH63806.1; -; mRNA.
DR EMBL; BC063829; AAH63829.1; -; mRNA.
DR CCDS; CCDS7529.1; -. [Q5VV67-1]
DR PIR; T00273; T00273.
DR RefSeq; NP_001275656.1; NM_001288727.1.
DR RefSeq; NP_001275657.1; NM_001288728.1. [Q5VV67-2]
DR RefSeq; NP_055877.3; NM_015062.4. [Q5VV67-1]
DR AlphaFoldDB; Q5VV67; -.
DR SMR; Q5VV67; -.
DR BioGRID; 116713; 15.
DR ELM; Q5VV67; -.
DR IntAct; Q5VV67; 10.
DR MINT; Q5VV67; -.
DR STRING; 9606.ENSP00000278070; -.
DR iPTMnet; Q5VV67; -.
DR PhosphoSitePlus; Q5VV67; -.
DR BioMuta; PPRC1; -.
DR DMDM; 74756889; -.
DR EPD; Q5VV67; -.
DR jPOST; Q5VV67; -.
DR MassIVE; Q5VV67; -.
DR MaxQB; Q5VV67; -.
DR PaxDb; Q5VV67; -.
DR PeptideAtlas; Q5VV67; -.
DR PRIDE; Q5VV67; -.
DR ProteomicsDB; 65451; -. [Q5VV67-1]
DR ProteomicsDB; 65452; -. [Q5VV67-2]
DR Antibodypedia; 48608; 127 antibodies from 25 providers.
DR DNASU; 23082; -.
DR Ensembl; ENST00000278070.7; ENSP00000278070.2; ENSG00000148840.11. [Q5VV67-1]
DR GeneID; 23082; -.
DR KEGG; hsa:23082; -.
DR MANE-Select; ENST00000278070.7; ENSP00000278070.2; NM_015062.5; NP_055877.3.
DR UCSC; uc001kum.5; human. [Q5VV67-1]
DR CTD; 23082; -.
DR DisGeNET; 23082; -.
DR GeneCards; PPRC1; -.
DR HGNC; HGNC:30025; PPRC1.
DR HPA; ENSG00000148840; Low tissue specificity.
DR MIM; 617462; gene.
DR neXtProt; NX_Q5VV67; -.
DR OpenTargets; ENSG00000148840; -.
DR PharmGKB; PA134886297; -.
DR VEuPathDB; HostDB:ENSG00000148840; -.
DR eggNOG; ENOG502QQME; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_001907_0_0_1; -.
DR InParanoid; Q5VV67; -.
DR OMA; IGECHTV; -.
DR OrthoDB; 94418at2759; -.
DR PhylomeDB; Q5VV67; -.
DR TreeFam; TF343068; -.
DR PathwayCommons; Q5VV67; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q5VV67; -.
DR BioGRID-ORCS; 23082; 401 hits in 1092 CRISPR screens.
DR ChiTaRS; PPRC1; human.
DR GeneWiki; PPRC1; -.
DR GenomeRNAi; 23082; -.
DR Pharos; Q5VV67; Tbio.
DR PRO; PR:Q5VV67; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VV67; protein.
DR Bgee; ENSG00000148840; Expressed in left uterine tube and 176 other tissues.
DR ExpressionAtlas; Q5VV67; baseline and differential.
DR Genevisible; Q5VV67; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd12624; RRM_PRC; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034597; PRC.
DR InterPro; IPR034834; PRC_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF5; PTHR15528:SF5; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..1664
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator-related protein 1"
FT /id="PRO_0000296666"
FT DOMAIN 1543..1619
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..467
FT /note="Necessary for interaction with CREB1 and NRF1 and
FT for transcriptional coactivation"
FT /evidence="ECO:0000269|PubMed:16908542"
FT REGION 436..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1450
FT /note="Necessary for interaction with CREB1 and NRF1"
FT /evidence="ECO:0000269|PubMed:16908542"
FT COMPBIAS 480..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1471
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027229"
FT VAR_SEQ 121..147
FT /note="DQNEVSLLTALTEILDNADSENLSPFD -> MRHCWGPCRATWMPPLSPSLR
FT ILGALE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027230"
FT VAR_SEQ 1518..1519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027231"
FT VARIANT 536
FT /note="S -> G (in dbSNP:rs17114388)"
FT /id="VAR_034633"
FT VARIANT 834
FT /note="P -> R (in dbSNP:rs17855877)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034634"
FT VARIANT 1288
FT /note="R -> Q (in dbSNP:rs118161359)"
FT /evidence="ECO:0000269|PubMed:25676728"
FT /id="VAR_074628"
FT CONFLICT 33
FT /note="G -> R (in Ref. 1; AAK11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="L -> Q (in Ref. 1; AAK11573)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Q -> H (in Ref. 1; AAK11573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1664 AA; 177544 MW; 01D4138F80C620E8 CRC64;
MAARRGRRDG VAPPPSGGPG PDPGGGARGS GWGSRSQAPY GTLGAVSGGE QVLLHEEAGD
SGFVSLSRLG PSLRDKDLEM EELMLQDETL LGTMQSYMDA SLISLIEDFG SLGESRLSLE
DQNEVSLLTA LTEILDNADS ENLSPFDSIP DSELLVSPRE GSSLHKLLTL SRTPPERDLI
TPVDPLGPST GSSRGSGVEM SLPDPSWDFS PPSFLETSSP KLPSWRPPRS RPRWGQSPPP
QQRSDGEEEE EVASFSGQIL AGELDNCVSS IPDFPMHLAC PEEEDKATAA EMAVPAAGDE
SISSLSELVR AMHPYCLPNL THLASLEDEL QEQPDDLTLP EGCVVLEIVG QAATAGDDLE
IPVVVRQVSP GPRPVLLDDS LETSSALQLL MPTLESETEA AVPKVTLCSE KEGLSLNSEE
KLDSACLLKP REVVEPVVPK EPQNPPANAA PGSQRARKGR KKKSKEQPAA CVEGYARRLR
SSSRGQSTVG TEVTSQVDNL QKQPQEELQK ESGPLQGKGK PRAWARAWAA ALENSSPKNL
ERSAGQSSPA KEGPLDLYPK LADTIQTNPI PTHLSLVDSA QASPMPVDSV EADPTAVGPV
LAGPVPVDPG LVDLASTSSE LVEPLPAEPV LINPVLADSA AVDPAVVPIS DNLPPVDAVP
SGPAPVDLAL VDPVPNDLTP VDPVLVKSRP TDPRRGAVSS ALGGSAPQLL VESESLDPPK
TIIPEVKEVV DSLKIESGTS ATTHEARPRP LSLSEYRRRR QQRQAETEER SPQPPTGKWP
SLPETPTGLA DIPCLVIPPA PAKKTALQRS PETPLEICLV PVGPSPASPS PEPPVSKPVA
SSPTEQVPSQ EMPLLARPSP PVQSVSPAVP TPPSMSAALP FPAGGLGMPP SLPPPPLQPP
SLPLSMGPVL PDPFTHYAPL PSWPCYPHVS PSGYPCLPPP PTVPLVSGTP GAYAVPPTCS
VPWAPPPAPV SPYSSTCTYG PLGWGPGPQH APFWSTVPPP PLPPASIGRA VPQPKMESRG
TPAGPPENVL PLSMAPPLSL GLPGHGAPQT EPTKVEVKPV PASPHPKHKV SALVQSPQMK
ALACVSAEGV TVEEPASERL KPETQETRPR EKPPLPATKA VPTPRQSTVP KLPAVHPARL
RKLSFLPTPR TQGSEDVVQA FISEIGIEAS DLSSLLEQFE KSEAKKECPP PAPADSLAVG
NSGGVDIPQE KRPLDRLQAP ELANVAGLTP PATPPHQLWK PLAAVSLLAK AKSPKSTAQE
GTLKPEGVTE AKHPAAVRLQ EGVHGPSRVH VGSGDHDYCV RSRTPPKKMP ALVIPEVGSR
WNVKRHQDIT IKPVLSLGPA APPPPCIAAS REPLDHRTSS EQADPSAPCL APSSLLSPEA
SPCRNDMNTR TPPEPSAKQR SMRCYRKACR SASPSSQGWQ GRRGRNSRSV SSGSNRTSEA
SSSSSSSSSS SRSRSRSLSP PHKRWRRSSC SSSGRSRRCS SSSSSSSSSS SSSSSSSSSR
SRSRSPSPRR RSDRRRRYSS YRSHDHYQRQ RVLQKERAIE ERRVVFIGKI PGRMTRSELK
QRFSVFGEIE ECTIHFRVQG DNYGFVTYRY AEEAFAAIES GHKLRQADEQ PFDLCFGGRR
QFCKRSYSDL DSNREDFDPA PVKSKFDSLD FDTLLKQAQK NLRR
