CPT2_MOUSE
ID CPT2_MOUSE Reviewed; 658 AA.
AC P52825; Q3TFS0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000305};
DE EC=2.3.1.21 {ECO:0000250|UniProtKB:P23786};
DE AltName: Full=Carnitine palmitoyltransferase II;
DE Short=CPT II;
DE Flags: Precursor;
GN Name=Cpt2 {ECO:0000312|MGI:MGI:109176}; Synonyms=Cpt-2;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=8307575; DOI=10.1016/s0888-7543(05)80368-4;
RA Gelb B.D.;
RT "Genomic structure of and a cardiac promoter for the mouse carnitine
RT palmitoyltransferase II gene.";
RL Genomics 18:651-655(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-85; LYS-239; LYS-418;
RP LYS-424; LYS-439; LYS-510 AND LYS-544, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-239; LYS-305; LYS-418;
RP LYS-510 AND LYS-544, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Involved in the intramitochondrial synthesis of
CC acylcarnitines from accumulated acyl-CoA metabolites. Reconverts
CC acylcarnitines back into the respective acyl-CoA esters that can then
CC undergo beta-oxidation, an essential step for the mitochondrial uptake
CC of long-chain fatty acids and their subsequent beta-oxidation in the
CC mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18)
CC acyl-CoA esters. {ECO:0000250|UniProtKB:P23786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + dodecanoyl-CoA = CoA + O-dodecanoyl-R-
CC carnitine; Xref=Rhea:RHEA:40279, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:77086;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + tetradecanoyl-CoA = CoA + O-tetradecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44832, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:84634;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octadecanoyl-CoA = CoA + O-octadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44840, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:84644;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + eicosanoyl-CoA = CoA + O-eicosanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44844, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:84645;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44848, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:65060, ChEBI:CHEBI:84647;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(5Z)-
CC tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44852, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:84649, ChEBI:CHEBI:84650;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC octadecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44856, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:84651;
CC Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000250|UniProtKB:P23786};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P23786}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U01170; AAA18922.1; -; Unassigned_DNA.
DR EMBL; U01166; AAA18922.1; JOINED; Unassigned_DNA.
DR EMBL; U01167; AAA18922.1; JOINED; Unassigned_DNA.
DR EMBL; U01168; AAA18922.1; JOINED; Unassigned_DNA.
DR EMBL; U01169; AAA18922.1; JOINED; Unassigned_DNA.
DR EMBL; U01163; AAA18921.1; -; mRNA.
DR EMBL; AK169038; BAE40828.1; -; mRNA.
DR EMBL; AL611936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL30761.1; -; Genomic_DNA.
DR EMBL; BC138514; AAI38515.1; -; mRNA.
DR EMBL; BC145859; AAI45860.1; -; mRNA.
DR CCDS; CCDS18443.1; -.
DR PIR; A49362; A49362.
DR RefSeq; NP_034079.2; NM_009949.2.
DR AlphaFoldDB; P52825; -.
DR SMR; P52825; -.
DR BioGRID; 198865; 25.
DR IntAct; P52825; 1.
DR STRING; 10090.ENSMUSP00000030345; -.
DR iPTMnet; P52825; -.
DR PhosphoSitePlus; P52825; -.
DR SwissPalm; P52825; -.
DR EPD; P52825; -.
DR jPOST; P52825; -.
DR MaxQB; P52825; -.
DR PaxDb; P52825; -.
DR PeptideAtlas; P52825; -.
DR PRIDE; P52825; -.
DR ProteomicsDB; 284004; -.
DR Antibodypedia; 33067; 496 antibodies from 36 providers.
DR DNASU; 12896; -.
DR Ensembl; ENSMUST00000030345; ENSMUSP00000030345; ENSMUSG00000028607.
DR GeneID; 12896; -.
DR KEGG; mmu:12896; -.
DR UCSC; uc008uan.2; mouse.
DR CTD; 1376; -.
DR MGI; MGI:109176; Cpt2.
DR VEuPathDB; HostDB:ENSMUSG00000028607; -.
DR eggNOG; KOG3719; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_4_2_1; -.
DR InParanoid; P52825; -.
DR OMA; HILVMRR; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P52825; -.
DR TreeFam; TF315202; -.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 12896; 3 hits in 74 CRISPR screens.
DR PRO; PR:P52825; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P52825; protein.
DR Bgee; ENSMUSG00000028607; Expressed in brown adipose tissue and 256 other tissues.
DR ExpressionAtlas; P52825; baseline and differential.
DR Genevisible; P52825; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR Gene3D; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transferase; Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..658
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000004426"
FT TOPO_DOM 26..178
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT INTRAMEM 179..208
FT /note="Note=Mitochondrial inner membrane"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..658
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 452..464
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 85
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 418
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 418
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 424
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 439
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 510
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 510
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 503
FT /note="R -> C (in Ref. 1; AAA18921/AAA18922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 73981 MW; 3A02DA887DF1D3A1 CRC64;
MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP RLPIPKLEDT
MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL AQDKQNKHTS YISGPWFDMY
LTARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLRAGL LEPEVFHLNP
ARSDTDAFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPKPS RDELFTDTKA
RHLLVLRKGH FYVFDVLDQD GNIVNPSEIQ AHLKYILSDS SPVPEFPLAY LTSENRDVWA
ELRQKLIHGG NEETLRKVDS AVFCLCLDDF PMKDLVHLSH TMLHGDGTNR WFDKSFNLIV
AKDGTAAVHF EHAWGDGVAV LRFFNEVFRD STQTPAIAPQ SQPAATDSSV SVQKLSFKLS
SALKAGVTAA KEKFDATMKT LTIDAIQFQR GGKEFLKKKK LSPDAVAQLA FQMAFLRQYG
QTVATYESCS TAAFKHGRTE TIRPASIFTK RCSEAFVREP SKHSVGELQH MMAECSKYHG
QLTKEAAMGQ GFDRHLFALR YLAAARGVTL PELYQDPAYQ RINHNILSTS TLSSPAVSLG
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDMFDA LEGKAIKT
