CPT2_RAT
ID CPT2_RAT Reviewed; 658 AA.
AC P18886; P97781;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 158.
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|RGD:2398}; Synonyms=Cpt-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2355018; DOI=10.1016/s0021-9258(18)87006-5;
RA Woeltje K.F., Esser V., Weis B.C., Sen A., Cox W.F., McPhaul M.J.,
RA Slaughter C.A., Foster D.W., McGarry J.D.;
RT "Cloning, sequencing, and expression of a cDNA encoding rat liver
RT mitochondrial carnitine palmitoyltransferase II.";
RL J. Biol. Chem. 265:10720-10725(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9136891; DOI=10.1021/bi962875p;
RA de Vries Y., Arvidson D.N., Waterham H.R., Cregg J.M., Woldegiorgis G.;
RT "Functional characterization of mitochondrial carnitine
RT palmitoyltransferases I and II expressed in the yeast Pichia pastoris.";
RL Biochemistry 36:5285-5292(1997).
RN [3]
RP PEPTIDE CLEAVAGE SITE.
RX PubMed=1869564; DOI=10.1016/s0021-9258(18)98636-9;
RA Brown N.F., Esser V., Gonzalez A.D., Evans C.T., Slaughter C.A.,
RA Foster D.W., McGarry J.D.;
RT "Mitochondrial import and processing of rat liver carnitine
RT palmitoyltransferase II defines the amino terminus of the mature protein.
RT Possibility of differential modification of the rat and human isoforms.";
RL J. Biol. Chem. 266:15446-15449(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-656.
RX PubMed=16781677; DOI=10.1016/j.bbrc.2006.06.006;
RA Hsiao Y.-S., Jogl G., Esser V., Tong L.;
RT "Crystal structure of rat carnitine palmitoyltransferase II (CPT-II).";
RL Biochem. Biophys. Res. Commun. 346:974-980(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-658 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG ST1326.
RX PubMed=16615913; DOI=10.1016/j.str.2006.01.008;
RA Rufer A.C., Thoma R., Benz J., Stihle M., Gsell B., De Roo E., Banner D.W.,
RA Mueller F., Chomienne O., Hennig M.;
RT "The crystal structure of carnitine palmitoyltransferase 2 and implications
RT for diabetes treatment.";
RL Structure 14:713-723(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 27-658 IN COMPLEX WITH
RP PALMITOYL-AMINOCARNITHINE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17585909; DOI=10.1016/j.febslet.2007.05.080;
RA Rufer A.C., Lomize A., Benz J., Chomienne O., Thoma R., Hennig M.;
RT "Carnitine palmitoyltransferase 2: analysis of membrane association and
RT complex structure with a substrate analog.";
RL FEBS Lett. 581:3247-3252(2007).
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
CC {ECO:0000269|PubMed:17585909}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17585909}; Matrix side
CC {ECO:0000269|PubMed:17585909}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; J05470; AAB02339.1; -; mRNA.
DR EMBL; U88295; AAB48047.1; -; mRNA.
DR PIR; A35447; A35447.
DR RefSeq; NP_037062.1; NM_012930.1.
DR PDB; 2DEB; X-ray; 1.60 A; A/B=27-658.
DR PDB; 2FW3; X-ray; 2.50 A; A=27-658.
DR PDB; 2FYO; X-ray; 2.00 A; A=27-658.
DR PDB; 2H4T; X-ray; 1.90 A; A/B=32-656.
DR PDB; 2RCU; X-ray; 1.78 A; A/B=27-658.
DR PDB; 4EP9; X-ray; 2.03 A; A=27-658.
DR PDB; 4EPH; X-ray; 2.30 A; A=27-658.
DR PDB; 4EYW; X-ray; 1.88 A; A/B=27-658.
DR PDBsum; 2DEB; -.
DR PDBsum; 2FW3; -.
DR PDBsum; 2FYO; -.
DR PDBsum; 2H4T; -.
DR PDBsum; 2RCU; -.
DR PDBsum; 4EP9; -.
DR PDBsum; 4EPH; -.
DR PDBsum; 4EYW; -.
DR AlphaFoldDB; P18886; -.
DR SMR; P18886; -.
DR BioGRID; 247448; 2.
DR STRING; 10116.ENSRNOP00000016954; -.
DR BindingDB; P18886; -.
DR ChEMBL; CHEMBL4037; -.
DR DrugCentral; P18886; -.
DR iPTMnet; P18886; -.
DR PhosphoSitePlus; P18886; -.
DR jPOST; P18886; -.
DR PaxDb; P18886; -.
DR PRIDE; P18886; -.
DR GeneID; 25413; -.
DR KEGG; rno:25413; -.
DR UCSC; RGD:2398; rat.
DR CTD; 1376; -.
DR RGD; 2398; Cpt2.
DR eggNOG; KOG3719; Eukaryota.
DR InParanoid; P18886; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P18886; -.
DR BioCyc; MetaCyc:MON-14441; -.
DR BRENDA; 2.3.1.21; 5301.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR SABIO-RK; P18886; -.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P18886; -.
DR PRO; PR:P18886; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0016746; F:acyltransferase activity; ISO:RGD.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; TAS:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
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 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT CHAIN 26..658
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000004427"
FT TOPO_DOM 26..178
FT /note="Mitochondrial matrix"
FT INTRAMEM 179..208
FT /note="Note=Mitochondrial inner membrane"
FT TOPO_DOM 209..658
FT /note="Mitochondrial matrix"
FT ACT_SITE 372
FT /note="Proton acceptor"
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 BINDING 488
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT BINDING 499
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT MOD_RES 69
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 85
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 424
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 439
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT CONFLICT 135
FT /note="M -> V (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Q -> R (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> I (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="L -> S (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="D -> E (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="S -> A (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="T -> S (in Ref. 2; AAB48047)"
FT /evidence="ECO:0000305"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4EYW"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2FW3"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:2DEB"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2RCU"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 421..438
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 463..479
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 507..517
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 525..547
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 553..565
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:2DEB"
FT HELIX 577..582
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 621..627
FT /evidence="ECO:0007829|PDB:2DEB"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:2FW3"
FT HELIX 633..651
FT /evidence="ECO:0007829|PDB:2DEB"
SQ SEQUENCE 658 AA; 74110 MW; E48D1429E6B2EB27 CRC64;
MMPRLLFRAW PRCPSLVLGA PSRPLSAVSG PDDYLQHSIV PTMHYQDSLP RLPIPKLEDT
MKRYLNAQKP LLDDSQFRRT EALCKNFETG VGKELHAHLL AQDKQNKHTS YISGPWFDMY
LTARDSIVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLQAGL LEPEVFHLNP
SKSDTDAFKR LIRFVPPSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPRPN RDELFTDTKA
RHLLVLRKGH FYVFDVLDQD GNIVNPLEIQ AHLKYILSDS SPVPEFPVAY LTSENRDVWA
ELRQKLIFDG NEETLKKVDS AVFCLCLDDF PMKDLIHLSH TMLHGDGTNR WFDKSFNLIV
AEDGTAAVHF EHSWGDGVAV LRFFNEVFRD STQTPAITPQ SQPAATNSSA SVETLSFNLS
GALKAGITAA KEKFDTTVKT LSIDSIQFQR GGKEFLKKKQ LSPDAVAQLA FQMAFLRQYG
QTVATYESCS TAAFKHGRTE TIRPASIFTK RCSEAFVRDP SKHSVGELQH MMAECSKYHG
QLTKEAAMGQ GFDRHLYALR YLATARGLNL PELYLDPAYQ QMNHNILSTS TLNSPAVSLG
GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDIFDA LEGKAIKT
