CH60_RAT
ID CH60_RAT Reviewed; 573 AA.
AC P63039; P19226; P19227; P97602;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=60 kDa heat shock protein, mitochondrial;
DE EC=5.6.1.7 {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Chaperonin 60;
DE Short=CPN60;
DE AltName: Full=HSP-65;
DE AltName: Full=Heat shock protein 60;
DE Short=HSP-60;
DE Short=Hsp60;
DE AltName: Full=Mitochondrial matrix protein P1;
DE Flags: Precursor;
GN Name=Hspd1; Synonyms=Hsp60;
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].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1979858; DOI=10.1093/nar/18.23.7162;
RA Peralta D., Hartman D.J., McIntosh A.M., Hoogenraad N.J., Hoej P.B.;
RT "cDNA and deduced amino acid sequence of rat liver prehsp60 (chaperonin-
RT 60).";
RL Nucleic Acids Res. 18:7162-7162(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley, and Wistar;
RA Ryan M.T., Herd S.M., Sberna G., Samuel M.M., Hoogenraad N.J., Hoej P.B.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 27-573.
RC TISSUE=Kidney;
RX PubMed=1976241; DOI=10.1093/nar/18.17.5309;
RA Venner T.J., Gupta R.S.;
RT "Nucleotide sequence of rat hsp60 (chaperonin, GroEL homolog) cDNA.";
RL Nucleic Acids Res. 18:5309-5309(1990).
RN [5]
RP PROTEIN SEQUENCE OF 38-58; 61-72; 143-157; 222-233; 237-309; 345-352;
RP 371-387; 397-405; 421-446; 463-469 AND 482-493, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Chaperonin implicated in mitochondrial protein import and
CC macromolecular assembly. Together with Hsp10, facilitates the correct
CC folding of imported proteins. May also prevent misfolding and promote
CC the refolding and proper assembly of unfolded polypeptides generated
CC under stress conditions in the mitochondrial matrix. The functional
CC units of these chaperonins consist of heptameric rings of the large
CC subunit Hsp60, which function as a back-to-back double ring. In a
CC cyclic reaction, Hsp60 ring complexes bind one unfolded substrate
CC protein per ring, followed by the binding of ATP and association with 2
CC heptameric rings of the co-chaperonin Hsp10. This leads to
CC sequestration of the substrate protein in the inner cavity of Hsp60
CC where, for a certain period of time, it can fold undisturbed by other
CC cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits
CC results in the dissociation of the chaperonin rings and the release of
CC ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P10809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P10809};
CC -!- SUBUNIT: Homoheptamer arranged in a ring structure. The functional
CC units of these chaperonins consist of heptameric rings of the large
CC subunit Hsp60, which function as a back-to-back double ring. Interacts
CC with 2 heptameric Hsp10 rings to form the symmetrical football complex
CC (By similarity). Interacts with HRAS (By similarity). Interacts with
CC ATAD3A. Interacts with ETFBKMT and EEF1AKMT3 (By similarity). Interacts
CC with MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P10809,
CC ECO:0000250|UniProtKB:P63038}.
CC -!- INTERACTION:
CC P63039; Q63690: Bax; NbExp=2; IntAct=EBI-432091, EBI-822405;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10809}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; X54793; CAA38564.1; -; mRNA.
DR EMBL; U68562; AAC53362.1; -; Genomic_DNA.
DR EMBL; BC086507; AAH86507.1; -; mRNA.
DR EMBL; X53585; CAA37654.1; -; mRNA.
DR PIR; S13089; HHRT60.
DR RefSeq; NP_071565.2; NM_022229.2.
DR RefSeq; XP_006244994.1; XM_006244932.2.
DR AlphaFoldDB; P63039; -.
DR SMR; P63039; -.
DR BioGRID; 248912; 10.
DR CORUM; P63039; -.
DR IntAct; P63039; 11.
DR MINT; P63039; -.
DR STRING; 10116.ENSRNOP00000063666; -.
DR CarbonylDB; P63039; -.
DR iPTMnet; P63039; -.
DR PhosphoSitePlus; P63039; -.
DR SwissPalm; P63039; -.
DR World-2DPAGE; 0004:P63039; -.
DR jPOST; P63039; -.
DR PaxDb; P63039; -.
DR PRIDE; P63039; -.
DR Ensembl; ENSRNOT00000066589; ENSRNOP00000063666; ENSRNOG00000014525.
DR GeneID; 63868; -.
DR KEGG; rno:63868; -.
DR UCSC; RGD:621314; rat.
DR CTD; 3329; -.
DR RGD; 621314; Hspd1.
DR eggNOG; KOG0356; Eukaryota.
DR GeneTree; ENSGT00390000005727; -.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; P63039; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; P63039; -.
DR TreeFam; TF300475; -.
DR Reactome; R-RNO-1268020; Mitochondrial protein import.
DR PRO; PR:P63039; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014525; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; P63039; baseline and differential.
DR Genevisible; P63039; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0030135; C:coated vesicle; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0031985; C:Golgi cisterna; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0097225; C:sperm midpiece; ISO:RGD.
DR GO; GO:0097524; C:sperm plasma membrane; IEA:Ensembl.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0034186; F:apolipoprotein A-I binding; ISO:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:RGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0140030; F:modification-dependent protein binding; IPI:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006458; P:'de novo' protein folding; IC:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:RGD.
DR GO; GO:0042113; P:B cell activation; ISO:RGD.
DR GO; GO:0042100; P:B cell proliferation; ISO:RGD.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
DR GO; GO:0048291; P:isotype switching to IgG isotypes; ISO:RGD.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:RGD.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
DR GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0033198; P:response to ATP; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0006986; P:response to unfolded protein; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Direct protein sequencing; Isomerase;
KW Isopeptide bond; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 27..573
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000005029"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 111..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 82
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 125
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 125
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 133
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 218
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 218
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 389
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 396
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 396
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 455
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 481
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 481
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT CONFLICT 121
FT /note="R -> P (in Ref. 2; AAC53362)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="S -> P (in Ref. 1; CAA38564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 60955 MW; 0014B58B77D0127B CRC64;
MLRLPTVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK
DIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV TKDDAMLLKG
KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLKPANED QKIGIEIIKR ALKIPAMTIA
KNAGVEGSLI VEKILQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT
TAEAVVTEIP KEEKDPGMGA MGGMGGGMGG GMF
