ATPG_HUMAN
ID ATPG_HUMAN Reviewed; 298 AA.
AC P36542; A8KA31; Q5VYP3; Q6I9V2; Q96AS8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit gamma {ECO:0000312|HGNC:HGNC:833};
DE AltName: Full=F-ATPase gamma subunit;
DE Flags: Precursor;
GN Name=ATP5F1C {ECO:0000312|HGNC:HGNC:833};
GN Synonyms=ATP5C {ECO:0000312|HGNC:HGNC:833},
GN ATP5C1 {ECO:0000312|HGNC:HGNC:833}, ATP5CL1 {ECO:0000312|HGNC:HGNC:833};
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 [GENOMIC DNA / MRNA] (ISOFORMS HEART AND LIVER).
RC TISSUE=Heart, and Liver;
RX PubMed=8227057; DOI=10.1016/s0021-9258(19)74556-6;
RA Matsuda C., Endo H., Ohta S., Kagawa Y.;
RT "Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue
RT specificity produced by alternative RNA splicing.";
RL J. Biol. Chem. 268:24950-24958(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HEART).
RC TISSUE=Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIVER).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LIVER).
RC TISSUE=Liver, Muscle, Placenta, and Urinary bladder;
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 [7]
RP PROTEIN SEQUENCE OF 68-79; 116-126; 144-154; 263-277 AND 286-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Frame M.C.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-154 AND LYS-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(1) domain and the central stalk which is part of the complex rotary
CC element. The gamma subunit protrudes into the catalytic domain formed
CC of alpha(3)beta(3). Rotation of the central stalk against the
CC surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC three separate catalytic sites on the beta subunits.
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). {ECO:0000250|UniProtKB:P05631}.
CC -!- INTERACTION:
CC P36542; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-711768, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P05631}; Matrix side
CC {ECO:0000250|UniProtKB:P05631}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Liver; Synonyms=L;
CC IsoId=P36542-1; Sequence=Displayed;
CC Name=Heart; Synonyms=H;
CC IsoId=P36542-2; Sequence=VSP_000439;
CC -!- TISSUE SPECIFICITY: Isoform Heart is expressed specifically in the
CC heart and skeletal muscle, which require rapid energy supply. Isoform
CC Liver is expressed in the brain, liver and kidney. Isoform Heart and
CC Isoform Liver are expressed in the skin, intestine, stomach and aorta.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; D16561; BAA03994.1; -; Genomic_DNA.
DR EMBL; D16561; BAA03995.1; -; Genomic_DNA.
DR EMBL; D16562; BAA03996.1; -; mRNA.
DR EMBL; D16563; BAA03997.1; -; mRNA.
DR EMBL; AK292896; BAF85585.1; -; mRNA.
DR EMBL; CR457403; CAG33684.1; -; mRNA.
DR EMBL; AL353754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86372.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86373.1; -; Genomic_DNA.
DR EMBL; BC000470; AAH00470.1; -; mRNA.
DR EMBL; BC000931; AAH00931.1; -; mRNA.
DR EMBL; BC013394; AAH13394.1; -; mRNA.
DR EMBL; BC016812; AAH16812.1; -; mRNA.
DR EMBL; BC020824; AAH20824.1; -; mRNA.
DR CCDS; CCDS31142.1; -. [P36542-1]
DR CCDS; CCDS7081.1; -. [P36542-2]
DR PIR; A49108; A49108.
DR RefSeq; NP_001001973.1; NM_001001973.2. [P36542-1]
DR RefSeq; NP_005165.1; NM_005174.3. [P36542-2]
DR AlphaFoldDB; P36542; -.
DR SMR; P36542; -.
DR BioGRID; 106997; 365.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P36542; -.
DR IntAct; P36542; 126.
DR MINT; P36542; -.
DR STRING; 9606.ENSP00000349142; -.
DR ChEMBL; CHEMBL4295752; -.
DR DrugBank; DB07384; 1-ACETYL-2-CARBOXYPIPERIDINE.
DR DrugBank; DB07394; AUROVERTIN B.
DR DrugBank; DB08629; N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINE.
DR DrugBank; DB08399; Piceatannol.
DR DrugBank; DB04216; Quercetin.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR GlyGen; P36542; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36542; -.
DR MetOSite; P36542; -.
DR PhosphoSitePlus; P36542; -.
DR SwissPalm; P36542; -.
DR BioMuta; ATP5C1; -.
DR DMDM; 543875; -.
DR UCD-2DPAGE; P36542; -.
DR EPD; P36542; -.
DR jPOST; P36542; -.
DR MassIVE; P36542; -.
DR MaxQB; P36542; -.
DR PaxDb; P36542; -.
DR PeptideAtlas; P36542; -.
DR PRIDE; P36542; -.
DR ProteomicsDB; 55207; -. [P36542-1]
DR ProteomicsDB; 55208; -. [P36542-2]
DR TopDownProteomics; P36542-1; -. [P36542-1]
DR TopDownProteomics; P36542-2; -. [P36542-2]
DR Antibodypedia; 54768; 281 antibodies from 30 providers.
DR DNASU; 509; -.
DR Ensembl; ENST00000335698.4; ENSP00000338568.4; ENSG00000165629.20. [P36542-2]
DR Ensembl; ENST00000356708.12; ENSP00000349142.7; ENSG00000165629.20. [P36542-1]
DR GeneID; 509; -.
DR KEGG; hsa:509; -.
DR MANE-Select; ENST00000356708.12; ENSP00000349142.7; NM_001001973.3; NP_001001973.1.
DR UCSC; uc001iju.4; human. [P36542-1]
DR CTD; 509; -.
DR DisGeNET; 509; -.
DR GeneCards; ATP5F1C; -.
DR HGNC; HGNC:833; ATP5F1C.
DR HPA; ENSG00000165629; Tissue enhanced (tongue).
DR MIM; 108729; gene.
DR neXtProt; NX_P36542; -.
DR OpenTargets; ENSG00000165629; -.
DR PharmGKB; PA25125; -.
DR VEuPathDB; HostDB:ENSG00000165629; -.
DR eggNOG; KOG1531; Eukaryota.
DR GeneTree; ENSGT00390000006837; -.
DR HOGENOM; CLU_050669_4_0_1; -.
DR InParanoid; P36542; -.
DR OMA; MQITSAM; -.
DR PhylomeDB; P36542; -.
DR TreeFam; TF105765; -.
DR BioCyc; MetaCyc:HS09257-MON; -.
DR PathwayCommons; P36542; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P36542; -.
DR SIGNOR; P36542; -.
DR BioGRID-ORCS; 509; 431 hits in 1084 CRISPR screens.
DR ChiTaRS; ATP5C1; human.
DR GeneWiki; ATP5C1; -.
DR GenomeRNAi; 509; -.
DR Pharos; P36542; Tbio.
DR PRO; PR:P36542; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P36542; protein.
DR Bgee; ENSG00000165629; Expressed in heart right ventricle and 213 other tissues.
DR Genevisible; P36542; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB.
DR GO; GO:0006119; P:oxidative phosphorylation; NAS:UniProtKB.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR PROSITE; PS00153; ATPASE_GAMMA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP synthesis; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT CHAIN 26..298
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000002685"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 49
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 154
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 270
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VR2"
FT VAR_SEQ 298
FT /note="Missing (in isoform Heart)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8227057"
FT /id="VSP_000439"
FT CONFLICT 45
FT /note="T -> A (in Ref. 6; AAH16812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32996 MW; 021A95168FD53E04 CRC64;
MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE
RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR GLCGAIHSSI AKQMKSEVAT
LTAAGKEVML VGIGDKIRGI LYRTHSDQFL VAFKEVGRKP PTFGDASVIA LELLNSGYEF
DEGSIIFNKF RSVISYKTEE KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY
SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
