M2OM_HUMAN
ID M2OM_HUMAN Reviewed; 314 AA.
AC Q02978; F5GY65; O75537; Q969P7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein {ECO:0000303|PubMed:29431636};
DE Short=OGCP {ECO:0000303|PubMed:21448454};
DE Short=alpha-oxoglutarate carrier {ECO:0000303|PubMed:21448454};
DE AltName: Full=Solute carrier family 25 member 11;
DE Short=SLC25A11;
GN Name=SLC25A11; Synonyms=SLC20A4;
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].
RX PubMed=1457818; DOI=10.3109/10425179209034000;
RA Iacobazzi V., Palmieri F., Runswick M.J., Walker J.E.;
RT "Sequences of the human and bovine genes for the mitochondrial 2-
RT oxoglutarate carrier.";
RL DNA Seq. 3:79-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, 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 [5]
RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21448454; DOI=10.1371/journal.pone.0017827;
RA Gallo M., Park D., Luciani D.S., Kida K., Palmieri F., Blacque O.E.,
RA Johnson J.D., Riddle D.L.;
RT "MISC-1/OGC links mitochondrial metabolism, apoptosis and insulin
RT secretion.";
RL PLoS ONE 6:E17827-E17827(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [15]
RP INVOLVEMENT IN PGL6, VARIANTS PGL6 LYS-141; VAL-147 AND THR-239,
RP CHARACTERIZATION OF VARIANTS PGL6 LYS-141; VAL-147 AND THR-239, AND
RP FUNCTION.
RX PubMed=29431636; DOI=10.1158/0008-5472.can-17-2463;
RA Buffet A., Morin A., Castro-Vega L.J., Habarou F., Lussey-Lepoutre C.,
RA Letouze E., Lefebvre H., Guilhem I., Haissaguerre M., Raingeard I.,
RA Padilla-Girola M., Tran T., Tchara L., Bertherat J., Amar L.,
RA Ottolenghi C., Burnichon N., Gimenez-Roqueplo A.P., Favier J.;
RT "Germline Mutations in the Mitochondrial 2-Oxoglutarate/Malate Carrier
RT SLC25A11 Gene Confer a Predisposition to Metastatic Paragangliomas.";
RL Cancer Res. 78:1914-1922(2018).
CC -!- FUNCTION: Catalyzes the transport of 2-oxoglutarate (alpha-
CC oxoglutarate) across the inner mitochondrial membrane in an
CC electroneutral exchange for malate. Can also exchange 2-oxoglutarate
CC for other dicarboxylic acids such as malonate, succinate, maleate and
CC oxaloacetate, although with lower affinity. Contributes to several
CC metabolic processes, including the malate-aspartate shuttle, the
CC oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and
CC in nitrogen metabolism (By similarity). Maintains mitochondrial fusion
CC and fission events, and the organization and morphology of cristae
CC (PubMed:21448454). Involved in the regulation of apoptosis (By
CC similarity). Helps protect from cytotoxic-induced apoptosis by
CC modulating glutathione levels in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:P22292, ECO:0000250|UniProtKB:P97700,
CC ECO:0000250|UniProtKB:Q9CR62, ECO:0000269|PubMed:21448454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-
CC oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) +
CC malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) +
CC succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) +
CC maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30780; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) +
CC oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- INTERACTION:
CC Q02978; O43865: AHCYL1; NbExp=3; IntAct=EBI-359174, EBI-2371423;
CC Q02978; P27797: CALR; NbExp=3; IntAct=EBI-359174, EBI-1049597;
CC Q02978; P12830: CDH1; NbExp=3; IntAct=EBI-359174, EBI-727477;
CC Q02978; Q15078: CDK5R1; NbExp=3; IntAct=EBI-359174, EBI-746189;
CC Q02978; P36957: DLST; NbExp=3; IntAct=EBI-359174, EBI-351007;
CC Q02978; P42858: HTT; NbExp=6; IntAct=EBI-359174, EBI-466029;
CC Q02978; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-359174, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P97700}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97700}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02978-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02978-2; Sequence=VSP_046745;
CC -!- TISSUE SPECIFICITY: Most highly expressed in the heart.
CC {ECO:0000269|PubMed:21448454}.
CC -!- DISEASE: Paragangliomas 6 (PGL6) [MIM:618464]: An autosomal dominant
CC tumor predisposition syndrome characterized by adult-onset development
CC of paragangliomas, neural crest tumors usually derived from the
CC chromoreceptor tissue of a paraganglion. Paragangliomas can develop at
CC various body sites, including the head, neck, thorax and abdomen. Some
CC of the tumors may secrete biologically active normetanephrine,
CC resulting in secondary hypertension. PGL6 patients are at high risk for
CC metastatic disease. {ECO:0000269|PubMed:29431636}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X66114; CAA46905.1; -; Genomic_DNA.
DR EMBL; AF070548; AAC28637.1; -; mRNA.
DR EMBL; AC004771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006508; AAH06508.1; -; mRNA.
DR EMBL; BC006519; AAH06519.1; -; mRNA.
DR EMBL; BC016294; AAH16294.1; -; mRNA.
DR EMBL; BC017170; AAH17170.1; -; mRNA.
DR CCDS; CCDS11059.1; -. [Q02978-1]
DR CCDS; CCDS54069.1; -. [Q02978-2]
DR PIR; A56650; A56650.
DR RefSeq; NP_003553.2; NM_003562.4. [Q02978-1]
DR AlphaFoldDB; Q02978; -.
DR SMR; Q02978; -.
DR BioGRID; 113990; 202.
DR IntAct; Q02978; 84.
DR MINT; Q02978; -.
DR STRING; 9606.ENSP00000225665; -.
DR TCDB; 2.A.29.2.13; the mitochondrial carrier (mc) family.
DR CarbonylDB; Q02978; -.
DR GlyGen; Q02978; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02978; -.
DR MetOSite; Q02978; -.
DR PhosphoSitePlus; Q02978; -.
DR SwissPalm; Q02978; -.
DR BioMuta; SLC25A11; -.
DR DMDM; 20141580; -.
DR EPD; Q02978; -.
DR jPOST; Q02978; -.
DR MassIVE; Q02978; -.
DR MaxQB; Q02978; -.
DR PaxDb; Q02978; -.
DR PeptideAtlas; Q02978; -.
DR PRIDE; Q02978; -.
DR ProteomicsDB; 24639; -.
DR ProteomicsDB; 58148; -. [Q02978-1]
DR TopDownProteomics; Q02978-1; -. [Q02978-1]
DR Antibodypedia; 11377; 226 antibodies from 29 providers.
DR DNASU; 8402; -.
DR Ensembl; ENST00000225665.12; ENSP00000225665.7; ENSG00000108528.14. [Q02978-1]
DR Ensembl; ENST00000544061.6; ENSP00000440804.2; ENSG00000108528.14. [Q02978-2]
DR GeneID; 8402; -.
DR KEGG; hsa:8402; -.
DR MANE-Select; ENST00000225665.12; ENSP00000225665.7; NM_003562.5; NP_003553.2.
DR UCSC; uc021toe.2; human. [Q02978-1]
DR CTD; 8402; -.
DR DisGeNET; 8402; -.
DR GeneCards; SLC25A11; -.
DR HGNC; HGNC:10981; SLC25A11.
DR HPA; ENSG00000108528; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; SLC25A11; -.
DR MIM; 604165; gene.
DR MIM; 618464; phenotype.
DR neXtProt; NX_Q02978; -.
DR OpenTargets; ENSG00000108528; -.
DR Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
DR PharmGKB; PA35857; -.
DR VEuPathDB; HostDB:ENSG00000108528; -.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000158465; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q02978; -.
DR OMA; FLHTPFM; -.
DR OrthoDB; 892773at2759; -.
DR PhylomeDB; Q02978; -.
DR TreeFam; TF354262; -.
DR PathwayCommons; Q02978; -.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SignaLink; Q02978; -.
DR BioGRID-ORCS; 8402; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; SLC25A11; human.
DR GeneWiki; SLC25A11; -.
DR GenomeRNAi; 8402; -.
DR Pharos; Q02978; Tbio.
DR PRO; PR:Q02978; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q02978; protein.
DR Bgee; ENSG00000108528; Expressed in apex of heart and 204 other tissues.
DR ExpressionAtlas; Q02978; baseline and differential.
DR Genevisible; Q02978; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015367; F:oxoglutarate:malate antiporter activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Antiport; Direct protein sequencing;
KW Disease variant; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..314
FT /note="Mitochondrial 2-oxoglutarate/malate carrier protein"
FT /id="PRO_0000090625"
FT TRANSMEM 24..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 23..108
FT /note="Solcar 1"
FT REPEAT 117..208
FT /note="Solcar 2"
FT REPEAT 217..306
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR62"
FT VAR_SEQ 32..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046745"
FT VARIANT 141
FT /note="E -> K (in PGL6; loss of protein expression;
FT dbSNP:rs1567651815)"
FT /evidence="ECO:0000269|PubMed:29431636"
FT /id="VAR_082966"
FT VARIANT 147
FT /note="M -> V (in PGL6; loss of protein expression;
FT dbSNP:rs1203876038)"
FT /evidence="ECO:0000269|PubMed:29431636"
FT /id="VAR_082967"
FT VARIANT 239
FT /note="P -> T (in PGL6; loss of protein expression;
FT dbSNP:rs1567650859)"
FT /evidence="ECO:0000269|PubMed:29431636"
FT /id="VAR_082968"
FT CONFLICT 12
FT /note="I -> M (in Ref. 1; CAA46905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 34062 MW; 9D61F817089FF5AA CRC64;
MAATASAGAG GIDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVKNRMQ LSGEGAKTRE
YKTSFHALTS ILKAEGLRGI YTGLSAGLLR QATYTTTRLG IYTVLFERLT GADGTPPGFL
LKAVIGMTAG ATGAFVGTPA EVALIRMTAD GRLPADQRRG YKNVFNALIR ITREEGVLTL
WRGCIPTMAR AVVVNAAQLA SYSQSKQFLL DSGYFSDNIL CHFCASMISG LVTTAASMPV
DIAKTRIQNM RMIDGKPEYK NGLDVLFKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL
EQMNKAYKRL FLSG
