ID   ACSF2_HUMAN             Reviewed;         615 AA.
AC   Q96CM8; B4DFQ6; B4DHT5; B4DUF5; Q9H7G2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000305};
DE            EC=6.2.1.2 {ECO:0000269|PubMed:17762044};
DE   Flags: Precursor;
GN   Name=ACSF2 {ECO:0000312|HGNC:HGNC:26101}; ORFNames=UNQ493/PRO1009;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Adipose tissue, Amygdala, and Caudate nucleus;
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 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 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-75.
RC   TISSUE=Kidney, and Skin;
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   FUNCTION, AND INDUCTION.
RX   PubMed=16380219; DOI=10.1016/j.gene.2005.10.021;
RA   Perera R.J., Marcusson E.G., Koo S., Kang X., Kim Y., White N., Dean N.M.;
RT   "Identification of novel PPARgamma target genes in primary human
RT   adipocytes.";
RL   Gene 369:90-99(2006).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17762044; DOI=10.1194/jlr.m700378-jlr200;
RA   Watkins P.A., Maiguel D., Jia Z., Pevsner J.;
RT   "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human
RT   genome.";
RL   J. Lipid Res. 48:2736-2750(2007).
RN   [8]
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   [9]
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: Acyl-CoA synthases catalyze the initial reaction in fatty
CC       acid metabolism, by forming a thioester with CoA (PubMed:17762044). Has
CC       some preference toward medium-chain substrates (PubMed:17762044). Plays
CC       a role in adipocyte differentiation (PubMed:16380219).
CC       {ECO:0000269|PubMed:16380219, ECO:0000269|PubMed:17762044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000269|PubMed:17762044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:17762044};
CC   -!- INTERACTION:
CC       Q96CM8; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-2876502, EBI-741181;
CC       Q96CM8; Q6Q788: APOA5; NbExp=3; IntAct=EBI-2876502, EBI-3936819;
CC       Q96CM8; P02654: APOC1; NbExp=3; IntAct=EBI-2876502, EBI-1220105;
CC       Q96CM8; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2876502, EBI-11343438;
CC       Q96CM8; Q15041: ARL6IP1; NbExp=8; IntAct=EBI-2876502, EBI-714543;
CC       Q96CM8; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-2876502, EBI-13381098;
CC       Q96CM8; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-2876502, EBI-2873246;
CC       Q96CM8; Q96DZ9: CMTM5; NbExp=5; IntAct=EBI-2876502, EBI-2548702;
CC       Q96CM8; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2876502, EBI-11522780;
CC       Q96CM8; O75208: COQ9; NbExp=4; IntAct=EBI-2876502, EBI-724524;
CC       Q96CM8; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-2876502, EBI-12831978;
CC       Q96CM8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2876502, EBI-13345167;
CC       Q96CM8; Q5XKP0: MICOS13; NbExp=3; IntAct=EBI-2876502, EBI-1053887;
CC       Q96CM8; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-2876502, EBI-11913715;
CC       Q96CM8; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-2876502, EBI-17589229;
CC       Q96CM8; Q9HC62: SENP2; NbExp=3; IntAct=EBI-2876502, EBI-714881;
CC       Q96CM8; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2876502, EBI-2623095;
CC       Q96CM8; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-2876502, EBI-17640454;
CC       Q96CM8; O43761: SYNGR3; NbExp=3; IntAct=EBI-2876502, EBI-11321949;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96CM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96CM8-2; Sequence=VSP_055804;
CC       Name=3;
CC         IsoId=Q96CM8-3; Sequence=VSP_055805;
CC       Name=4;
CC         IsoId=Q96CM8-4; Sequence=VSP_055803;
CC   -!- INDUCTION: By PPARG. {ECO:0000269|PubMed:16380219}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AY358660; AAQ89023.1; -; mRNA.
DR   EMBL; AK024573; BAB14930.1; -; mRNA.
DR   EMBL; AK294205; BAG57517.1; -; mRNA.
DR   EMBL; AK295258; BAG58247.1; -; mRNA.
DR   EMBL; AK300625; BAG62317.1; -; mRNA.
DR   EMBL; AC004707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC021491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471109; EAW94612.1; -; Genomic_DNA.
DR   EMBL; BC012053; AAH12053.1; -; mRNA.
DR   EMBL; BC014123; AAH14123.1; -; mRNA.
DR   CCDS; CCDS11567.1; -. [Q96CM8-1]
DR   CCDS; CCDS74103.1; -. [Q96CM8-2]
DR   CCDS; CCDS74104.1; -. [Q96CM8-3]
DR   RefSeq; NP_001275897.1; NM_001288968.1. [Q96CM8-2]
DR   RefSeq; NP_001275898.1; NM_001288969.1. [Q96CM8-3]
DR   RefSeq; NP_001275899.1; NM_001288970.1.
DR   RefSeq; NP_001275900.1; NM_001288971.1. [Q96CM8-4]
DR   RefSeq; NP_001275901.1; NM_001288972.1. [Q96CM8-4]
DR   RefSeq; NP_079425.3; NM_025149.5. [Q96CM8-1]
DR   AlphaFoldDB; Q96CM8; -.
DR   SMR; Q96CM8; -.
DR   BioGRID; 123187; 136.
DR   IntAct; Q96CM8; 34.
DR   MINT; Q96CM8; -.
DR   STRING; 9606.ENSP00000401831; -.
DR   SwissLipids; SLP:000001145; -.
DR   GlyCosmos; Q96CM8; 1 site, 1 glycan.
DR   GlyGen; Q96CM8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96CM8; -.
DR   PhosphoSitePlus; Q96CM8; -.
DR   SwissPalm; Q96CM8; -.
DR   BioMuta; ACSF2; -.
DR   DMDM; 166198367; -.
DR   CPTAC; CPTAC-5; -.
DR   CPTAC; CPTAC-6; -.
DR   EPD; Q96CM8; -.
DR   jPOST; Q96CM8; -.
DR   MassIVE; Q96CM8; -.
DR   MaxQB; Q96CM8; -.
DR   PaxDb; 9606-ENSP00000401831; -.
DR   PeptideAtlas; Q96CM8; -.
DR   ProteomicsDB; 4067; -.
DR   ProteomicsDB; 4247; -.
DR   ProteomicsDB; 5184; -.
DR   ProteomicsDB; 76194; -. [Q96CM8-1]
DR   Pumba; Q96CM8; -.
DR   TopDownProteomics; Q96CM8-1; -. [Q96CM8-1]
DR   Antibodypedia; 30532; 154 antibodies from 24 providers.
DR   DNASU; 80221; -.
DR   Ensembl; ENST00000300441.9; ENSP00000300441.4; ENSG00000167107.13. [Q96CM8-1]
DR   Ensembl; ENST00000427954.6; ENSP00000401831.2; ENSG00000167107.13. [Q96CM8-2]
DR   Ensembl; ENST00000502667.5; ENSP00000421884.1; ENSG00000167107.13. [Q96CM8-3]
DR   GeneID; 80221; -.
DR   KEGG; hsa:80221; -.
DR   MANE-Select; ENST00000300441.9; ENSP00000300441.4; NM_025149.6; NP_079425.3.
DR   UCSC; uc002iqu.4; human. [Q96CM8-1]
DR   AGR; HGNC:26101; -.
DR   CTD; 80221; -.
DR   DisGeNET; 80221; -.
DR   GeneCards; ACSF2; -.
DR   HGNC; HGNC:26101; ACSF2.
DR   HPA; ENSG00000167107; Tissue enhanced (kidney).
DR   MIM; 610465; gene.
DR   neXtProt; NX_Q96CM8; -.
DR   OpenTargets; ENSG00000167107; -.
DR   PharmGKB; PA162375338; -.
DR   VEuPathDB; HostDB:ENSG00000167107; -.
DR   eggNOG; KOG1177; Eukaryota.
DR   GeneTree; ENSGT00940000156830; -.
DR   HOGENOM; CLU_000022_59_7_1; -.
DR   InParanoid; Q96CM8; -.
DR   OMA; KQSDMKA; -.
DR   OrthoDB; 2596785at2759; -.
DR   PhylomeDB; Q96CM8; -.
DR   TreeFam; TF313466; -.
DR   PathwayCommons; Q96CM8; -.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q96CM8; -.
DR   BioGRID-ORCS; 80221; 19 hits in 1161 CRISPR screens.
DR   ChiTaRS; ACSF2; human.
DR   GenomeRNAi; 80221; -.
DR   Pharos; Q96CM8; Tbio.
DR   PRO; PR:Q96CM8; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96CM8; Protein.
DR   Bgee; ENSG00000167107; Expressed in right lobe of thyroid gland and 155 other cell types or tissues.
DR   ExpressionAtlas; Q96CM8; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; TAS:Reactome.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; TAS:Reactome.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd05917; FACL_like_2; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; Q96CM8; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Fatty acid metabolism;
KW   Ligase; Lipid metabolism; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..615
FT                   /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT                   /id="PRO_0000315793"
FT   BINDING         263..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         599
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         182
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         182
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         340
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         398
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         478
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         510
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         544
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         544
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         570
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         570
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   MOD_RES         599
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT   VAR_SEQ         1..160
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055803"
FT   VAR_SEQ         43
FT                   /note="S -> SARGGMEAGRQRISVPSSFTASAAAH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055804"
FT   VAR_SEQ         146..158
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055805"
FT   VARIANT         75
FT                   /note="G -> V (in dbSNP:rs17856448)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038304"
FT   VARIANT         316
FT                   /note="V -> M (in dbSNP:rs3744523)"
FT                   /id="VAR_038305"
SQ   SEQUENCE   615 AA;  68125 MW;  A3356EEA7C14730B CRC64;
     MAVYVGMLRL GRLCAGSSGV LGARAALSRS WQEARLQGVR FLSSREVDRM VSTPIGGLSY
     VQGCTKKHLN SKTVGQCLET TAQRVPEREA LVVLHEDVRL TFAQLKEEVD KAASGLLSIG
     LCKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYVLKKV GCKALVFPKQ
     FKTQQYYNVL KQICPEVENA QPGALKSQRL PDLTTVISVD APLPGTLLLD EVVAAGSTRQ
     HLDQLQYNQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNSNILGER LKLHEKTPEQ
     LRMILPNPLY HCLGSVAGTM MCLMYGATLI LASPIFNGKK ALEAISRERG TFLYGTPTMF
     VDILNQPDFS SYDISTMCGG VIAGSPAPPE LIRAIINKIN MKDLVVAYGT TENSPVTFAH
     FPEDTVEQKA ESVGRIMPHT EARIMNMEAG TLAKLNTPGE LCIRGYCVML GYWGEPQKTE
     EAVDQDKWYW TGDVATMNEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPKVQEVQV
     VGVKDDRMGE EICACIRLKD GEETTVEEIK AFCKGKISHF KIPKYIVFVT NYPLTISGKI
     QKFKLREQME RHLNL
//