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Database: UniProt
Entry: P07108
LinkDB: P07108
Original site: P07108 
ID   ACBP_HUMAN              Reviewed;          87 AA.
AC   P07108; B8ZWD2; B8ZWD6; B8ZWD7; P08869; Q4VWZ6; Q53SQ7; Q6IB48;
AC   Q9UCI8;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-OCT-2014, entry version 153.
DE   RecName: Full=Acyl-CoA-binding protein;
DE            Short=ACBP;
DE   AltName: Full=Diazepam-binding inhibitor;
DE            Short=DBI;
DE   AltName: Full=Endozepine;
DE            Short=EP;
GN   Name=DBI;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=3020548; DOI=10.1073/pnas.83.19.7547;
RA   Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E.;
RT   "Cloning and expression of cDNA for human diazepam binding inhibitor,
RT   a natural ligand of an allosteric regulatory site of the gamma-
RT   aminobutyric acid type A receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2881742; DOI=10.1089/dna.1987.6.71;
RA   Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J.,
RA   Lee D.C.;
RT   "Bovine and human cDNA sequences encoding a putative benzodiazepine
RT   receptor ligand.";
RL   DNA 6:71-79(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX   PubMed=16055366; DOI=10.1016/j.biocel.2005.06.008;
RA   Nitz I., Doering F., Schrezenmeir J., Burwinkel B.;
RT   "Identification of new acyl-CoA binding protein transcripts in human
RT   and mouse.";
RL   Int. J. Biochem. Cell Biol. 37:2395-2405(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=21698759; DOI=10.1002/iub.471;
RA   Ludewig A.H., Nitz I., Klapper M., Doring F.;
RT   "Identification of a novel human Acyl-CoA binding protein isoform with
RT   a unique C-terminal domain.";
RL   IUBMB Life 63:547-552(2011).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE
RP   SPLICING, AND ALTERNATIVE PROMOTER USAGE.
RX   PubMed=20345851; DOI=10.1111/j.1582-4934.2010.01055.x;
RA   Nitz I., Kruse M.L., Klapper M., Doring F.;
RT   "Specific regulation of low-abundance transcript variants encoding
RT   human Acyl-CoA binding protein (ACBP) isoforms.";
RL   J. Cell. Mol. Med. 15:909-927(2011).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), AND ACETYLATION AT SER-2.
RC   TISSUE=Brain;
RX   PubMed=3525533;
RA   Marquardt H., Todaro G.J., Shoyab M.;
RT   "Complete amino acid sequences of bovine and human endozepines.
RT   Homology with rat diazepam binding inhibitor.";
RL   J. Biol. Chem. 261:9727-9731(1986).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-14 (ISOFORM 1).
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [12]
RP   PROTEIN SEQUENCE OF 26-30 AND 72-87.
RX   PubMed=1292782;
RA   Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U.;
RT   "Purification and analysis of growth regulating proteins secreted by a
RT   human melanoma cell line.";
RL   Melanoma Res. 2:327-336(1992).
RN   [13]
RP   ALTERNATIVE SPLICING.
RX   PubMed=7534063;
RA   Kolmer M., Rovio A., Alho H.;
RT   "The characterization of two diazepam binding inhibitor (DBI)
RT   transcripts in humans.";
RL   Biochem. J. 306:327-330(1995).
RN   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17953517; DOI=10.1042/BJ20070559;
RA   Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.;
RT   "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic
RT   reticulum and Golgi in a ligand-dependent manner in mammalian cells.";
RL   Biochem. J. 410:463-472(2008).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8; LYS-19; LYS-55 AND
RP   LYS-77, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
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.,
RA   Buerckstuemmer T., 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   [19]
RP   MALONYLATION AT LYS-55.
RX   PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA   Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA   He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA   Dai J., Verdin E., Ye Y., Zhao Y.;
RT   "The first identification of lysine malonylation substrates and its
RT   regulatory enzyme.";
RL   Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A.
RX   PubMed=17044054; DOI=10.1002/prot.21124;
RA   Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K.;
RT   "High resolution crystal structures of unliganded and liganded human
RT   liver ACBP reveal a new mode of binding for the acyl-CoA ligand.";
RL   Proteins 66:229-238(2007).
CC   -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very
CC       high affinity and may function as an intracellular carrier of
CC       acyl-CoA esters. It is also able to displace diazepam from the
CC       benzodiazepine (BZD) recognition site located on the GABA type A
CC       receptor. It is therefore possible that this protein also acts as
CC       a neuropeptide to modulate the action of the GABA receptor.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17044054}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus.
CC       Note=Golgi localization is dependent on ligand binding.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=ACBP-1a, Short;
CC         IsoId=P07108-1; Sequence=Displayed;
CC       Name=2; Synonyms=ACBP-1b, Long;
CC         IsoId=P07108-2; Sequence=VSP_000068;
CC       Name=3; Synonyms=ACBP-1c;
CC         IsoId=P07108-3; Sequence=VSP_038680;
CC       Name=4; Synonyms=ACBP-1a1-g;
CC         IsoId=P07108-4; Sequence=VSP_043437;
CC       Name=5; Synonyms=ACBP-1g;
CC         IsoId=P07108-5; Sequence=VSP_043438;
CC       Name=6; Synonyms=ACBP-1e;
CC         IsoId=P07108-6; Sequence=VSP_044114;
CC         Note=Predominantly expressed in adipose tissue and hippocampus.;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitous, with a moderate
CC       expression level. Isoform 2 is ubiquitous with high level in liver
CC       and adipose tissue. Isoform 3 is ubiquitous with strong expression
CC       in adipose tissue and heart. {ECO:0000269|PubMed:16055366,
CC       ECO:0000269|PubMed:21698759}.
CC   -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00573}.
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DR   EMBL; M14200; AAA52171.1; -; mRNA.
DR   EMBL; M15887; AAA35788.1; -; mRNA.
DR   EMBL; FM213123; CAR82405.1; -; mRNA.
DR   EMBL; FM213124; CAR82406.1; -; mRNA.
DR   EMBL; FM213125; CAR82407.1; -; mRNA.
DR   EMBL; FM213126; CAR82408.1; -; mRNA.
DR   EMBL; FM213127; CAR82409.1; -; mRNA.
DR   EMBL; FM213128; CAR82410.1; -; mRNA.
DR   EMBL; FM213131; CAR82414.1; -; mRNA.
DR   EMBL; CR456956; CAG33237.1; -; mRNA.
DR   EMBL; AC016736; AAY14873.1; -; Genomic_DNA.
DR   EMBL; CH471103; EAW95214.1; -; Genomic_DNA.
DR   EMBL; BC006466; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC062996; AAH62996.1; -; mRNA.
DR   EMBL; AM000001; CAJ00736.1; -; mRNA.
DR   CCDS; CCDS2126.1; -. [P07108-2]
DR   CCDS; CCDS42740.1; -. [P07108-1]
DR   CCDS; CCDS42741.1; -. [P07108-3]
DR   CCDS; CCDS54390.1; -. [P07108-4]
DR   CCDS; CCDS54391.1; -. [P07108-5]
DR   PIR; B26448; NZHU.
DR   RefSeq; NP_001073331.1; NM_001079862.2. [P07108-1]
DR   RefSeq; NP_001073332.1; NM_001079863.1. [P07108-3]
DR   RefSeq; NP_001171488.1; NM_001178017.1. [P07108-5]
DR   RefSeq; NP_001171512.1; NM_001178041.2. [P07108-4]
DR   RefSeq; NP_001171513.1; NM_001178042.2. [P07108-2]
DR   RefSeq; NP_001269562.1; NM_001282633.1. [P07108-2]
DR   RefSeq; NP_001269563.1; NM_001282634.1. [P07108-2]
DR   RefSeq; NP_001269564.1; NM_001282635.1. [P07108-2]
DR   RefSeq; NP_065438.1; NM_020548.7. [P07108-2]
DR   UniGene; Hs.78888; -.
DR   PDB; 2CB8; X-ray; 1.40 A; A/B=2-87.
DR   PDB; 2FJ9; X-ray; 1.60 A; A=2-87.
DR   PDBsum; 2CB8; -.
DR   PDBsum; 2FJ9; -.
DR   ProteinModelPortal; P07108; -.
DR   SMR; P07108; 2-87.
DR   BioGrid; 107990; 10.
DR   IntAct; P07108; 9.
DR   MINT; MINT-1394907; -.
DR   STRING; 9606.ENSP00000311117; -.
DR   PhosphoSite; P07108; -.
DR   MaxQB; P07108; -.
DR   PaxDb; P07108; -.
DR   PRIDE; P07108; -.
DR   DNASU; 1622; -.
DR   Ensembl; ENST00000311521; ENSP00000311117; ENSG00000155368. [P07108-2]
DR   Ensembl; ENST00000355857; ENSP00000348116; ENSG00000155368. [P07108-1]
DR   Ensembl; ENST00000393103; ENSP00000376815; ENSG00000155368. [P07108-3]
DR   Ensembl; ENST00000409094; ENSP00000386486; ENSG00000155368. [P07108-2]
DR   Ensembl; ENST00000535617; ENSP00000442917; ENSG00000155368. [P07108-4]
DR   Ensembl; ENST00000535757; ENSP00000439012; ENSG00000155368. [P07108-2]
DR   Ensembl; ENST00000542275; ENSP00000440698; ENSG00000155368. [P07108-5]
DR   GeneID; 1622; -.
DR   KEGG; hsa:1622; -.
DR   UCSC; uc002tlv.3; human. [P07108-1]
DR   UCSC; uc002tlw.3; human. [P07108-2]
DR   UCSC; uc002tlx.3; human. [P07108-3]
DR   UCSC; uc010yyk.2; human. [P07108-4]
DR   UCSC; uc021vnj.1; human. [P07108-5]
DR   CTD; 1622; -.
DR   GeneCards; GC02P120124; -.
DR   HGNC; HGNC:2690; DBI.
DR   HPA; CAB008595; -.
DR   MIM; 125950; gene.
DR   neXtProt; NX_P07108; -.
DR   PharmGKB; PA27158; -.
DR   eggNOG; COG4281; -.
DR   HOVERGEN; HBG000398; -.
DR   KO; K08762; -.
DR   OMA; LTKRPSD; -.
DR   OrthoDB; EOG7SN8G8; -.
DR   PhylomeDB; P07108; -.
DR   TreeFam; TF335802; -.
DR   ChiTaRS; DBI; human.
DR   EvolutionaryTrace; P07108; -.
DR   GeneWiki; Diazepam_binding_inhibitor; -.
DR   GenomeRNAi; 1622; -.
DR   NextBio; 6658; -.
DR   PRO; PR:P07108; -.
DR   ArrayExpress; P07108; -.
DR   Bgee; P07108; -.
DR   CleanEx; HS_DBI; -.
DR   Genevestigator; P07108; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProt.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProt.
DR   GO; GO:0030156; F:benzodiazepine receptor binding; TAS:ProtInc.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProt.
DR   GO; GO:0046983; F:protein dimerization activity; IDA:UniProt.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProt.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   Pfam; PF00887; ACBP; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; SSF47027; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative promoter usage;
KW   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Endoplasmic reticulum; Golgi apparatus; Lipid-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:19608861,
FT                                ECO:0000269|PubMed:22814378,
FT                                ECO:0000269|PubMed:3525533}.
FT   CHAIN         2     87       Acyl-CoA-binding protein.
FT                                /FTId=PRO_0000214004.
FT   DOMAIN        2     87       ACB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00573}.
FT   REGION       29     33       Acyl-CoA binding.
FT   BINDING      14     14       Acyl-CoA.
FT   BINDING      55     55       Acyl-CoA.
FT   BINDING      74     74       Acyl-CoA.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:19608861,
FT                                ECO:0000269|PubMed:22814378,
FT                                ECO:0000269|PubMed:3525533}.
FT   MOD_RES       8      8       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES       8      8       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      17     17       N6-succinyllysine. {ECO:0000250}.
FT   MOD_RES      19     19       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      29     29       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:20068231}.
FT   MOD_RES      55     55       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      55     55       N6-malonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21908771}.
FT   MOD_RES      55     55       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      77     77       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      77     77       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   VAR_SEQ       1      3       MSQ -> MWGDLWLLPPASANPGTGTE (in isoform
FT                                2). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:20345851,
FT                                ECO:0000303|PubMed:3020548}.
FT                                /FTId=VSP_000068.
FT   VAR_SEQ       1      3       MSQ -> MPAF (in isoform 3).
FT                                {ECO:0000303|PubMed:16055366}.
FT                                /FTId=VSP_038680.
FT   VAR_SEQ       1      3       MSQ -> MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSE
FT                                CGTRRIAARGE (in isoform 4).
FT                                {ECO:0000303|PubMed:20345851}.
FT                                /FTId=VSP_043437.
FT   VAR_SEQ       1      3       MSQ -> MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKR
FT                                GVRGRELGGQGKYGAGCSECGTRRIAARGE (in
FT                                isoform 5).
FT                                {ECO:0000303|PubMed:20345851}.
FT                                /FTId=VSP_043438.
FT   VAR_SEQ      43     87       ERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKK
FT                                KYGI -> GMQSGGWKGICSSKQAQQLRLEVPGNFTLKLPE
FT                                ALLFRWGMVMVPEVEKTMFRILSVSSSNRIQILVLEGLYWP
FT                                SPAATLY (in isoform 6).
FT                                {ECO:0000303|PubMed:21698759}.
FT                                /FTId=VSP_044114.
FT   VARIANT      39     39       D -> N (in dbSNP:rs8192504).
FT                                /FTId=VAR_048160.
FT   VARIANT      71     71       M -> V (in dbSNP:rs8192506).
FT                                /FTId=VAR_048161.
FT   VARIANT      86     86       G -> R (in dbSNP:rs8192507).
FT                                /FTId=VAR_048162.
FT   HELIX         3     12
FT   HELIX        13     15
FT   HELIX        22     36
FT   HELIX        50     60
FT   TURN         61     64
FT   HELIX        67     85
SQ   SEQUENCE   87 AA;  10044 MW;  B343A309F1B1AE28 CRC64;
     MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN
     ELKGTSKEDA MKAYINKVEE LKKKYGI
//
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