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 29-MAY-2013, entry version 141.
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;
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; LYS-8; LYS-19; LYS-55 AND
RP LYS-77, AND MASS SPECTROMETRY.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASS
RP SPECTROMETRY.
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 [17]
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 [18]
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 [19]
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.
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.
CC -!- SIMILARITY: Belongs to the ACBP family.
CC -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
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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 IPI; IPI00010182; -.
DR IPI; IPI00218836; -.
DR IPI; IPI00921830; -.
DR IPI; IPI00922055; -.
DR IPI; IPI00965476; -.
DR PIR; B26448; NZHU.
DR RefSeq; NP_001073331.1; NM_001079862.1.
DR RefSeq; NP_001073332.1; NM_001079863.1.
DR RefSeq; NP_001171488.1; NM_001178017.1.
DR RefSeq; NP_001171512.1; NM_001178041.1.
DR RefSeq; NP_001171513.1; NM_001178042.1.
DR RefSeq; NP_001171514.1; NM_001178043.1.
DR RefSeq; NP_065438.1; NM_020548.6.
DR UniGene; Hs.78888; -.
DR PDB; 2CB8; X-ray; 1.40 A; A/B=1-87.
DR PDB; 2FJ9; X-ray; 1.60 A; A=2-87.
DR PDBsum; 2CB8; -.
DR PDBsum; 2FJ9; -.
DR ProteinModelPortal; P07108; -.
DR IntAct; P07108; 1.
DR MINT; MINT-1394907; -.
DR STRING; 9606.ENSP00000311117; -.
DR PhosphoSite; P07108; -.
DR DMDM; 118276; -.
DR PaxDb; P07108; -.
DR PRIDE; P07108; -.
DR DNASU; 1622; -.
DR Ensembl; ENST00000311521; ENSP00000311117; ENSG00000155368.
DR Ensembl; ENST00000355857; ENSP00000348116; ENSG00000155368.
DR Ensembl; ENST00000393103; ENSP00000376815; ENSG00000155368.
DR Ensembl; ENST00000409094; ENSP00000386486; ENSG00000155368.
DR Ensembl; ENST00000535617; ENSP00000442917; ENSG00000155368.
DR Ensembl; ENST00000535757; ENSP00000439012; ENSG00000155368.
DR Ensembl; ENST00000542275; ENSP00000440698; ENSG00000155368.
DR GeneID; 1622; -.
DR KEGG; hsa:1622; -.
DR UCSC; uc002tlv.3; human.
DR UCSC; uc002tlw.3; human.
DR UCSC; uc002tlx.3; human.
DR UCSC; uc010yyk.2; human.
DR UCSC; uc021vnj.1; human.
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; GDNTTDK; -.
DR OrthoDB; EOG4GF3GS; -.
DR ChiTaRS; DBI; human.
DR EvolutionaryTrace; P07108; -.
DR GenomeRNAi; 1622; -.
DR NextBio; 6658; -.
DR ArrayExpress; P07108; -.
DR Bgee; P07108; -.
DR CleanEx; HS_DBI; -.
DR Genevestigator; P07108; -.
DR GermOnline; ENSG00000155368; Homo sapiens.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR GO; GO:0030156; F:benzodiazepine receptor binding; TAS:ProtInc.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0001942; P:hair follicle development; IEA:Compara.
DR GO; GO:0043588; P:skin development; IEA:Compara.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Compara.
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; ACBP; 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.
FT CHAIN 2 87 Acyl-CoA-binding protein.
FT /FTId=PRO_0000214004.
FT DOMAIN 2 87 ACB.
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 MOD_RES 8 8 N6-acetyllysine.
FT MOD_RES 19 19 N6-acetyllysine.
FT MOD_RES 29 29 Phosphotyrosine.
FT MOD_RES 55 55 N6-acetyllysine; alternate.
FT MOD_RES 55 55 N6-malonyllysine; alternate.
FT MOD_RES 77 77 N6-acetyllysine.
FT VAR_SEQ 1 3 MSQ -> MWGDLWLLPPASANPGTGTE (in isoform
FT 2).
FT /FTId=VSP_000068.
FT VAR_SEQ 1 3 MSQ -> MPAF (in isoform 3).
FT /FTId=VSP_038680.
FT VAR_SEQ 1 3 MSQ -> MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSE
FT CGTRRIAARGE (in isoform 4).
FT /FTId=VSP_043437.
FT VAR_SEQ 1 3 MSQ -> MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKR
FT GVRGRELGGQGKYGAGCSECGTRRIAARGE (in
FT isoform 5).
FT /FTId=VSP_043438.
FT VAR_SEQ 43 87 ERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKK
FT KYGI -> GMQSGGWKGICSSKQAQQLRLEVPGNFTLKLPE
FT ALLFRWGMVMVPEVEKTMFRILSVSSSNRIQILVLEGLYWP
FT SPAATLY (in isoform 6).
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
//
