ID GCP60_HUMAN Reviewed; 528 AA.
AC Q9H3P7; B2RB29; Q5VTJ0; Q6P9F1; Q8IZC5; Q8N4D6; Q9H6U3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 01-MAY-2013, entry version 105.
DE RecName: Full=Golgi resident protein GCP60;
DE AltName: Full=Acyl-CoA-binding domain-containing protein 3;
DE AltName: Full=Golgi complex-associated protein 1;
DE Short=GOCAP1;
DE AltName: Full=Golgi phosphoprotein 1;
DE Short=GOLPH1;
DE AltName: Full=PBR- and PKA-associated protein 7;
DE AltName: Full=Peripheral benzodiazepine receptor-associated protein PAP7;
GN Name=ACBD3; Synonyms=GCP60, GOCAP1, GOLPH1;
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], FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH GOLGB1, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11590181; DOI=10.1074/jbc.M108961200;
RA Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y.;
RT "Identification and characterization of a novel Golgi protein, GCP60,
RT that interacts with the integral membrane protein giantin.";
RL J. Biol. Chem. 276:45298-45306(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-187.
RC TISSUE=Placenta;
RA Liu J., Tobin D., Tasken K., Papadopoulos V.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-187.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ovary;
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 [7]
RP PROTEIN SEQUENCE OF 2-9.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-20, 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 [11]
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).
CC -!- FUNCTION: Involved in the maintenance of Golgi structure by
CC interacting with giantin, affecting protein transport between the
CC endoplasmic reticulum and Golgi. Involved in hormone-induced
CC steroid biosynthesis in testicular Leydig cells (By similarity).
CC -!- SUBUNIT: Interacts with the C-terminal cytoplasmic domain of
CC giantin/GOLGB1. Interacts with PBR and PKA regulatory subunit RI-
CC alpha. Does not interact with PKA regulatory subunit RI-beta nor
CC PKA regulatory subunit RII-alpha (By similarity).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Mitochondrion
CC (By similarity). Note=Also mitochondrial (via its interaction with
CC PBR) (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis
CC and ovary.
CC -!- DOMAIN: The GOLD domain is essential for giantin binding.
CC -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC -!- SIMILARITY: Contains 1 GOLD domain.
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DR EMBL; AB043587; BAB20592.2; -; mRNA.
DR EMBL; AY150218; AAN60219.1; -; mRNA.
DR EMBL; AK025520; BAB15159.1; -; mRNA.
DR EMBL; AK314468; BAG37076.1; -; mRNA.
DR EMBL; AL592045; CAH71922.1; -; Genomic_DNA.
DR EMBL; CH471098; EAW69775.1; -; Genomic_DNA.
DR EMBL; BC034563; AAH34563.2; -; mRNA.
DR EMBL; BC045533; AAH45533.1; -; mRNA.
DR EMBL; BC060792; AAH60792.1; -; mRNA.
DR IPI; IPI00009315; -.
DR RefSeq; NP_073572.2; NM_022735.3.
DR UniGene; Hs.520207; -.
DR ProteinModelPortal; Q9H3P7; -.
DR DIP; DIP-40673N; -.
DR IntAct; Q9H3P7; 4.
DR MINT; MINT-5003562; -.
DR STRING; 9606.ENSP00000355777; -.
DR PhosphoSite; Q9H3P7; -.
DR DMDM; 51316096; -.
DR PaxDb; Q9H3P7; -.
DR PeptideAtlas; Q9H3P7; -.
DR PRIDE; Q9H3P7; -.
DR Ensembl; ENST00000366812; ENSP00000355777; ENSG00000182827.
DR GeneID; 64746; -.
DR KEGG; hsa:64746; -.
DR UCSC; uc001hpy.3; human.
DR CTD; 64746; -.
DR GeneCards; GC01M226332; -.
DR H-InvDB; HIX0159664; -.
DR HGNC; HGNC:15453; ACBD3.
DR HPA; HPA015594; -.
DR MIM; 606809; gene.
DR neXtProt; NX_Q9H3P7; -.
DR PharmGKB; PA28803; -.
DR eggNOG; NOG287879; -.
DR HOVERGEN; HBG051712; -.
DR InParanoid; Q9H3P7; -.
DR OMA; FGVFFEW; -.
DR OrthoDB; EOG4WH8M8; -.
DR BindingDB; Q9H3P7; -.
DR ChiTaRS; ACBD3; human.
DR GenomeRNAi; 64746; -.
DR NextBio; 66697; -.
DR Bgee; Q9H3P7; -.
DR CleanEx; HS_ACBD3; -.
DR Genevestigator; Q9H3P7; -.
DR GermOnline; ENSG00000182827; Homo sapiens.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:InterPro.
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 InterPro; IPR009038; GOLD.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR SUPFAM; SSF47027; ACBP; 1.
DR SUPFAM; SSF101576; GOLD; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Direct protein sequencing;
KW Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome;
KW Steroid biosynthesis.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 528 Golgi resident protein GCP60.
FT /FTId=PRO_0000214029.
FT DOMAIN 83 174 ACB.
FT DOMAIN 384 526 GOLD.
FT COILED 174 257 Potential.
FT COMPBIAS 21 60 Pro-rich.
FT COMPBIAS 182 240 Glu-rich.
FT COMPBIAS 196 238 Arg-rich.
FT COMPBIAS 241 308 Gln-rich.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 20 20 Phosphoserine.
FT MOD_RES 43 43 Phosphoserine.
FT VARIANT 187 187 E -> D (in dbSNP:rs2306120).
FT /FTId=VAR_019615.
FT CONFLICT 93 93 F -> L (in Ref. 2; AAN60219).
FT CONFLICT 230 230 R -> I (in Ref. 2; AAN60219).
FT CONFLICT 265 265 Q -> R (in Ref. 2; AAN60219).
FT CONFLICT 333 333 S -> P (in Ref. 2; AAN60219).
FT CONFLICT 384 397 KEKIQQDADSVITV -> QREDSAGCRFRDYS (in Ref.
FT 2).
FT CONFLICT 425 425 Y -> C (in Ref. 2; AAN60219).
FT CONFLICT 473 473 K -> R (in Ref. 6; AAH60792).
SQ SEQUENCE 528 AA; 60593 MW; B36EC550F8268FC2 CRC64;
MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG PGASGEQPEP
GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK AFHPTYEEKL KLVALHKQVL
MGPYNPDTCP EVGFFDVLGN DRRREWAALG NMSKEDAMVE FVKLLNRCCH LFSTYVASHK
IEKEEQEKKR KEEEERRRRE EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE
QQKQQIMAAL NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ
QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE PEAAEEALEN
GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG EVVTVRVPTH EEGSYLFWEF
ATDNYDIGFG VYFEWTDSPN TAVSVHVSES SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV
PVYRRDCHEE VYAGSHQYPG RGVYLLKFDN SYSLWRSKSV YYRVYYTR
//
