GenomeNet

Database: UniProt
Entry: Q7TNY6
LinkDB: Q7TNY6
Original site: Q7TNY6 
ID   GCP60_RAT               Reviewed;         526 AA.
AC   Q7TNY6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-JUN-2016, entry version 93.
DE   RecName: Full=Golgi resident protein GCP60;
DE   AltName: Full=Acyl-CoA-binding domain-containing protein 3;
DE   AltName: Full=DMT1-associated protein;
DE            Short=DAP;
DE   AltName: Full=Golgi complex-associated protein 1;
DE            Short=GOCAP1;
DE   AltName: Full=Golgi phosphoprotein 1;
DE            Short=GOLPH1;
DE   Contains:
DE     RecName: Full=Golgi resident protein GCP60, N-terminally processed;
GN   Name=Acbd3; Synonyms=Gcp60;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Brown Norway;
RA   Chen Y., Rodriguez-Paris J.M., Ma Y., Yeh M., Yeh K.-Y., Glass J.;
RT   "Intestinal iron absorption: the interaction of DMT1 with DAP, an iron
RT   responsive protein.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the C-terminal cytoplasmic domain of
CC       giantin/GOLGB1 (By similarity). Interacts with PBR and PKA
CC       regulatory subunit RI-alpha. Does not interact with PKA regulatory
CC       subunit RI-beta nor PKA regulatory subunit RII-alpha (By
CC       similarity). Interacts with PI4KB, TBC1D22A AND TBC1D22B;
CC       interactions with PI4KB and with TBC1D22A and TBC1D22B are
CC       mutually exclusive. Interacts with C10ORF76 and RAB11B (By
CC       similarity). {ECO:0000250|UniProtKB:Q8BMP6,
CC       ECO:0000250|UniProtKB:Q9H3P7}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also
CC       mitochondrial (via its interaction with PBR). {ECO:0000250}.
CC   -!- DOMAIN: The GOLD domain is essential for giantin binding.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00573}.
CC   -!- SIMILARITY: Contains 1 GOLD domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00096}.
DR   EMBL; AY336075; AAP94639.1; -; mRNA.
DR   RefSeq; NP_878263.1; NM_182843.1.
DR   UniGene; Rn.57036; -.
DR   ProteinModelPortal; Q7TNY6; -.
DR   MINT; MINT-4576509; -.
DR   STRING; 10116.ENSRNOP00000004293; -.
DR   iPTMnet; Q7TNY6; -.
DR   PhosphoSite; Q7TNY6; -.
DR   PaxDb; Q7TNY6; -.
DR   PRIDE; Q7TNY6; -.
DR   GeneID; 289312; -.
DR   KEGG; rno:289312; -.
DR   UCSC; RGD:727851; rat.
DR   CTD; 64746; -.
DR   RGD; 727851; Acbd3.
DR   eggNOG; KOG3878; Eukaryota.
DR   eggNOG; ENOG410XS5V; LUCA.
DR   HOGENOM; HOG000247039; -.
DR   HOVERGEN; HBG051712; -.
DR   InParanoid; Q7TNY6; -.
DR   PhylomeDB; Q7TNY6; -.
DR   PRO; PR:Q7TNY6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of 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_dom.
DR   Pfam; PF00887; ACBP; 1.
DR   Pfam; PF13897; GOLD_2; 1.
DR   SUPFAM; SSF101576; SSF101576; 2.
DR   SUPFAM; SSF47027; SSF47027; 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   Acetylation; Coiled coil; Complete proteome; Golgi apparatus;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Steroid biosynthesis.
FT   CHAIN         1    526       Golgi resident protein GCP60.
FT                                /FTId=PRO_0000436451.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
FT   CHAIN         2    526       Golgi resident protein GCP60, N-
FT                                terminally processed.
FT                                /FTId=PRO_0000214031.
FT   DOMAIN       80    171       ACB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00573}.
FT   DOMAIN      381    524       GOLD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00096}.
FT   COILED      169    254       {ECO:0000255}.
FT   COILED      450    471       {ECO:0000255}.
FT   COMPBIAS    179    184       Poly-Glu.
FT   COMPBIAS    186    235       Arg-rich.
FT   COMPBIAS    238    305       Gln-rich.
FT   MOD_RES       2      2       N-acetylalanine; in Golgi resident
FT                                protein GCP60, N-terminally processed.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
FT   MOD_RES      18     18       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
FT   MOD_RES      20     20       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
FT   MOD_RES      40     40       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H3P7}.
SQ   SEQUENCE   526 AA;  60479 MW;  FB1147D95DA48B45 CRC64;
     MAAQLNVEQL EVSLDGLTLS PDSEERPGAE GAPLQTPPSS PPRDGLGSGT AGQQREPGEA
     AAEGAAEEAR RMEQHWGFGL EELYGLALRF YKIKDGKAFH PTYEEKLKFV ALHKQVLLGP
     YNPDTSPEVG FFDVLGNDRR REWAALGNMS KEDAMVEFVK LLNKCCPLLS AYVASHRIEK
     EEEEKRRKAE EERRQREEEE RERLQKEEEK RKREEEDRLR REEEERRRIE EERLRLEQQK
     QQIMAALNSQ TAVQFQQYAA QQYPGNYEQQ QILIRQLQEQ HYQQYMQQLY QVQLAQQQAA
     LQKQQEVVVA GASLPASTKV NTAGASDPLP VNGQAKTHTE NPEKVLEPEA AEEALENGPK
     DSLPVIAAPS MWTRPQIKDF KEKIRQDADS VITVRRGEVV TVRVPTHEEG SYLFWEFATD
     SYDIGFGVYF EWTDSPNAAV SVHVSESSDD EEEEEEENVT CEEKAKKNVN KPLLDEIVPV
     YRRDCHEEVY AGSHQYPGRG VYLLKFDNSY SLWRSKSVYY RVYYTR
//
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