GCP60_RAT
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 25-MAY-2022, entry version 115.
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;
GN Name=Acbd3; Synonyms=Gcp60;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the maintenance of Golgi structure by interacting
CC with giantin, affecting protein transport between the endoplasmic
CC reticulum and Golgi. Involved in hormone-induced steroid biosynthesis
CC in testicular Leydig cells. Recruits PI4KB to the Golgi apparatus
CC membrane; enhances the enzyme activity of PI4KB activity via its
CC membrane recruitment thereby increasing the local concentration of the
CC substrate in the vicinity of the kinase. {ECO:0000250|UniProtKB:Q8BMP6,
CC ECO:0000250|UniProtKB:Q9H3P7}.
CC -!- SUBUNIT: Interacts with the C-terminal cytoplasmic domain of
CC giantin/GOLGB1 (By similarity). Interacts with PBR and PKA regulatory
CC subunit RI-alpha. Does not interact with PKA regulatory subunit RI-beta
CC nor PKA regulatory subunit RII-alpha (By similarity). Interacts with
CC PI4KB, TBC1D22A AND TBC1D22B; interactions with PI4KB and with TBC1D22A
CC and TBC1D22B are mutually exclusive. Interacts with C10ORF76 and RAB11B
CC (By similarity). {ECO:0000250|UniProtKB:Q8BMP6,
CC ECO:0000250|UniProtKB:Q9H3P7}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9H3P7}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Also mitochondrial (via its interaction with PBR).
CC {ECO:0000250}.
CC -!- DOMAIN: The GOLD domain is essential for giantin binding.
CC {ECO:0000250}.
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DR EMBL; AY336075; AAP94639.1; -; mRNA.
DR RefSeq; NP_878263.1; NM_182843.1.
DR AlphaFoldDB; Q7TNY6; -.
DR SMR; Q7TNY6; -.
DR BioGRID; 252874; 1.
DR STRING; 10116.ENSRNOP00000004293; -.
DR iPTMnet; Q7TNY6; -.
DR PhosphoSitePlus; Q7TNY6; -.
DR jPOST; 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 InParanoid; Q7TNY6; -.
DR OrthoDB; 733463at2759; -.
DR PhylomeDB; Q7TNY6; -.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR PRO; PR:Q7TNY6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
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; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT CHAIN 2..526
FT /note="Golgi resident protein GCP60"
FT /id="PRO_0000436451"
FT DOMAIN 80..171
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT DOMAIN 381..524
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 13..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..305
FT /note="Interaction with PI4KB"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT REGION 318..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..254
FT /evidence="ECO:0000255"
FT COILED 450..471
FT /evidence="ECO:0000255"
FT COMPBIAS 318..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="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
