GCP60_MOUSE
ID GCP60_MOUSE Reviewed; 525 AA.
AC Q8BMP6; O35371;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 146.
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, Pap7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PBR AND PKA, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11731621; DOI=10.1210/mend.15.12.0736;
RA Li H., Degenhardt B., Tobin D., Yao Z.-X., Tasken K., Papadopoulos V.;
RT "Identification, localization, and function in steroidogenesis of PAP7: a
RT peripheral-type benzodiazepine receptor- and PKA (RIalpha)-associated
RT protein.";
RL Mol. Endocrinol. 15:2211-2228(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12711385; DOI=10.1016/s0378-1119(03)00453-0;
RA Liu J., Cavalli L.R., Haddad B.R., Papadopoulos V.;
RT "Molecular cloning, genomic organization, chromosomal mapping and
RT subcellular localization of mouse PAP7: a PBR and PKA-RIalpha associated
RT protein.";
RL Gene 308:1-10(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the maintenance of Golgi structure by interacting
CC with giantin, affecting protein transport between the endoplasmic
CC reticulum and Golgi (By similarity). Involved in hormone-induced
CC steroid biosynthesis in testicular Leydig cells (PubMed:12711385).
CC Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme
CC activity of PI4KB activity via its membrane recruitment thereby
CC increasing the local concentration of the substrate in the vicinity of
CC the kinase (By similarity). {ECO:0000250|UniProtKB:Q9H3P7,
CC ECO:0000269|PubMed:12711385}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with the C-terminal
CC cytoplasmic domain of giantin/GOLGB1 (By similarity). Interacts with
CC PBR and PKA regulatory subunit RI-alpha. Does not interact with PKA
CC regulatory subunit RI-beta nor PKA regulatory subunit RII-alpha
CC (PubMed:11731621). Interacts (via Q domain) with PI4KB (via N-terminus)
CC (By similarity). Interacts (via Q domain) with TBC1D22A AND TBC1D22B;
CC interactions with PI4KB and with TBC1D22A and TBC1D22B are mutually
CC exclusive (By similarity). Interacts with C10ORF76 and RAB11B (By
CC similarity). {ECO:0000250|UniProtKB:Q9H3P7,
CC ECO:0000269|PubMed:11731621}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12711385}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12711385}; Cytoplasmic side
CC {ECO:0000269|PubMed:12711385}. Mitochondrion
CC {ECO:0000269|PubMed:12711385}. Note=Also mitochondrial (via its
CC interaction with PBR).
CC -!- TISSUE SPECIFICITY: Expressed in brain (hippocampus, olfactory bulb,
CC neuronal and glial cells of the cortex), eye, submaxillary gland,
CC testis (interstitial and tubular compartments), ovary (granulosa cells,
CC theca cells at late stages and primary follicles), adrenal gland
CC (fasciculata and glomerulosa cells), heart, liver, and steroidogenic
CC cell lines. {ECO:0000269|PubMed:11731621}.
CC -!- DEVELOPMENTAL STAGE: Present in embryo. Decreases before birth.
CC {ECO:0000269|PubMed:11731621}.
CC -!- DOMAIN: The central Gln-rich region (Q domain) is involved in binding
CC to PI4KB, TBC1D22A and TBC1D22B (By similarity). The C-terminal GOLD
CC domain is essential for giantin binding. The GOLD domain is also
CC involved in homodimerization (By similarity).
CC {ECO:0000250|UniProtKB:Q9H3P7}.
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DR EMBL; AF022770; AAB71197.3; -; mRNA.
DR EMBL; AF501319; AAM22185.1; -; Genomic_DNA.
DR EMBL; AK030371; BAC26928.1; -; mRNA.
DR CCDS; CCDS15572.1; -.
DR RefSeq; NP_573488.2; NM_133225.3.
DR AlphaFoldDB; Q8BMP6; -.
DR SMR; Q8BMP6; -.
DR BioGRID; 228422; 18.
DR IntAct; Q8BMP6; 1.
DR STRING; 10090.ENSMUSP00000027780; -.
DR iPTMnet; Q8BMP6; -.
DR PhosphoSitePlus; Q8BMP6; -.
DR SwissPalm; Q8BMP6; -.
DR EPD; Q8BMP6; -.
DR jPOST; Q8BMP6; -.
DR MaxQB; Q8BMP6; -.
DR PaxDb; Q8BMP6; -.
DR PeptideAtlas; Q8BMP6; -.
DR PRIDE; Q8BMP6; -.
DR ProteomicsDB; 265735; -.
DR DNASU; 170760; -.
DR GeneID; 170760; -.
DR KEGG; mmu:170760; -.
DR UCSC; uc007dwq.2; mouse.
DR CTD; 64746; -.
DR MGI; MGI:2181074; Acbd3.
DR eggNOG; KOG3878; Eukaryota.
DR InParanoid; Q8BMP6; -.
DR OrthoDB; 733463at2759; -.
DR PhylomeDB; Q8BMP6; -.
DR TreeFam; TF321667; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 170760; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acbd3; mouse.
DR PRO; PR:Q8BMP6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BMP6; protein.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
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:MGI.
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..525
FT /note="Golgi resident protein GCP60"
FT /id="PRO_0000436450"
FT DOMAIN 80..171
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT DOMAIN 381..523
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 12..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="Q domain; Interaction with PI4KB, TBC1D22A and
FT TBC1D22B"
FT /evidence="ECO:0000250|UniProtKB:Q9H3P7"
FT REGION 319..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..254
FT /evidence="ECO:0000255"
FT COILED 448..470
FT /evidence="ECO:0000255"
FT COMPBIAS 319..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 525 AA; 60181 MW; C043CEBF56FCE702 CRC64;
MAAQLNVEQL EVSLDGLTLS PDSEERPGAE GAPPQTPPSS APGNGLGSGA SGQQREPGEA
AAEGAAEEAR RMEQHWGFGL EELYGLALRF YKIKDGKAFH PTYEEKLKFV ALHKQVLLGP
YNPDTSPEVG FFDVLGNDRR REWAALGNMS KEDAMVEFVK LLNKCCPLLS AYVASHRIEK
EEEEKRRKAE EERRQREEEE RERLQKEEEK RKREKEDRLR REEEERRRIE EERLRLEQQK
QQIMAALNSQ TAVQFQQYAA QQYPGNYEQQ QILIRQLQEQ HYQQYMQQLY QVQLAQQQAA
LQKQQEVVMA GASLPASSKV NTAGASDTLS VNGQAKTHTE NSEKVLEPEA AEEALENGPK
DSLPVIAAPS MWTRPQIKDF KEKIRQDADS VITVRRGEVV TVRVPTHEEG SYLFWEFATD
SYDIGFGVYF EWTDSPNAAV SVHVSESSDE EEEEEENVTC EEKAKKNANK PLLDEIVPVY
RRDCHEEVYA GSHQYPGRGV YLLKFDNSYS LWRSKSVYYR VYYTR
