GOGA5_MOUSE
ID GOGA5_MOUSE Reviewed; 729 AA.
AC Q9QYE6; O88317; Q3TGE7; Q3U6S5; Q3UUF9;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Golgin subfamily A member 5;
DE AltName: Full=Golgin-84;
DE AltName: Full=Protein Ret-II;
DE AltName: Full=Protein Sumiko;
GN Name=Golga5; Synonyms=Retii;
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].
RC TISSUE=B-cell lymphoma;
RA Ku P.T., You M.J., Cottam M.K., Bose H.R. Jr.;
RT "Suppression of anti-immunoglobulin-induced apoptosis in B lymphoma cells
RT by a novel nuclear protein.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Snider J., Sano H., Ohta M.;
RT "Unknown, 5' similar to RET-II mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Spinal cord;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP 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 maintaining Golgi structure. Stimulates the
CC formation of Golgi stacks and ribbons. Involved in intra-Golgi
CC retrograde transport (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with RAB1A that has been activated by
CC GTP-binding. Interacts with isoform CASP of CUX1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9QYE6; Q99N72: Mcf2; NbExp=3; IntAct=EBI-644242, EBI-641874;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Note=Found throughout the
CC Golgi. {ECO:0000250}.
CC -!- PTM: Highly phosphorylated during mitosis. Phosphorylation is barely
CC detectable during interphase (By similarity). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF026274; AAF21628.1; -; mRNA.
DR EMBL; AB016784; BAA33010.1; -; mRNA.
DR EMBL; AK138455; BAE23668.1; -; mRNA.
DR EMBL; AK152533; BAE31289.1; -; mRNA.
DR EMBL; AK153010; BAE31649.1; -; mRNA.
DR EMBL; AK168765; BAE40601.1; -; mRNA.
DR EMBL; BC016883; AAH16883.1; -; mRNA.
DR EMBL; BC086782; AAH86782.1; -; mRNA.
DR CCDS; CCDS36526.1; -.
DR RefSeq; NP_001185933.1; NM_001199004.1.
DR RefSeq; NP_038775.1; NM_013747.4.
DR RefSeq; XP_006515998.1; XM_006515935.3.
DR AlphaFoldDB; Q9QYE6; -.
DR SMR; Q9QYE6; -.
DR BioGRID; 205157; 2.
DR IntAct; Q9QYE6; 1.
DR STRING; 10090.ENSMUSP00000137305; -.
DR iPTMnet; Q9QYE6; -.
DR PhosphoSitePlus; Q9QYE6; -.
DR EPD; Q9QYE6; -.
DR jPOST; Q9QYE6; -.
DR MaxQB; Q9QYE6; -.
DR PaxDb; Q9QYE6; -.
DR PeptideAtlas; Q9QYE6; -.
DR PRIDE; Q9QYE6; -.
DR ProteomicsDB; 267742; -.
DR Antibodypedia; 15; 264 antibodies from 26 providers.
DR Ensembl; ENSMUST00000021609; ENSMUSP00000021609; ENSMUSG00000021192.
DR Ensembl; ENSMUST00000179218; ENSMUSP00000137305; ENSMUSG00000021192.
DR GeneID; 27277; -.
DR KEGG; mmu:27277; -.
DR UCSC; uc007oug.2; mouse.
DR CTD; 9950; -.
DR MGI; MGI:1351475; Golga5.
DR VEuPathDB; HostDB:ENSMUSG00000021192; -.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000018470; -.
DR HOGENOM; CLU_022484_0_0_1; -.
DR InParanoid; Q9QYE6; -.
DR OMA; CSSYEAH; -.
DR OrthoDB; 1325011at2759; -.
DR PhylomeDB; Q9QYE6; -.
DR TreeFam; TF319468; -.
DR BioGRID-ORCS; 27277; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Golga5; mouse.
DR PRO; PR:Q9QYE6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QYE6; protein.
DR Bgee; ENSMUSG00000021192; Expressed in animal zygote and 264 other tissues.
DR ExpressionAtlas; Q9QYE6; baseline and differential.
DR Genevisible; Q9QYE6; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; ISO:MGI.
DR GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; ISO:MGI.
DR InterPro; IPR019177; Golgin_subfamily_A_member_5.
DR PANTHER; PTHR13815; PTHR13815; 2.
DR Pfam; PF09787; Golgin_A5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Golgi apparatus; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TBA6"
FT CHAIN 2..729
FT /note="Golgin subfamily A member 5"
FT /id="PRO_0000190062"
FT TOPO_DOM 2..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..729
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 89..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..629
FT /evidence="ECO:0000255"
FT COMPBIAS 151..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBA6"
FT MOD_RES 27
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZU82"
FT MOD_RES 89
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZU82"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 93
FT /note="D -> N (in Ref. 1; AAF21628)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="G -> D (in Ref. 1; AAF21628)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="N -> D (in Ref. 3; BAE31649/BAE31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> M (in Ref. 3; BAE23668)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="A -> S (in Ref. 1; AAF21628)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="S -> R (in Ref. 3; BAE40601)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="S -> P (in Ref. 1; AAF21628)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="G -> R (in Ref. 3; BAE31649/BAE31289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 82368 MW; 8418BE8E6E4865E1 CRC64;
MSWFADLAGR AEDLLNRVDQ GAATALRKEN TSNIFYSKNT DYPELQQQNT DSNYQTGQKA
NYISSAADNI RHQKATILAG TANVKVGSRT VGDATHPTEH ASAPRPSSQF VRRKKSEPDD
ELLFDFLNSS QKEPTGRVEV KKEKGRAPVS PSSPSGVSSV NTSVTTTKAM GGNAGSQSPG
VNSSDSVPEV HKEPSEESTA PSATSEEHSS TPSDGSSRSQ ELSNLRLENQ LLRNEVQSLN
QEMASLLQRS KETQEELNKA RVRVEKWNVD NSKSDRITRE LRAQVDDLTE AVAAKDSQLA
VLKVRLQEAD QVLSSRTEAL EALRSEKSRI MQDHKEGSSL QNQALQTLQE RLHEADATLK
REQESYKQMQ SEFAARLNKM EVDRQNLAEA VTLAERKYSE EKKKVDELQQ QVKLHRASLE
SAKQELVDYK QKATRILQSK EKLINSLKEG SSFEGLESST ASSMELEELR HEKEMQKEEI
QKLMGQMHQL RSELQDMEAQ QVSEAESARE QLQDLQDQIA KQRTSKQELE TELERMKQEF
RYMEEDLHRT KNTLQSRIKD REEEIQKLRN QLTNKTLSNS SQSELESRLH QLTETLIQKQ
TMLESLSTEK NSLVFQLERL EQQVHSASSG PNSGSAINMS GVDSGEGTRL RNVPVLFNDT
ETNLAGMYGK VRKAASSIDQ FSIRLGIFLR RYPIARVFVI IYMALLHLWV MIVLLTYSPE
MHHDQPYGK
