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Golgin subfamily A member 5 (Golgin-84) (Protein Ret-II) (Protein Sumiko)

 GOGA5_MOUSE             Reviewed;         729 AA.
Q9QYE6; O88317; Q3TGE7; Q3U6S5; Q3UUF9;
03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
03-JUL-2003, sequence version 2.
10-MAY-2017, entry version 120.
RecName: Full=Golgin subfamily A member 5;
AltName: Full=Golgin-84;
AltName: Full=Protein Ret-II;
AltName: Full=Protein Sumiko;
Name=Golga5; Synonyms=Retii;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell lymphoma;
Ku P.T., You M.J., Cottam M.K., Bose H.R. Jr.;
"Suppression of anti-immunoglobulin-induced apoptosis in B lymphoma
cells by a novel nuclear protein.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Snider J., Sano H., Ohta M.;
"Unknown, 5' similar to RET-II mRNA.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Involved in maintaining Golgi structure. Stimulates the
formation of Golgi stacks and ribbons. Involved in intra-Golgi
retrograde transport (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with RAB1A that has been activated
by GTP-binding. Interacts with isoform CASP of CUX1 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q99N72:Mcf2; NbExp=3; IntAct=EBI-644242, EBI-641874;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type IV membrane protein {ECO:0000250}. Note=Found
throughout the Golgi. {ECO:0000250}.
-!- PTM: Highly phosphorylated during mitosis. Phosphorylation is
barely detectable during interphase (By similarity).
{ECO:0000250}.
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EMBL; AF026274; AAF21628.1; -; mRNA.
EMBL; AB016784; BAA33010.1; -; mRNA.
EMBL; AK138455; BAE23668.1; -; mRNA.
EMBL; AK152533; BAE31289.1; -; mRNA.
EMBL; AK153010; BAE31649.1; -; mRNA.
EMBL; AK168765; BAE40601.1; -; mRNA.
EMBL; BC016883; AAH16883.1; -; mRNA.
EMBL; BC086782; AAH86782.1; -; mRNA.
CCDS; CCDS36526.1; -.
RefSeq; NP_001185933.1; NM_001199004.1.
RefSeq; NP_038775.1; NM_013747.4.
RefSeq; XP_006515998.1; XM_006515935.3.
UniGene; Mm.273370; -.
ProteinModelPortal; Q9QYE6; -.
SMR; Q9QYE6; -.
IntAct; Q9QYE6; 1.
MINT; MINT-1762194; -.
STRING; 10090.ENSMUSP00000021609; -.
iPTMnet; Q9QYE6; -.
PhosphoSitePlus; Q9QYE6; -.
EPD; Q9QYE6; -.
MaxQB; Q9QYE6; -.
PaxDb; Q9QYE6; -.
PeptideAtlas; Q9QYE6; -.
PRIDE; Q9QYE6; -.
Ensembl; ENSMUST00000021609; ENSMUSP00000021609; ENSMUSG00000021192.
Ensembl; ENSMUST00000179218; ENSMUSP00000137305; ENSMUSG00000021192.
GeneID; 27277; -.
KEGG; mmu:27277; -.
UCSC; uc007oug.2; mouse.
CTD; 9950; -.
MGI; MGI:1351475; Golga5.
eggNOG; KOG4677; Eukaryota.
eggNOG; ENOG410XR4F; LUCA.
GeneTree; ENSGT00390000018470; -.
HOGENOM; HOG000273871; -.
HOVERGEN; HBG051755; -.
InParanoid; Q9QYE6; -.
OMA; NRVDQGA; -.
OrthoDB; EOG091G0HP5; -.
PhylomeDB; Q9QYE6; -.
TreeFam; TF319468; -.
Reactome; R-MMU-6811438; Intra-Golgi traffic.
ChiTaRS; Golga5; mouse.
PRO; PR:Q9QYE6; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000021192; -.
CleanEx; MM_GOLGA5; -.
Genevisible; Q9QYE6; MM.
GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IBA:GO_Central.
InterPro; IPR019177; Golgin_subfamily_A_member_5.
Pfam; PF09787; Golgin_A5; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Golgi apparatus;
Membrane; Methylation; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8TBA6}.
CHAIN 2 729 Golgin subfamily A member 5.
/FTId=PRO_0000190062.
TOPO_DOM 2 696 Cytoplasmic. {ECO:0000255}.
TRANSMEM 697 717 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 718 729 Lumenal. {ECO:0000255}.
COILED 215 629 {ECO:0000255}.
COMPBIAS 150 223 Ser-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q8TBA6}.
MOD_RES 27 27 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q3ZU82}.
MOD_RES 27 27 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 89 89 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q3ZU82}.
MOD_RES 89 89 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CONFLICT 93 93 D -> N (in Ref. 1; AAF21628).
{ECO:0000305}.
CONFLICT 145 145 G -> D (in Ref. 1; AAF21628).
{ECO:0000305}.
CONFLICT 224 224 N -> D (in Ref. 3; BAE31649/BAE31289).
{ECO:0000305}.
CONFLICT 312 312 V -> M (in Ref. 3; BAE23668).
{ECO:0000305}.
CONFLICT 417 417 A -> S (in Ref. 1; AAF21628).
{ECO:0000305}.
CONFLICT 463 463 S -> R (in Ref. 3; BAE40601).
{ECO:0000305}.
CONFLICT 640 640 S -> P (in Ref. 1; AAF21628).
{ECO:0000305}.
CONFLICT 669 669 G -> R (in Ref. 3; BAE31649/BAE31289).
{ECO:0000305}.
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


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