GOGA5_RAT
ID GOGA5_RAT Reviewed; 728 AA.
AC Q3ZU82;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Golgin subfamily A member 5;
DE AltName: Full=Golgin-84;
GN Name=Golga5;
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], INTERACTION WITH RAB1A, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=12656988; DOI=10.1034/j.1600-0854.2003.00103.x;
RA Satoh A., Wang Y., Malsam J., Beard M.B., Warren G.;
RT "Golgin-84 is a rab1 binding partner involved in Golgi structure.";
RL Traffic 4:153-161(2003).
RN [2]
RP METHYLATION AT ARG-27 AND ARG-89, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA Yates J.R. III, Howell K.E.;
RT "Organellar proteomics reveals Golgi arginine dimethylation.";
RL Mol. Biol. Cell 15:2907-2919(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH CUX1.
RX PubMed=15718469; DOI=10.1126/science.1108061;
RA Malsam J., Satoh A., Pelletier L., Warren G.;
RT "Golgin tethers define subpopulations of COPI vesicles.";
RL Science 307:1095-1098(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP 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 maintaining Golgi structure. Stimulates the
CC formation of Golgi stacks and ribbons. Involved in intra-Golgi
CC retrograde transport. {ECO:0000269|PubMed:12656988,
CC ECO:0000269|PubMed:15718469}.
CC -!- SUBUNIT: Homodimer. Interacts with RAB1A that has been activated by
CC GTP-binding. Interacts with isoform CASP of CUX1.
CC {ECO:0000269|PubMed:12656988, ECO:0000269|PubMed:15718469}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12656988}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:12656988}. Note=Found throughout the Golgi.
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; AY144587; AAN17671.1; -; mRNA.
DR RefSeq; NP_001028237.1; NM_001033065.1.
DR AlphaFoldDB; Q3ZU82; -.
DR SMR; Q3ZU82; -.
DR STRING; 10116.ENSRNOP00000010385; -.
DR iPTMnet; Q3ZU82; -.
DR PhosphoSitePlus; Q3ZU82; -.
DR jPOST; Q3ZU82; -.
DR PaxDb; Q3ZU82; -.
DR PeptideAtlas; Q3ZU82; -.
DR PRIDE; Q3ZU82; -.
DR GeneID; 299258; -.
DR KEGG; rno:299258; -.
DR UCSC; RGD:1308163; rat.
DR CTD; 9950; -.
DR RGD; 1308163; Golga5.
DR eggNOG; KOG4677; Eukaryota.
DR InParanoid; Q3ZU82; -.
DR PhylomeDB; Q3ZU82; -.
DR PRO; PR:Q3ZU82; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005801; C:cis-Golgi network; ISO:RGD.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:RGD.
DR GO; GO:0031985; C:Golgi cisterna; ISO:RGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0007030; P:Golgi organization; IDA:RGD.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:RGD.
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..728
FT /note="Golgin subfamily A member 5"
FT /id="PRO_0000190063"
FT TOPO_DOM 2..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..728
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 88..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..628
FT /evidence="ECO:0000255"
FT COMPBIAS 149..186
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:0000269|PubMed:15047867"
FT MOD_RES 89
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 728 AA; 82334 MW; 0C30FCB93C8E310A CRC64;
MSWFADLAGR AEDLLNRVDQ GAATALRKES TSNTFYSKNT DYPELHQQNT DSTYHTGQKA
NYISSAADNI RHQKATIIAG TANVKVGSRT GGDASHPTEH ASVPRPSSHF VRRKKSEPDD
ELLFDFLNSS QKEPTGRVEI KKEKGKAPVL PSSQSSAVSS VTTSVTTIKA TEENSGSQSP
EVSSSDSMPE GHKKSTEEST VSNAISVEHS SVPSDGSMSH ELSNLRLENQ LLRNEVQSLN
QEMASLLQRS KETQEELNEA RVRVEKWNVD NSKSDRITRE LRAQVDDLTE AVAAKDSQLA
VLKVRLQEAD QVLSSRTEAL EALQSEKSRI MQDHNEGSSL QNQALQTLQE RHEADATLKR
EQESYKQMQS EFATRLNKME VERQNLAEAV TLAERKYSEE RKKVDDLQQQ VKLHRSSLES
AKQELVDYKQ KATRILQSKE KLINSLKEGS SFEGLDSSTA SSMELEELRH ERELQKEEIQ
KLMGQIHQLR SELQDMEAQQ VSEAESAREQ LQDLQDQIAK QRASKQELET ELDRMKQEFH
YVEEDLHRTK NTLQSRIKDR EEEIQKLRNQ LTNKTLSNSS QSELESRLHQ LTETLIQKQT
LLESLSTEKN SLVFQLERLE QQLHSAATGP SSGSSINMSG VDSGEGTRLR NVPVLFNDTE
TNLAGMYGKV RKAASSIDQF SIRLGIFLRR YPIARVFVII YMALLHLWVM IVLLTYSPEM
HHDQPYGK
