GOGA2_MOUSE
ID GOGA2_MOUSE Reviewed; 999 AA.
AC Q921M4; A2AN43; A2AN47;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Golgin subfamily A member 2;
DE AltName: Full=130 kDa cis-Golgi matrix protein;
DE Short=GM130 {ECO:0000303|PubMed:21552007, ECO:0000303|PubMed:26165940};
GN Name=Golga2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-999 (ISOFORM 2).
RC TISSUE=Mammary cancer;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21552007; DOI=10.4161/cc.10.11.15797;
RA Zhang C.H., Wang Z.B., Quan S., Huang X., Tong J.S., Ma J.Y., Guo L.,
RA Wei Y.C., Ouyang Y.C., Hou Y., Xing F.Q., Sun Q.Y.;
RT "GM130, a cis-Golgi protein, regulates meiotic spindle assembly and
RT asymmetric division in mouse oocyte.";
RL Cell Cycle 10:1861-1870(2011).
RN [6]
RP FUNCTION, AND MICROTUBULE-BINDING.
RX PubMed=26165940; DOI=10.1016/j.cell.2015.06.014;
RA Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.;
RT "GM130 regulates Golgi-derived spindle assembly by activating TPX2 and
RT capturing microtubules.";
RL Cell 162:287-299(2015).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=28617811; DOI=10.1371/journal.pgen.1006803;
RA Cartier-Michaud A., Bailly A.L., Betzi S., Shi X., Lissitzky J.C.,
RA Zarubica A., Serge A., Roche P., Lugari A., Hamon V., Bardin F.,
RA Derviaux C., Lembo F., Audebert S., Marchetto S., Durand B., Borg J.P.,
RA Shi N., Morelli X., Aurrand-Lions M.;
RT "Genetic, structural, and chemical insights into the dual function of
RT GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization
RT during spermatogenesis.";
RL PLoS Genet. 13:e1006803-e1006803(2017).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=28028212; DOI=10.1073/pnas.1608576114;
RA Liu C., Mei M., Li Q., Roboti P., Pang Q., Ying Z., Gao F., Lowe M.,
RA Bao S.;
RT "Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss,
RT and ataxia in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:346-351(2017).
CC -!- FUNCTION: Peripheral membrane component of the cis-Golgi stack that
CC acts as a membrane skeleton that maintains the structure of the Golgi
CC apparatus, and as a vesicle thether that facilitates vesicle fusion to
CC the Golgi membrane (PubMed:28028212). Required for normal protein
CC transport from the endoplasmic reticulum to the Golgi apparatus and the
CC cell membrane (PubMed:28028212). Together with p115/USO1 and STX5,
CC involved in vesicle tethering and fusion at the cis-Golgi membrane to
CC maintain the stacked and inter-connected structure of the Golgi
CC apparatus. Plays a central role in mitotic Golgi disassembly:
CC phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the
CC interaction with p115/USO1, preventing tethering of COPI vesicles and
CC thereby inhibiting transport through the Golgi apparatus during
CC mitosis. Also plays a key role in spindle pole assembly and centrosome
CC organization (By similarity). Promotes the mitotic spindle pole
CC assembly by activating the spindle assembly factor TPX2 to nucleate
CC microtubules around the Golgi and capture them to couple mitotic
CC membranes to the spindle: upon phosphorylation at the onset of mitosis,
CC GOLGA2 interacts with importin-alpha via the nuclear localization
CC signal region, leading to recruit importin-alpha to the Golgi membranes
CC and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2
CC then activates AURKA kinase and stimulates local microtubule
CC nucleation. Upon filament assembly, nascent microtubules are further
CC captured by GOLGA2, thus linking Golgi membranes to the spindle (By
CC similarity). Regulates the meiotic spindle pole assembly, probably via
CC the same mechanism (PubMed:21552007). Also regulates the centrosome
CC organization (By similarity). Also required for the Golgi ribbon
CC formation and glycosylation of membrane and secretory proteins (By
CC similarity). {ECO:0000250|UniProtKB:Q08379,
CC ECO:0000250|UniProtKB:Q62839, ECO:0000269|PubMed:21552007,
CC ECO:0000269|PubMed:28028212}.
CC -!- SUBUNIT: Homodimer, may assemble into homohexamers (By similarity).
CC Homotetramer; forms a parallel homotetramer with a flexible rod-like
CC structure that can give rise to I- and Y-shaped conformations.
CC Interacts with GORASP1/GRASP65. The homooligomer forms a complex with
CC GORASP1 with a 1:1 stoichiometry (By similarity). Interacts with RAB1B
CC that has been activated by GTP-binding. Interacts with p115/USO1;
CC interaction with p115/USO1 inhibits interaction with STX5 and/or RAB1B.
CC Interacts with STX5 (By similarity). Interacts with ZFPL1 (By
CC similarity). Interacts with AKAP450/AKAP9; leading to recruit
CC AKAP450/AKAP9 to the cis-Golgi (By similarity).
CC {ECO:0000250|UniProtKB:Q08379, ECO:0000250|UniProtKB:Q62839}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q08379}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q08379}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:Q08379};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q08379}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000250|UniProtKB:Q08379}. Note=Associates with the mitotic
CC spindle during mitosis. {ECO:0000250|UniProtKB:Q08379,
CC ECO:0000250|UniProtKB:Q62839}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q921M4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921M4-2; Sequence=VSP_039027;
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, liver, thymus and pancreas
CC (PubMed:28028212). Detected in spermatocytes (PubMed:28617811). Present
CC in oocytes during all oocyte meiotic maturation (at protein level).
CC {ECO:0000269|PubMed:21552007, ECO:0000269|PubMed:28028212,
CC ECO:0000269|PubMed:28617811}.
CC -!- DOMAIN: Extended rod-like protein with long coiled-coil domains.
CC {ECO:0000250|UniProtKB:Q62839}.
CC -!- DOMAIN: The nuclear localization signal (cNLS) mediates interaction
CC with importin-alpha, recruiting importin-alpha to the Golgi membrane
CC and liberating TPX2. {ECO:0000250|UniProtKB:Q08379}.
CC -!- PTM: Phosphorylated at Ser-37 by CDK1 at the onset of mitosis,
CC inhibiting the interaction with p115/USO1 and triggering Golgi
CC disassembly. A report however suggests that Golgi disassembly is
CC independent of phosphorylation at Ser-37. Phosphorylated at Ser-37 in
CC prophase as the Golgi complex starts to break down, and remains
CC phosphorylated during further breakdown and partitioning of the Golgi
CC fragments in metaphase and anaphase. In telophase, GM130 is
CC dephosphorylated by PP2A as the Golgi fragments start to reassemble.
CC {ECO:0000250|UniProtKB:Q62839}.
CC -!- PTM: Cleaved by caspases at the onset of apoptosis.
CC {ECO:0000250|UniProtKB:Q08379}.
CC -!- PTM: Methylation by PRMT5 is required for Golgi ribbon formation.
CC {ECO:0000250|UniProtKB:Q08379}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and
CC have normal weight at birth. However, they display strongly decreased
CC growth during the following weeks and die between 15 and 35 days after
CC birth. Mice display ataxia and motor coordination defects that worsen
CC with increasing age. Mice with a neuron-specific gene disruption
CC display normal overall brain architecture, but the size of the
CC cerebellum is strongly reduced in adults. After the third week after
CC birth, a progressive loss of Purkinje cell is observed, leading to
CC cerebellar atrophy. Purkinje cells from mutant mice appear normal at 9
CC days after birth, but display a strong decrease of the size and
CC arborization of dendrites, associated with impaired dendritic protein
CC transport. Other neurons in the molecular or granule layer of the
CC cerebellum are not affected. Mice with a neuron-specific gene
CC disruption display decreased growth, but have a normal lifespan and
CC have only mild motor coordination defects at three weeks after birth,
CC but defects are obvious at 8 weeks after birth.
CC {ECO:0000269|PubMed:28028212}.
CC -!- SIMILARITY: Belongs to the GOLGA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM15849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL808027; CAM15845.1; -; Genomic_DNA.
DR EMBL; AL808027; CAM15849.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH466542; EDL08537.1; -; Genomic_DNA.
DR EMBL; BC011407; AAH11407.1; ALT_INIT; mRNA.
DR RefSeq; NP_001074437.1; NM_001080968.1.
DR RefSeq; XP_006498556.1; XM_006498493.3.
DR AlphaFoldDB; Q921M4; -.
DR SMR; Q921M4; -.
DR BioGRID; 221239; 17.
DR IntAct; Q921M4; 7.
DR MINT; Q921M4; -.
DR STRING; 10090.ENSMUSP00000109004; -.
DR iPTMnet; Q921M4; -.
DR PhosphoSitePlus; Q921M4; -.
DR SwissPalm; Q921M4; -.
DR EPD; Q921M4; -.
DR jPOST; Q921M4; -.
DR MaxQB; Q921M4; -.
DR PaxDb; Q921M4; -.
DR PeptideAtlas; Q921M4; -.
DR PRIDE; Q921M4; -.
DR ProteomicsDB; 271245; -. [Q921M4-1]
DR ProteomicsDB; 271246; -. [Q921M4-2]
DR Ensembl; ENSMUST00000113377; ENSMUSP00000109004; ENSMUSG00000002546. [Q921M4-1]
DR GeneID; 99412; -.
DR KEGG; mmu:99412; -.
DR UCSC; uc008jew.1; mouse. [Q921M4-1]
DR UCSC; uc008jex.1; mouse. [Q921M4-2]
DR CTD; 2801; -.
DR MGI; MGI:2139395; Golga2.
DR VEuPathDB; HostDB:ENSMUSG00000002546; -.
DR eggNOG; KOG4725; Eukaryota.
DR GeneTree; ENSGT00530000062932; -.
DR InParanoid; Q921M4; -.
DR PhylomeDB; Q921M4; -.
DR TreeFam; TF316990; -.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 99412; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Golga2; mouse.
DR PRO; PR:Q921M4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q921M4; protein.
DR Bgee; ENSMUSG00000002546; Expressed in animal zygote and 249 other tissues.
DR ExpressionAtlas; Q921M4; baseline and differential.
DR Genevisible; Q921M4; MM.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000137; C:Golgi cis cisterna; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
DR GO; GO:0051645; P:Golgi localization; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR043937; GM130_C.
DR InterPro; IPR043976; GOLGA_cons_dom.
DR InterPro; IPR024858; Golgin_A.
DR PANTHER; PTHR10881; PTHR10881; 1.
DR Pfam; PF19046; GM130_C; 1.
DR Pfam; PF15070; GOLGA2L5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Membrane; Methylation; Microtubule; Mitosis;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..999
FT /note="Golgin subfamily A member 2"
FT /id="PRO_0000190055"
FT REGION 1..86
FT /note="Interaction with p115/USO1"
FT /evidence="ECO:0000250|UniProtKB:Q62839"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..999
FT /note="Interaction with GORASP1/GRASP65"
FT /evidence="ECO:0000250|UniProtKB:Q62839"
FT COILED 147..895
FT /evidence="ECO:0000255"
FT MOTIF 26..49
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT COMPBIAS 244..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 30
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62839"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 70..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039027"
SQ SEQUENCE 999 AA; 113278 MW; 0D84161E727EA9F5 CRC64;
MWPPRFPPPR PGMSEETRQS KLAAAKKKLR EYQQKNSPGV PAGAKKKKKI KNGHSPERPT
ASDCQSPENV PTDHIAPAPP TAATDTMFLG VTPSPDADLT QSHDAGNCSN LMEETKTFSS
TESLRQLSQQ LNGLVSESTS YINGEGLTSS NMKELENRYQ ELAVALDSSY VTNKQLSSTI
EELKQQNQDT LDQLEKEKKD YQQKLAKEQG SLREQLQVHI QTIGILVSEK AELQTALAHT
QQAARQKAGE SEDLASRLQS SRQRVGELER TLSTVSTQQK QADRYNKDLT KERDALKLEL
YKNSKSNEDL RQQNSELEEK LRVLVAEKAA AQLGVEELQK KLEMSELLLQ QFSSQSSAAG
GNEQLQHAME ERAQLETHVS QLMESLKQLQ VERDQYAENL KGESAMWQQR VQQMAEQVHT
LKEEKEHRER QVQELETSLA ALRSQMEEPP PPEPPAGPSE AEEQLQGEVE QLHKELERLT
GQLRAQVQDN ESLSHLNREQ EGRLLELERE AQRWSEQAEE RKQILESMQS DRTTISRALS
QNRELKEQLA ELQNGFVRLT NENMEITSAL QSEQHVKKEL ARKLGELQER LGELKETVEL
KSQEAQGLQE QRDQCLSHLQ QYAAAYQQHL AAYEQLTSEK EAIHKQLLLQ TQLMDQLQHE
EVQGKMAAEL ARQELQEAQE RLKATSQENQ QLQAQLSLLV LPGEGDVDQE EEDEEVPQSS
LAIPEDLDSR EAMVAFFNAA IARAEEEQAR LRVQLKEQKA RCRSLSHLAA PVQSKLEKEA
VVPRNVDDSA SEESNQALHV AMEKLQSRFL EVMQEKVELK ERVEELEHCC IQLSGETDTI
GEYIALYQNQ RAVLKARHLE KEEYISRLAQ DKEEMKVKLL ELQELVLRLV NERNEWQGKF
LAVSQNPGDV LTPVPTGSQE FGAADQQDDL REVSLADDIE PAQGEAGVPA PHENPTAQQI
MQLLREIQNP RERPGLGSNP CIPFFYRADE NDEVKIMVV
