ID COPG2_MOUSE Reviewed; 871 AA.
AC Q9QXK3; A6H6J5; Q3TQD5; Q3UEL6; Q8C2J6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=Copg2;
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] (ISOFORM 1).
RA Lee Y.J., Chung J.H.;
RT "Imprinted Copg2 gene for gamma2-COP from mouse.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=11032317; DOI=10.1023/a:1009263504671;
RA Brunner B., Gruetzner F., Yaspo M.-L., Ropers H.-H., Haaf T.,
RA Kalscheuer V.M.;
RT "Molecular cloning and characterization of the Fugu rubripes MEST/COPG2
RT imprinting cluster and chromosomal localization in Fugu and Tetraodon
RT nigroviridis.";
RL Chromosome Res. 8:465-476(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Medulla oblongata, and Thymus;
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] (ISOFORM 1).
RC TISSUE=Brain, and Olfactory epithelium;
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 SUBCELLULAR LOCATION.
RX PubMed=17360540; DOI=10.1073/pnas.0611360104;
RA Moelleken J., Malsam J., Betts M.J., Movafeghi A., Reckmann I.,
RA Meissner I., Hellwig A., Russell R.B., Sollner T., Brugger B.,
RA Wieland F.T.;
RT "Differential localization of coatomer complex isoforms within the Golgi
RT apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4425-4430(2007).
RN [6]
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: The coatomer is a cytosolic protein complex that binds to
CC dilysine motifs and reversibly associates with Golgi non-clathrin-
CC coated vesicles, which further mediate biosynthetic protein transport
CC from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC complex is required for budding from Golgi membranes, and is essential
CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC In mammals, the coatomer can only be recruited by membranes associated
CC to ADP-ribosylation factors (ARFs), which are small GTP-binding
CC proteins; the complex also influences the Golgi structural integrity,
CC as well as the processing, activity, and endocytic recycling of LDL
CC receptors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex. Binds to CDC42. Interacts with JAGN1.
CC Interacts with TMED10 (via cytoplasmic domain).
CC {ECO:0000250|UniProtKB:Q9UBF2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}.
CC Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. Tends to be more
CC abundant in the trans-Golgi network compared to the cis-Golgi.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9QXK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXK3-2; Sequence=VSP_034480, VSP_034481;
CC Name=3;
CC IsoId=Q9QXK3-3; Sequence=VSP_034482, VSP_034483;
CC Name=4;
CC IsoId=Q9QXK3-4; Sequence=VSP_034484;
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; AF205065; AAF17607.1; -; mRNA.
DR EMBL; AJ251067; CAB96146.1; -; mRNA.
DR EMBL; AK088492; BAC40387.1; -; mRNA.
DR EMBL; AK149462; BAE28895.1; -; mRNA.
DR EMBL; AK163668; BAE37449.1; -; mRNA.
DR EMBL; BC049178; AAH49178.1; -; mRNA.
DR EMBL; BC145898; AAI45899.1; -; mRNA.
DR EMBL; BC145900; AAI45901.1; -; mRNA.
DR CCDS; CCDS85027.1; -. [Q9QXK3-1]
DR RefSeq; NP_059506.1; NM_017478.3. [Q9QXK3-1]
DR AlphaFoldDB; Q9QXK3; -.
DR SMR; Q9QXK3; -.
DR BioGRID; 207586; 6.
DR IntAct; Q9QXK3; 2.
DR MINT; Q9QXK3; -.
DR STRING; 10090.ENSMUSP00000038368; -.
DR GlyGen; Q9QXK3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9QXK3; -.
DR PhosphoSitePlus; Q9QXK3; -.
DR SwissPalm; Q9QXK3; -.
DR EPD; Q9QXK3; -.
DR jPOST; Q9QXK3; -.
DR MaxQB; Q9QXK3; -.
DR PaxDb; 10090-ENSMUSP00000038368; -.
DR PeptideAtlas; Q9QXK3; -.
DR ProteomicsDB; 284085; -. [Q9QXK3-1]
DR ProteomicsDB; 284086; -. [Q9QXK3-2]
DR ProteomicsDB; 284087; -. [Q9QXK3-3]
DR ProteomicsDB; 284088; -. [Q9QXK3-4]
DR Pumba; Q9QXK3; -.
DR Antibodypedia; 69166; 118 antibodies from 21 providers.
DR DNASU; 54160; -.
DR Ensembl; ENSMUST00000048774.13; ENSMUSP00000038368.7; ENSMUSG00000025607.16. [Q9QXK3-1]
DR Ensembl; ENSMUST00000166192.7; ENSMUSP00000126726.4; ENSMUSG00000025607.16. [Q9QXK3-4]
DR GeneID; 54160; -.
DR KEGG; mmu:54160; -.
DR UCSC; uc029vty.2; mouse. [Q9QXK3-1]
DR AGR; MGI:1858683; -.
DR CTD; 26958; -.
DR MGI; MGI:1858683; Copg2.
DR VEuPathDB; HostDB:ENSMUSG00000025607; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; Q9QXK3; -.
DR OMA; IEDCEYN; -.
DR OrthoDB; 5260816at2759; -.
DR PhylomeDB; Q9QXK3; -.
DR TreeFam; TF300324; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 54160; 2 hits in 23 CRISPR screens.
DR ChiTaRS; Copg2; mouse.
DR PRO; PR:Q9QXK3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QXK3; Protein.
DR Bgee; ENSMUSG00000025607; Expressed in spermatocyte and 253 other cell types or tissues.
DR Genevisible; Q9QXK3; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072384; P:organelle transport along microtubule; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR Gene3D; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR032154; Coatomer_g_Cpla.
DR InterPro; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10261; COATOMER SUBUNIT GAMMA; 1.
DR PANTHER; PTHR10261:SF4; COATOMER SUBUNIT GAMMA-2; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF16381; Coatomer_g_Cpla; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..871
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000193863"
FT REPEAT 64..101
FT /note="HEAT 1"
FT REPEAT 283..320
FT /note="HEAT 2"
FT REPEAT 321..355
FT /note="HEAT 3"
FT REPEAT 356..392
FT /note="HEAT 4"
FT REPEAT 395..430
FT /note="HEAT 5"
FT REPEAT 467..504
FT /note="HEAT 6"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
FT VAR_SEQ 247..250
FT /note="HESP -> LQRN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034480"
FT VAR_SEQ 251..871
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034481"
FT VAR_SEQ 377..382
FT /note="VVVVQA -> ALLYPM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034482"
FT VAR_SEQ 383..871
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034483"
FT VAR_SEQ 795
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034484"
SQ SEQUENCE 871 AA; 97681 MW; B3F49178ABDE4A7F CRC64;
MIKKFDKKDE ESGSGSNPFQ HLEKSAVLQE ARIFNETPIN PRRCLHILTK ILYLLNQGEH
FGTMEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMATISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDGTMLQAV ERYMKQAIVD KVSSVASSAL VSSLHMMKIS YDVVKRWINE
AQEAASSDNI MVQYHALGVL YHLRKNDRLA VSKMLNKFTK SGLKSQFAYC MLIRIASRLL
KESEDGHESP LFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCHKY PRKHSVMMTF LSNMLRDDGG FEYKKAIVDC
IISIVEENPE SKEAGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPVPS KYIRFIFNRV
VLENEAVRAA AVSALAKFGA QNESLLPSIL VLLQRCMMDT DDEVRDRATF YLNVLQQRQM
ALNATYIFNG LTVSIPGMEK ALHQYTLEPS EKPFDMKSIP LAMAPVFEQK SEITLVTPKP
EKLAPSRQDI FQEQLAAIPE FMNLGPLFKS SEPVQLTEAE TEYFVRCVKH MFTDHIVFQF
DCTNTLNDQL LEKVTVQMEP SDSYEVLCCI PAPSLPYNQP GICYTLVRLP DEDPTAVAGT
FSCTMKFTVR DCDPNTGVPD EDGYDDEYVL EDLEVTVSDH IQKILKPNFA AAWEEVGDAF
EKEETFALSS TKTLEEAVNN IITFLGMQPC ERSDKVPENK NSHSLYLAGV YRGGYDLLVR
SRLALADGVT MQVTVRSKER TPVDVILASV G
//
