COPG2_RAT
ID COPG2_RAT Reviewed; 715 AA.
AC D4ABY2;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=Copg2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
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).
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 (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:0000250}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17360540}; Cytoplasmic side
CC {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it (By similarity). Over 60% of the
CC COPG1-containing coatomers are found in the trans-Golgi apparatus and
CC less than 40% in the cis-Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; AABR06030227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06030238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D4ABY2; -.
DR SMR; D4ABY2; -.
DR STRING; 10116.ENSRNOP00000038134; -.
DR iPTMnet; D4ABY2; -.
DR PhosphoSitePlus; D4ABY2; -.
DR jPOST; D4ABY2; -.
DR PaxDb; D4ABY2; -.
DR PeptideAtlas; D4ABY2; -.
DR PRIDE; D4ABY2; -.
DR UCSC; RGD:1566215; rat.
DR RGD; 1566215; Copg2.
DR eggNOG; KOG1078; Eukaryota.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; D4ABY2; -.
DR TreeFam; TF300324; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:D4ABY2; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; D4ABY2; RN.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:RGD.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
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:RGD.
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; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 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; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_sf.
DR PANTHER; PTHR10261; PTHR10261; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF08752; COP-gamma_platf; 1.
DR PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..715
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000425264"
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..391
FT /note="HEAT 4"
FT REPEAT 394..429
FT /note="HEAT 5"
FT REPEAT 466..503
FT /note="HEAT 6"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
SQ SEQUENCE 715 AA; 80489 MW; BB9DC0D22E5C958B CRC64;
MIKKFDKKDE ESGSGSNPFQ HLEKSAVLQE ARIFNETPIN PRRCLHILTK ILYLLNQGEH
FGTMEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMATISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDGTMLQAI ERYMKQAIVD KVSSVSSSAL VSSLHMMKIS YDVVKRWINE
AQEAASSDNI MVQYHALGVL YHLRKNDRLA VSKMLNKFTK SGLKSQFAYC MLIRIASRLL
KESEDGHESP LFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISLCQKYP RKHSVMMTFL SNMLRDDGGF EYKKAIVDCI
ISIVEENPES KEAGLAHLCE FIEDCEHTVL ATKILHLLGK EGPRTPVPSK YIRFIFNRVV
LENEAVRAAA VSALAKFGAQ NESLLPSILV LLQRCMMDTD DEVRDRATFY LNVLQQRQMA
LNATYIFNGL TVSIPGMEKA LHQYTLEPSE KPFDMKSIPL AMAPVFEQKS EITLVTPKPE
KLAPSRQDIF QEQLAAIPEF VNLGPLFKSS EPVQLTEAET EYFVRCVKHM FTDHIVFQFD
CTNTLNDQLL EKVTVQMEPS DSYEVLCCVP APSLPYNQPG ICYTLVRLPD EDPTA
