ID   COPG2_ORYSJ             Reviewed;         889 AA.
AC   Q6Z382; B9FW22;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Coatomer subunit gamma-2;
DE   AltName: Full=Gamma-2-coat protein;
DE            Short=Gamma-2-COP;
GN   OrderedLocusNames=Os07g0201100, LOC_Os07g10150;
GN   ORFNames=OsJ_23473 {ECO:0000312|EMBL:EEE66759.1}, P0519E02.25;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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 that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR   EMBL; AP005259; BAC84213.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF21045.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00500.1; -; Genomic_DNA.
DR   EMBL; CM000144; EEE66759.1; -; Genomic_DNA.
DR   EMBL; AK100095; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015647270.1; XM_015791784.1.
DR   AlphaFoldDB; Q6Z382; -.
DR   SMR; Q6Z382; -.
DR   BioGRID; 811702; 1.
DR   STRING; 4530.OS07T0201100-01; -.
DR   PaxDb; Q6Z382; -.
DR   PRIDE; Q6Z382; -.
DR   EnsemblPlants; Os07t0201100-01; Os07t0201100-01; Os07g0201100.
DR   GeneID; 4342665; -.
DR   Gramene; Os07t0201100-01; Os07t0201100-01; Os07g0201100.
DR   KEGG; osa:4342665; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; Q6Z382; -.
DR   OMA; YMTQYHA; -.
DR   OrthoDB; 255234at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   Genevisible; Q6Z382; OS.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   Gene3D; 3.30.310.10; -; 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; PTHR10261; 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; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..889
FT                   /note="Coatomer subunit gamma-2"
FT                   /id="PRO_0000285629"
FT   REPEAT          67..102
FT                   /note="HEAT 1"
FT   REPEAT          103..140
FT                   /note="HEAT 2"
FT   REPEAT          289..326
FT                   /note="HEAT 3"
FT   REPEAT          328..360
FT                   /note="HEAT 4"
FT   REPEAT          361..398
FT                   /note="HEAT 5"
FT   REGION          596..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        761
FT                   /note="E -> K (in Ref. 5; AK100095)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   889 AA;  98554 MW;  5B5FE7A1C4228BF6 CRC64;
     MAQPLVVKKD DDLDEEEYYS PFLGIEKGAV LQEARVFHDP QLDARRCCQV ITKLLYLLNQ
     GDTFTKVEAT EVFFATTKLF QSKDAGLRRM VYLMIKELSP SADEVIIVTS SLMKDMNSKT
     DMYRANAIRV LCRIIDSTLL TQIERYLKQA IVDKNPVVAS AALVSGIYLL QTSPEVVKRW
     SNEVQEAVQS RAALVQFHAL ALLHQIRQND RLAVSKLVTS LTRGSVRSPL AQCLLIRYTS
     QVIRESSMNS QGGDRPFFDF LESCLRNKAE MVILEAARAI TELNGVTSRE LTPAITVLQL
     FLSSSKPVLR FAAVRTLNKV ASTHPLAVTN CNIDMESLIS DQNRSIATLA ITTLLKTGNE
     SSVDRLMKQM TNFMSDIADE FKIVVVEAIR SLCLKFPLKY RSLMNFLSNI LREEGGFEYK
     KAIVDSIIIL IRDIPDAKES GLFHLCEFIE DCEFTYMSTQ ILHFLGNEGP KTSDPSKYIR
     YIYNRVILEN ATVRASAVST LAKFGALVDS LKPRIFVLLR RCLFDGDDEV RDRATLYLKL
     LGGEATVGET EKDVNEFLFG SFDIPLVNLE TSLQNYEPSE APFDISSVSL ETKSQPLAEK
     KTTGKKPTGP ASALSGPVPT VDASYEKLLS SIPEFAGFGK LFKSSAPVEL TEAETEYSVN
     VVKHIYDGHV VLQYNCTNTI PEQLLEEVVV FVDASEADEF SEVATKSLRS LPYDSPGQTF
     VAFEKLEGVL ATGKFSNILK FIVKEVDPST GEADDDGVED EYQLEDLEIT SADYMLKVGV
     SNFRNAWESM DPESERVDEY GLGARESLAE AVSAVIGILG MQPCEGTDVV PSNSRSHTCL
     LSGVFIGNVK VLVRLSFGLS GPKEVAMKLA VRSDDPEISD KIHEIVANG