COPG2_XENLA
ID COPG2_XENLA Reviewed; 872 AA.
AC Q6DKD7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=copg2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. {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}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; BC074209; AAH74209.1; -; mRNA.
DR RefSeq; NP_001086117.1; NM_001092648.1.
DR AlphaFoldDB; Q6DKD7; -.
DR SMR; Q6DKD7; -.
DR BioGRID; 102709; 2.
DR IntAct; Q6DKD7; 1.
DR DNASU; 444546; -.
DR GeneID; 444546; -.
DR KEGG; xla:444546; -.
DR CTD; 444546; -.
DR Xenbase; XB-GENE-941269; copg2.S.
DR OrthoDB; 255234at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 444546; Expressed in testis and 19 other tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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..872
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000342521"
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"
SQ SEQUENCE 872 AA; 97792 MW; 239C24E6973F784A CRC64;
MIKKFDKKDE ESGIGSNPFQ HLEKSAVLQE ARLFNETPIN PRRCLHILTK ILYLLNQGEH
FGTMEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMANISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDATMLQGI ERYMKQAIVD KIPSVSSSAL VSSLNMTKIS YDVVKRWINE
AQEAASSDNI MVQYHALGLL YNLKKNDRLA VSKMLNKYTK SGVKSPFAYC MLIRIASRLL
EESEEGHNSP LFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISTFVSE ISDEFKVVVV QAISALCQKY PRKHSVMMTF LSNMLRDDGG FEYKRAIVDC
IISIIEENPD SKESGLAHMC EFIEDCEHTV LATKILHLLG KEGPKTPTPS KYIRFIFNRV
VLENEAVRAA AVSALAKFGA QNESLLPSVL VLLQRCMMDS DDEVRDRATF YFNVLKQQQL
ALNAAYIFNG LTVSVFGMEK ALHQYTLEPS EKPFDMKTVP LATVPFMDQK TDLAPMATKQ
PEKAVPVRQD IFQEQLAVIP EFKNLGPLFK SSEPVQLTEA ETEYFVRCIK HVFPNHFVFQ
FDCTNTLNDQ LLEKVTVQME PSEAYEVLHY VPAPSLTYNQ PGICYTLVSL PDDDPTAVSC
TFSCTMKFVV RDCDPQTGVP DDEGYSDEYV LEDLELSLSD HIQKVLKPNF GASWEEVGDA
YEKEETFALT TTKTLEEAVN NIIKFLGMQP CERSDKVPEN KNSHVLYLSG VFRGGHDALV
RSRLALADGV TMQVTVRSQD ETPADVILAS VG