COPG2_TAKRU
ID COPG2_TAKRU Reviewed; 873 AA.
AC Q9I8E6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=copg2;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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; AJ251323; CAB96534.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9I8E6; -.
DR SMR; Q9I8E6; -.
DR STRING; 31033.ENSTRUP00000040385; -.
DR eggNOG; KOG1078; Eukaryota.
DR InParanoid; Q9I8E6; -.
DR Proteomes; UP000005226; Unplaced.
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 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..873
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000342520"
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 394..430
FT /note="HEAT 5"
FT REPEAT 467..504
FT /note="HEAT 6"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97470 MW; 31154D8BFF3AF440 CRC64;
MIKKFDKKDE ESGSGSNPFQ NLEKSAVLQE ARIFNETPIN PRRCLHILTK IIYLLNQGEH
FGTTEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMANISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDTTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHMVKMS YDVVKRWVNE
AQEAASSDNI MVQYHALGLL YHLRKNDRLA VTKMLNKFTK SGLKSPFAYC MLIRIASKLL
DETEAGHDSP LFDFIESCLR NKNEMVVYEA ASAIVHMPNC TARELAPAVS VLQLFCSSPK
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCQKY PRKHSAMMNF LSNMLRDDGG FEYKRAIVDC
IISIIEENPE SKETGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPQPS KYIRFIFNRV
VLESEAVRAA AVSALAKFGA QNDDLLPSVL VLMQRCMMDS DDEVRDRATF YMNVLQQKQK
ALNAAYIFNG LSVSIPGLEK SLHQYTLEPS EKPFDMKSVP LATTPITEQK TEIAPAATSK
LPEKLAPSRQ DIYQEQLAAI PEFQGLGPLF KSSDPVQLTE AETEYVVRCI KHTFARHMVF
QFDCTNTLND QLLQKVLVQM EPSEAYEVIH YIPAPSLPYS QPGSCYSLVR LPDDDPTAVS
CTFSCTMKYL VRDCDPNTGE PDDDGYDDEY VLEDLEVTVP DHIQKVLKPN FGAAWEEVGD
EFEKEETFAL ASVRTLDEAV GNIISFLGMQ PCERSDKVPE NKNSHVLFLA GVFRGGHDVL
VRARLALADG VTMQVTVRSS EETVVDVILA SVG