COPG2_BOVIN
ID COPG2_BOVIN Reviewed; 871 AA.
AC A2VE21;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Coatomer subunit gamma-2;
DE AltName: Full=Gamma-2-coat protein;
DE Short=Gamma-2-COP;
GN Name=COPG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) 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 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:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC 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 -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR EMBL; BC133529; AAI33530.1; -; mRNA.
DR RefSeq; NP_001075917.1; NM_001082448.1.
DR AlphaFoldDB; A2VE21; -.
DR SMR; A2VE21; -.
DR STRING; 9913.ENSBTAP00000022911; -.
DR PaxDb; A2VE21; -.
DR PeptideAtlas; A2VE21; -.
DR PRIDE; A2VE21; -.
DR Ensembl; ENSBTAT00000022911; ENSBTAP00000022911; ENSBTAG00000017245.
DR GeneID; 536616; -.
DR KEGG; bta:536616; -.
DR CTD; 26958; -.
DR VEuPathDB; HostDB:ENSBTAG00000017245; -.
DR VGNC; VGNC:27597; COPG2.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; A2VE21; -.
DR OMA; YMTQYHA; -.
DR OrthoDB; 255234at2759; -.
DR TreeFam; TF300324; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000017245; Expressed in spermatocyte and 110 other tissues.
DR ExpressionAtlas; A2VE21; baseline and differential.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
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: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 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; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..871
FT /note="Coatomer subunit gamma-2"
FT /id="PRO_0000342518"
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 COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y678"
SQ SEQUENCE 871 AA; 97565 MW; 23A92A6519916DA6 CRC64;
MIKKFDKKDE ESGSGSNPFR HLEKSAVLQE ARIFNETPIN PRRCLHILTK ILYLLNQGEH
FGTTEATEAF FAMTRLFQSN DQTLRRMCYL TIKEMATISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDGTMLQAI ERYMKQAIVD KVSSVSSSAL VSSLHMMKIS YDVVKRWVNE
AQEAASSDNI MVQYHALGVL YHLKKNDRLA VSKMLNKFTK SGLKSQFAYC MLIRIASRLL
KENEEGHESP VFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCQKY PRKHSVMMTF LSNMLRDDGG FEYKRAIVDC
IIHIVEENPE SKEAGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPVPS KYIRFIFNRV
VLENEAVRAA AVSALAKFGA QNENLLPSIL VLLQRCMMDT DDEVRDRATF YLNVLQQRQM
ALNATYIFNG LTVSVPGMEK ALHQYTLEPS EKPFDMKSIP LATAPVFEQK AEITLVSTKP
EKLAPSRQDI FQEQLAAIPE FMNLGPLFKS SEPVQLTEAE TEYFVRCVKH MFTNHIVFQF
DCTNTLNDQL LEKVTVQVEP SEAYEVLCCV PAPSLPYNQP GVCYTLVRLP EDDSIAAAGT
FSCTMKFTVR DCDPDTGVPT EEGYDDEYVL EDLEVTVSDH IQKVMKPNFA AAWEEVGNTF
EKEETFALSS TKTLEEAVNN IITFLGMQPC ERSDKVPENK NSHSLYLAGV YRGGYDLLVR
SRLALADGVT MQVTVRSKEG TPVDVILASV G
