ID G3W0Y6_SARHA Unreviewed; 890 AA.
AC G3W0Y6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=COPG2 {ECO:0000313|Ensembl:ENSSHAP00000009091.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000009091.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000009091.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000009091.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|PIRNR:PIRNR037093}.
CC -!- SUBUNIT: Oligomeric complex. {ECO:0000256|PIRNR:PIRNR037093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037093}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR037093};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR037093}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane
CC protein {ECO:0000256|PIRNR:PIRNR037093}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR037093}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the COPG family. {ECO:0000256|ARBA:ARBA00010720,
CC ECO:0000256|PIRNR:PIRNR037093}.
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DR AlphaFoldDB; G3W0Y6; -.
DR STRING; 9305.ENSSHAP00000009091; -.
DR Ensembl; ENSSHAT00000009168.2; ENSSHAP00000009091.2; ENSSHAG00000007876.2.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; G3W0Y6; -.
DR TreeFam; TF300324; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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; COATOMER SUBUNIT GAMMA; 1.
DR PANTHER; PTHR10261:SF4; COATOMER SUBUNIT GAMMA-2; 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; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037093};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR037093};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037093};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037093};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 43..557
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 630..775
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT DOMAIN 777..889
FT /note="Coatomer subunit gamma C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16381"
SQ SEQUENCE 890 AA; 99531 MW; D61DFD2C4232EF5C CRC64;
MLPLRCPSPP FPSCPGGWWR RGGGAMAGGG RSSGSNPFQH LEKSAVLQEA RIFNETPINP
RRCLHILTKI LYLLNQGEHF GTTEATEAFF AMTRLFQSND QTLRRMCYLT IKEMANISED
VIIVTSSLTK DMTGKEDVYR GPAIRALCRI TDGTMLQAIE RYMKQAIVDK VPSVSSSALV
SSLHMMKISY DVVKRWINEA QEAASSDNIM VQYHALGVLY HLRKNDRLAV SKMLNKFTKS
GLKSQFAYCM LIRIASRLLK ETEESHESPL FDFIESCLRN KHEMVIYEAA SAIIHLPNCT
ARELAPAVSV LQLFCSSPKP ALRYAAVRTL NKVAMKHPSA VTACNLDLEN LITDSNRSIA
TLAITTLLKT GSESSVDRLM KQISSFVSEI SDEFKVVVVQ AISALCQKYP RKHSVMMTFL
SNMLRDDGGF KYKRAIVDCI INIVEENPES KESGLAHLCE FIEDCEHTVL ATKILHLLGK
EGPRTPVPSK YIRFIFNRVV LENEAVRAAA VSALAKFGAQ NENLLPSILV LLQRCMMDTD
DEVRDRATFY LNVLQQKQMA LNAAYIFNGL TVSIPGMEKA LHQYTLSPSE KPFDLKSVPL
ATAPVFEQKA EITLVANKPE KLAPSRQDIF QEQLAAIPEF KNLGPLFKSS EPVQLTEAET
EYFVRCVKHM FNNHIVFQFD CTNTLNDQFL EKVTVQMEPS DAYDVLCCIP APSLTYNQPG
ICYTLVRLPD DDPTAVACTF SCTMKFTVRD CDPNTGIPDE DGYDDEYVLE DLEVSMSDHI
QKVLKPNFAV AWEEVGDNFE KEETFALSTT KTLEEAVNNI VTFLGMQPCE RSDKVPENKN
SHTLYLSGVY RGGYDLLVRS RLALGDGVTM QVTVRSKEET PVDVILASVG
//
