ID G1QF36_MYOLU Unreviewed; 726 AA.
AC G1QF36;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN Name=COPG2 {ECO:0000313|Ensembl:ENSMLUP00000022319.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022319.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022319.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000022319.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAPE02016891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02016892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02016893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02016894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QF36; -.
DR STRING; 59463.ENSMLUP00000022319; -.
DR Ensembl; ENSMLUT00000027106.1; ENSMLUP00000022319.1; ENSMLUG00000027742.1.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_1_1; -.
DR InParanoid; G1QF36; -.
DR OMA; IEDCEYN; -.
DR TreeFam; TF300324; -.
DR Proteomes; UP000001074; 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 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; IPR017106; Coatomer_gsu.
DR InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR InterPro; IPR037067; Coatomer_gsu_app_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; 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.
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:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|PIRNR:PIRNR037093}.
FT DOMAIN 23..538
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT DOMAIN 611..713
FT /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT /evidence="ECO:0000259|Pfam:PF08752"
FT REGION 1..21
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"
SQ SEQUENCE 726 AA; 81610 MW; 695F0A82A8ABB641 CRC64;
MLKKFDKKDE ESGSGSNPFR HLEKSTVLQE ARLFNETPIN PRRCLHILTK IIYLLNQGEH
FGTIEATEAF FAMTRLFQSN DQILRRMCYL TIKEMANISE DVIIVTSSLT KDMTGKEDVY
RGPAIRALCR ITDGTLLQAI ERYMKQAIVD RVPSVSSSAL VSSLHLMKIS YDVVKRWVNE
AQEAATSDNI MVQYHALGVL YHLKKNDRLA VSKMLNKFTK SGLKSQFAYC MLIRIASRLL
KESEEGHESP FFDFIESCLR NKHEMVIYEA ASAIIHLPNC TARELAPAVS VLQLFCSSPK
PALRYAAVRT LNKVAMKHPS AVTACNLDLE NLITDSNRSI ATLAITTLLK TGSESSVDRL
MKQISSFVSE ISDEFKVVVV QAISALCQKY PRKHGVMMTF LSNMLRDDGG FEYKRAIVDC
IISIVEENPE AKEAGLAHLC EFIEDCEHTV LATKILHLLG KEGPRTPAPS KYIRFIFNRV
VLENEAVRAA AVSALAKFGA QNENLLPSIL VLLQRCMMDT DDEVRDRATF YLNVLQQKQM
ALNATYIFNG LTVSIPGMEK ALHQYTLEPS EKPFDMKSIP LAMAPAFEQK AEITLVATKS
EKLAPSRQDI FQEQLAAIPE FMNLGPLFKS SEPVQLTEAE TEYFVRCVKH MFTNHIVFQF
DCTNTLNDQL LEKVTVQVEP SDSYEVLCCI PVPSLTYNQP GICYTLVRLP DDDSSAGTNP
QRGRDT
//
