ID A0A2K5CR92_AOTNA Unreviewed; 669 AA.
AC A0A2K5CR92;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=COPI coat complex subunit alpha {ECO:0000313|Ensembl:ENSANAP00000011220.1};
GN Name=COPA {ECO:0000313|Ensembl:ENSANAP00000011220.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000011220.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000011220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 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. {ECO:0000256|ARBA:ARBA00024791}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004347}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR AlphaFoldDB; A0A2K5CR92; -.
DR Ensembl; ENSANAT00000029027.1; ENSANAP00000011220.1; ENSANAG00000023326.1.
DR GeneTree; ENSGT00940000155451; -.
DR Proteomes; UP000233020; 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:InterPro.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR010714; Coatomer_asu_C.
DR InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19876; COATOMER; 1.
DR PANTHER; PTHR19876:SF1; COATOMER SUBUNIT ALPHA; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF06957; COPI_C; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 4: Predicted;
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022892};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 5..39
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 47..88
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 89..130
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 131..165
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 201..242
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 245..286
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 341..439
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 425..669
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
SQ SEQUENCE 669 AA; 76633 MW; F0E3CA05DE3F4D96 CRC64;
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
NWQSRTCVCV LTGHNHYVMC AQFHPSEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD
VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW
EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH
PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG
SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW
VARNRFAVLD RMHSVRLKNG VPAVGLKLND LIQRLQLCYQ LTTVGKFEEA VEKFRSILLS
VPLLVVDNKQ EIAEAQQLIT ICREYIVGLS MEIERKKLPK ETLEQQKRIC EMAAYFTHSN
LQPVHMILVL RTALNLFFKL KNFKTAATFA RRLLELGPKP EVAQQTRKIL SACEKNPTDA
YQLNYDMHNP FDICAASYRP IYRGKPVEKC PLSGACYSPE FKGQICRVTT VTEIGKDVIG
LRISPLQFR
//