ID H2Q0E3_PANTR Unreviewed; 1233 AA.
AC H2Q0E3; A0A2J8JAE7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN Name=COPA {ECO:0000313|Ensembl:ENSPTRP00000002599.5,
GN ECO:0000313|VGNC:VGNC:5021};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000002599.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000002599.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000002599.5}
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 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 -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|PIRNR:PIRNR003354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003354}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR003354}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. 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 EMBL; AACZ04025375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001171563.1; XM_001171563.4.
DR AlphaFoldDB; H2Q0E3; -.
DR STRING; 9598.ENSPTRP00000002599; -.
DR PaxDb; 9598-ENSPTRP00000002599; -.
DR Ensembl; ENSPTRT00000002831.6; ENSPTRP00000002599.5; ENSPTRG00000001549.6.
DR GeneID; 469552; -.
DR KEGG; ptr:469552; -.
DR CTD; 1314; -.
DR VGNC; VGNC:5021; COPA.
DR eggNOG; KOG0292; Eukaryota.
DR GeneTree; ENSGT00940000155451; -.
DR HOGENOM; CLU_007565_1_0_1; -.
DR InParanoid; H2Q0E3; -.
DR OMA; EMTYQKQ; -.
DR OrthoDB; 20819at2759; -.
DR TreeFam; TF105693; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001549; Expressed in pituitary gland and 21 other cell types or tissues.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; 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: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; IBA:GO_Central.
DR GO; GO:0030157; P:pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR CDD; cd22948; Coatomer_WDAD_alpha; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR047312; Coatomer_alpha_WD-assoc_reg.
DR InterPro; IPR016391; Coatomer_asu.
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 PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR003354};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003354};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR003354};
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..775
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 824..1233
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
SQ SEQUENCE 1233 AA; 139326 MW; 2BD39E6E406B29C0 CRC64;
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
NWQSRTCVCV LTGHNHYVMC AQFHPAEDLV 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 RMHSLLIKNL KNEITKKVQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK
RTLASVKISK VKYVIWSADM SHVALLAKHE HSCPLPLTAI VICNRKLDAL CNIHENIRVK
SGAWDESGVF IYTTSNHIKY AVTTGDHGII RTLDLPIYVT RVKGNNVYCL DRECRPRVLT
IDPTEFKFKL ALINRKYDEV LHMVRNAKLV GQSIIAYLQK KGYPEVALHF VKDEKTRFSL
ALECGNIEIA LEAAKALDDK NCWEKLGEVA LLQGNHQIVE MCYQRTKNFD KLSFLYLITG
NLEKLRKMMK IAEIRKDMSG HYQNALYLGD VSERVRILKN CGQKSLAYLT AATHGLDEEA
ESLKETFDPE KETIPDIDPN AKLLQPPAPI MPLDTNWPLL TVSKGFFEGT IASKGKGGAL
AADIDIDTVG TEGWGEDAEL QLDEDGFVEA TEGLGDDALG KGQEEGGGWD VEEDLELPPE
LDISPGAAGG AEDGFFVPPT KGTSPTQIWC NNSQLPVDHI LAGSFETAMR LLHDQVGVIQ
FGPYKQLFLQ TYARGRTTYQ ALPCLPSMYG YPNRNWKDAG LKNGVPAVGL KLNDLIQRLQ
LCYQLTTVGK FEEAVEKFRS ILLSVPLLVV DNKQEIAEAQ QLITICREYI VGLSMETERK
KLPKETLEQQ KRICEMAAYF THSNLQPVHM ILVLRTALNL FFKLKNFKTA ATFARRLLEL
GPKPEVAQQT RKILSACEKN PTDAYQLNYD MHNPFDICAA SYRPIYRGKP VEKCPLSGAC
YSPEFKGQIC RVTTVTEIGK DVIGLRISPL QFR
//
