ID   COPA_DICDI              Reviewed;        1221 AA.
AC   Q55FR9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Coatomer subunit alpha;
DE   AltName: Full=Alpha-coat protein;
DE            Short=Alpha-COP;
GN   Name=copa; ORFNames=DDB_G0267982;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
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DR   EMBL; AAFI02000003; EAL73444.1; -; Genomic_DNA.
DR   RefSeq; XP_647464.1; XM_642372.1.
DR   AlphaFoldDB; Q55FR9; -.
DR   SMR; Q55FR9; -.
DR   STRING; 44689.DDB0233797; -.
DR   PaxDb; Q55FR9; -.
DR   EnsemblProtists; EAL73444; EAL73444; DDB_G0267982.
DR   GeneID; 8616271; -.
DR   KEGG; ddi:DDB_G0267982; -.
DR   dictyBase; DDB_G0267982; copA.
DR   eggNOG; KOG0292; Eukaryota.
DR   HOGENOM; CLU_007565_1_0_1; -.
DR   InParanoid; Q55FR9; -.
DR   OMA; ICAEYIV; -.
DR   PhylomeDB; Q55FR9; -.
DR   Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q55FR9; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
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; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; ER-Golgi transport; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1221
FT                   /note="Coatomer subunit alpha"
FT                   /id="PRO_0000327495"
FT   REPEAT          7..46
FT                   /note="WD 1"
FT   REPEAT          49..88
FT                   /note="WD 2"
FT   REPEAT          91..130
FT                   /note="WD 3"
FT   REPEAT          133..172
FT                   /note="WD 4"
FT   REPEAT          202..241
FT                   /note="WD 5"
FT   REPEAT          243..282
FT                   /note="WD 6"
FT   REPEAT          285..323
FT                   /note="WD 7"
FT   REPEAT          358..399
FT                   /note="WD 8"
FT   REPEAT          528..567
FT                   /note="WD 9"
FT   REPEAT          910..953
FT                   /note="WD 10"
FT   REGION          820..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1221 AA;  138855 MW;  B969E4E9E32F0A66 CRC64;
     MLYKFETKAS RVKGLSFHPT RPWILASLHS GSIHLYDYRI KTLLEKFDEH EGPVRGINFH
     MTQPLFVSGG DDYKIKVWNY KQRRCLFTLK GHKDYIRSVE FHREAPWIVS SSDDMVIRIW
     NWQSRTCIAE LNGHNHYVMS ALFHPKDDLV VSASLDQTIR IWDISGLKKK MTTVKPYREN
     DPMRLQDELF GTDISVRLSL EGHDRGVNWA SFHPTQPYIV SASDDHQVKL WRMNDPIVDT
     FRGHYNNVSC ALFHPRQDLI ISNSEDKTIR VWDIIKKSTV HMIRRDHDRF WTLASHPNQN
     LFAAGHDSGM IVFKLERERP LFVQNGDSGV FFLKKKNFNS FDFQAGRTVS LFHISKLPSN
     NGTQTMSYNQ TERAILVSSD AEGGSYHLYK IPPKDSNTVN TKKGTGVAAI FVGRDRFAVL
     DKGNNVVIRD LENEEIKRCQ IPFTIDWIYP SGSPGTILIQ SEDKIHMFDI QQKKMLCEIQ
     VHGVRYVIWS KDRNYVAFLT RDFIVLANKK LEQICMIHET VLPKSGVWDD NGVFIYSTSN
     HLKYLLQNGD NGTIRTLEST IYITGVKNNK VFAIDREFKN RIIEIDTTEY VLKLSLLQQN
     YNQVMTILRE NRLVGKAIIA YLQKKGYPDV VHFVKDDRTR FNLALDAGNI DIALSSAKIL
     DDKDCWNRLG VEALKQGNYQ VVEMAYSRTS EFDRLSFLYL LVGNLSTLKK MISYESSDIM
     SRFHFSLYLG DVEERIKILQ EAGLHQLAYI TASIHGLTEK AESIGNLITS DGKSQLPQLP
     KQSYLLVPPS PINCNPNELN WPLLTTTKSV SDVMGENRFG VEQSTSTPTG DWESDEDIFS
     EGKSQQQSSQ QQQQQQQKGD WEEDILIGDG NNGGGDDGGW ERDDLKGLEK IGTDGFNNKQ
     NDHVALFVPP QPGPSFSMIW ARNSQFAVDH IAAGSFESAM NILNSQIGAV NFDPIKSMFM
     NIFMATRSSL GCNASTPSLL MPIQRKSAAP YITYGLGHLI ERLKTNAYKS TTEGKFNDAL
     SHFTYILHTI IFCSVDNKQE VNELKDLINI CREYILGIKI ELQRKELSIG AQKDSTLGRQ
     AELAAYFTHC NLDPSHLILS LRSAMNCAYK VKHFNLAASF ARRLISLNPN PDLATQAKKV
     FNFAQQTPTP SDIQQLNYDE RNPFVICAHS YVPIYKGSPL IKCPYCSSCY LPTHKGKVCS
     VCQISEIGKD VQGLQVITIQ K