ID COPA_SCHPO Reviewed; 1207 AA. AC Q96WV5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Putative coatomer subunit alpha; DE AltName: Full=Alpha-coat protein; DE Short=Alpha-COP; GN ORFNames=SPBPJ4664.04; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-942, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). 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 -!- INTERACTION: CC Q96WV5; P68978; Xeno; NbExp=2; IntAct=EBI-8503699, EBI-4407041; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral CC membrane protein; Cytoplasmic side. 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; CU329671; CAC38349.1; -; Genomic_DNA. DR RefSeq; NP_595279.1; NM_001021186.2. DR PDB; 4J87; X-ray; 1.67 A; A=1-327. DR PDB; 4J8B; X-ray; 1.88 A; A=1-327. DR PDB; 4J8G; X-ray; 1.90 A; A/B=1-327. DR PDB; 7S16; X-ray; 1.24 A; A=1-327. DR PDB; 7S22; X-ray; 1.75 A; A/B/C=1-327. DR PDB; 7S23; X-ray; 1.49 A; A/B/C=1-327. DR PDB; 8EVL; X-ray; 1.90 A; A/B/C=1-327. DR PDBsum; 4J87; -. DR PDBsum; 4J8B; -. DR PDBsum; 4J8G; -. DR PDBsum; 7S16; -. DR PDBsum; 7S22; -. DR PDBsum; 7S23; -. DR PDBsum; 8EVL; -. DR AlphaFoldDB; Q96WV5; -. DR SMR; Q96WV5; -. DR BioGRID; 277920; 13. DR IntAct; Q96WV5; 7. DR MINT; Q96WV5; -. DR STRING; 284812.Q96WV5; -. DR iPTMnet; Q96WV5; -. DR MaxQB; Q96WV5; -. DR PaxDb; 4896-SPBPJ4664-04-1; -. DR EnsemblFungi; SPBPJ4664.04.1; SPBPJ4664.04.1:pep; SPBPJ4664.04. DR GeneID; 2541412; -. DR KEGG; spo:SPBPJ4664.04; -. DR PomBase; SPBPJ4664.04; -. DR VEuPathDB; FungiDB:SPBPJ4664.04; -. DR eggNOG; KOG0292; Eukaryota. DR HOGENOM; CLU_007565_1_0_1; -. DR InParanoid; Q96WV5; -. DR OMA; EMTYQKQ; -. DR PhylomeDB; Q96WV5; -. DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport. DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR PRO; PR:Q96WV5; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; HDA:PomBase. DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase. 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 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; SSF82171; DPP6 N-terminal domain-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; ER-Golgi transport; Golgi apparatus; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; KW WD repeat. FT CHAIN 1..1207 FT /note="Putative coatomer subunit alpha" FT /id="PRO_0000316543" FT REPEAT 9..50 FT /note="WD 1" FT REPEAT 51..90 FT /note="WD 2" FT REPEAT 93..134 FT /note="WD 3" FT REPEAT 135..174 FT /note="WD 4" FT REPEAT 210..249 FT /note="WD 5" FT REPEAT 254..293 FT /note="WD 6" FT REPEAT 296..336 FT /note="WD 7" FT REPEAT 370..411 FT /note="WD 8" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 942 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT STRAND 2..10 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 21..30 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:7S16" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 63..72 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:7S16" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:7S16" FT TURN 124..127 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 147..156 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:7S16" FT HELIX 167..171 FT /evidence="ECO:0007829|PDB:7S16" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:7S16" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 202..208 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 222..231 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 246..252 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 266..275 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 278..284 FT /evidence="ECO:0007829|PDB:7S16" FT TURN 285..287 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 290..295 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 308..311 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 313..317 FT /evidence="ECO:0007829|PDB:7S16" FT STRAND 320..327 FT /evidence="ECO:0007829|PDB:7S16" SQ SEQUENCE 1207 AA; 136369 MW; 4AB701FD7310BE29 CRC64; MEMLTKFESR SSRAKGVAFH PTQPWILTSL HNGRIQLWDY RMGTLLDRFD GHDGPVRGIA FHPTQPLFVS GGDDYKVNVW NYKSRKLLFS LCGHMDYVRV CTFHHEYPWI LSCSDDQTIR IWNWQSRNCI AILTGHSHYV MCAAFHPSED LIVSASLDQT VRVWDISGLR MKNAAPVSMS LEDQLAQAHN SISNDLFGST DAIVKFVLEG HDRGVNWCAF HPTLPLILSA GDDRLVKLWR MTASKAWEVD TCRGHFNNVS CCLFHPHQEL ILSASEDKTI RVWDLNRRTA VQTFRRDNDR FWFITVHPKL NLFAAAHDSG VMVFKLERER PAHALNINTL LYVNKEKSIV SYDLLRAQST TVASVKHLGS AWLPPRSLSY NPAEKVALLT SSADNGVYEL VNVSSRSNSL PLKDNIKGPG DDAIFVARNR FAVFSRSDQT IEIKDLSNKV TKTIQLPEKT RDIFFAGMGH VLLSTATQVH LFDLQQKKIV SSFNANRVKY VVWSNDNSQA ALLGKHYVYI VKKNLELITS IHETIRIKSA VWVENNVLLY ATLDHLKYAL MSGDTGVIKT LESTLYLVKA KGNMVFALNR AAEPVSFEID PTEYLFKLAL LRKDYEQVLH LIQNSNLVGQ AIIAYLQKKG YPEIALQFVE DPSTRFELAL ECGNLETALE LARTIDRPEV WSRLASDAMS YGNHKIAEIT FQKLRYFEKL SFLYLITGNA EKLQKMAIIA EKRNDTLSLF QNSLYLNEVE SRINILEQAG MYPIAYLTAK SNGLEEKAQQ ILSHCNKTEE EIKLPSLGSA FTTPVPVNET YTHNWPLLDT SHSTFEKSLQ ERMEQLAIER QEEQESEEEY EEVEQSLMDV VDEMSDLAES VPEEEVDGWE VEDLAPEEAV NDVVDDASAF VGADEIFLWK RNSPLAADHI AAGDFESAMK ILNKQVGAIN FSPLKTRFLE IYTASRVYLP TISGLDPLVS YVRRNAETAE RSQALPFITR NLASIKSHEL HEAYRLVKAN KILEAQICFR SIIYLALTTV ANSEEEADEI SALIDECCRY IVALSCELER RRLGEEDTKR ALELSYYFAS ADLQPMHSII ALRLAINASH KLKNYKSASF LGNKLLQLAE SGPAAEAANR AITLGDRNPH DAFEIEYDPH VEMRICPKTL TPVYSGDDFD VCSVCGAVYH KGYVNEVCTV CDVGGIGQKG TGRRFFA //