COPA_SCHPO
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 03-AUG-2022, entry version 153.
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.
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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 PDBsum; 4J87; -.
DR PDBsum; 4J8B; -.
DR PDBsum; 4J8G; -.
DR PDBsum; 7S16; -.
DR PDBsum; 7S22; -.
DR PDBsum; 7S23; -.
DR AlphaFoldDB; Q96WV5; -.
DR SMR; Q96WV5; -.
DR BioGRID; 277920; 10.
DR IntAct; Q96WV5; 7.
DR MINT; Q96WV5; -.
DR STRING; 4896.SPBPJ4664.04.1; -.
DR iPTMnet; Q96WV5; -.
DR MaxQB; Q96WV5; -.
DR PaxDb; Q96WV5; -.
DR PRIDE; Q96WV5; -.
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; ICAEYIV; -.
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; ISO:PomBase.
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; ISO:PomBase.
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; ISO:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
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; 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 3..10
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:4J87"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4J87"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4J87"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:4J87"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4J87"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4J87"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4J87"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:4J87"
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
