ID   COPB2_SCHPO             Reviewed;         796 AA.
AC   O42937;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Probable coatomer subunit beta';
DE   AltName: Full=Beta'-coat protein;
DE            Short=Beta'-COP;
GN   Name=sec27; ORFNames=SPBC16C6.13c, SPBC244.03;
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).
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}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA16920.1; -; Genomic_DNA.
DR   PIR; T39962; T39962.
DR   RefSeq; XP_001713153.1; XM_001713101.2.
DR   AlphaFoldDB; O42937; -.
DR   SMR; O42937; -.
DR   BioGRID; 276588; 3.
DR   STRING; 4896.SPBC16C6.13c.1; -.
DR   iPTMnet; O42937; -.
DR   MaxQB; O42937; -.
DR   PaxDb; O42937; -.
DR   PRIDE; O42937; -.
DR   EnsemblFungi; SPBC16C6.13c.1; SPBC16C6.13c.1:pep; SPBC16C6.13c.
DR   PomBase; SPBC16C6.13c; sec27.
DR   VEuPathDB; FungiDB:SPBC16C6.13c; -.
DR   eggNOG; KOG0276; Eukaryota.
DR   HOGENOM; CLU_005507_1_0_1; -.
DR   InParanoid; O42937; -.
DR   OMA; NVFWNES; -.
DR   PhylomeDB; O42937; -.
DR   Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:O42937; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030126; C:COPI vesicle coat; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; ISO:PomBase.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:PomBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR016453; COPB2.
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; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW   WD repeat.
FT   CHAIN           1..796
FT                   /note="Probable coatomer subunit beta'"
FT                   /id="PRO_0000050917"
FT   REPEAT          4..42
FT                   /note="WD 1"
FT   REPEAT          46..84
FT                   /note="WD 2"
FT   REPEAT          88..126
FT                   /note="WD 3"
FT   REPEAT          131..170
FT                   /note="WD 4"
FT   REPEAT          172..214
FT                   /note="WD 5"
FT   REPEAT          218..256
FT                   /note="WD 6"
SQ   SEQUENCE   796 AA;  89803 MW;  3E4EF829FDD0C2DD CRC64;
     MMRLDFQRKL LSHTERVKAV DFHPTEPWVI ASHYNGQVGI WNYNTQTLVR SFDINDVPIR
     ACAFIARKNW FVCGSDDFQV RVYNYNTGEK VTQFEAHPDY IRALVVHPTQ PFLLTSSDDM
     TIKCFNWDMS WKCVQTFEGH SRYVMSLAIN PKDTNTFASS CLDGTVKVWS FGSSVANFTL
     QAHDRGVNYV NYYPAGDKPY LITAGDDNLI KVWDYQTKAC VRILEGHTNN VSFAFFHSKF
     PIIISGSEDG TVKIWHTLSY SLIKSYNFSL DRAWCIAQNK DNGLVTVGFD NGLITFSLGR
     DEPSVTMDSS GKVVWSNYNE VMSAMIRPAK EQSDLTDGSL ISLSVKELGT TELYPAVLKH
     SPNGRFVSVC GNGEYIVYTA LAWRNKAYGK ALDFAWSADS NVYGSRTSDR SIVIHKNFKE
     SNRLDLSYSC DKIFGGFLLG VVGSDFICFY DWDTGILVRK IDVKPKGVYW NDDGRFVILA
     CDDDFYLLGF NAEMFYSAVE SGTADEEEGV ADSFEALADV SESVVNGKWV AETFIYTTTA
     ARLNYLIGDQ TYKIANVESS FYLLGYIPRD DRIYLTDRDM NVVSYSFNLA IIEYQSLVLK
     GDLEAAQGLL EQISETDRPR LSDFLSRLGY KEAALELSGD SVQRFELALD AQRLDIASQI
     AQELDDPLKW RSLGDAALNA WDFVLAQECF EKGKDYGSLV LLYTATNNHE GLKELSQLTK
     STKINNTAFI CSWLTNQPAE CVNILTSTQR YPEANLFAAT YCPDEVKNVL PEWKVDLTKN
     QKERIADSLG DLELKN