COPB_SCHPO
ID COPB_SCHPO Reviewed; 940 AA.
AC Q9UUF7; O74812;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=sec26; ORFNames=SPBC146.14c, SPBC337.01c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000269|PubMed:16823372}. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is
CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as
CC well as on the vesicles/buds originating from it. {ECO:0000250}.
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DR EMBL; CU329671; CAB46767.1; -; Genomic_DNA.
DR PIR; T39428; T39428.
DR RefSeq; NP_595403.1; NM_001021310.2.
DR AlphaFoldDB; Q9UUF7; -.
DR SMR; Q9UUF7; -.
DR BioGRID; 276348; 6.
DR STRING; 4896.SPBC146.14c.1; -.
DR iPTMnet; Q9UUF7; -.
DR MaxQB; Q9UUF7; -.
DR PaxDb; Q9UUF7; -.
DR PRIDE; Q9UUF7; -.
DR EnsemblFungi; SPBC146.14c.1; SPBC146.14c.1:pep; SPBC146.14c.
DR GeneID; 2539798; -.
DR KEGG; spo:SPBC146.14c; -.
DR PomBase; SPBC146.14c; sec26.
DR VEuPathDB; FungiDB:SPBC146.14c; -.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q9UUF7; -.
DR OMA; QCGFMAA; -.
DR PhylomeDB; Q9UUF7; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9UUF7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:PomBase.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IC:PomBase.
DR GO; GO:0005829; C:cytosol; 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; ISS:PomBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR011710; Coatomer_bsu_C.
DR InterPro; IPR016460; COPB1.
DR InterPro; IPR029446; COPB1_appendage_platform_dom.
DR PANTHER; PTHR10635; PTHR10635; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF07718; Coatamer_beta_C; 1.
DR Pfam; PF14806; Coatomer_b_Cpla; 1.
DR PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..940
FT /note="Coatomer subunit beta"
FT /id="PRO_0000193838"
FT REPEAT 11..48
FT /note="HEAT 1"
FT REPEAT 90..125
FT /note="HEAT 2"
FT REPEAT 126..162
FT /note="HEAT 3"
FT REPEAT 310..347
FT /note="HEAT 4"
SQ SEQUENCE 940 AA; 104700 MW; CC1635162B2C2695 CRC64;
MSCWTLVQQD FLEAPSVDAL KTSLESKNDY VKISAMKTIL RVVINGDSLP SILMHVIRFV
MPSRNKELKK LLYYYWEVCP KYNNDGTMKQ EMILACNSFR NDLQHPNEFI RGATLRFLCK
LKEPELLDPL IPTVRQCLEH RHAYVRKNAI LAVFSIYQVS NHLIPDAASL AEDFLAAESE
GTCKRNALIV LFTIDPEKAK AWLLANFEQI PSLNASSLLV IIEFIRKVVL TKADGLEKLR
FQSLLVSLTA TNNSSVVFEA ATSVINVFPD AESLKLAASR LLALADREAD NNAKLIMLDR
ISQLAARDKS ILEDLITDVI PFLSSSDFDV CEKAISIIMG LVSSRNVEDI LNHFQKELTK
SNGETEKDDG RRRALTKAIH SCAINFPHTA ATAIQYLLSH ISDFQSKSAS SVLSFIKEVM
EKFPDLRSSN ITKLLLSLKE LRAGKIFRGV IWIAGEYCLT EDDIRVAWKS IRASLGEVPI
LASEEQLLKD VSNVPEDDLL IDISAPASTS RKVLPDGTYA TESAVTSEAL SAARLEAVKA
SKKPPLRTQI LSGDYYLAAV LASALTKLVM RFARLSFDKE RLNALKAEAC LIMTSIIRVG
QSKFVKYTID DDSVERIMNC IRAIYSFEEL PEFQTVFLDD MRKAFSSLVA QSDKRQKEAD
LLVNGSDAVQ ADELLNIRQF QRVIEEKQDL NFESDIIQAT NDGMVVEDLA SKLDHIVQLA
GFTDPVYCEA YVKIQQFDII LDILLVNRTD TTLQNLSVDL ATLGDLKVVE RPPPMNLGPH
AFKSVQATVK VSSTESAVIF GNIVYGGKAS DEDKIVVLNG IPVNIIDYIK PAFIPESQFR
SMWTEFEWEN KVDISSNEDI SLYDFLHKIM KKTNMNCLTP DASLRGDCGF LSANLYACSI
FGEDALMSLS VEKSVSGPIS GHVRIRSKTQ GIALSLGAFV
