COB21_ORYSJ
ID COB21_ORYSJ Reviewed; 907 AA.
AC Q5VQ78; A0A0P0WSR8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Coatomer subunit beta'-1;
DE AltName: Full=Beta'-coat protein 1;
DE Short=Beta'-COP 1;
GN OrderedLocusNames=Os06g0143900, LOC_Os06g05180; ORFNames=OSJNBa0007O20.8-1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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; AP003487; BAD68397.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18693.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96117.1; -; Genomic_DNA.
DR EMBL; AK111584; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015643763.1; XM_015788277.1.
DR AlphaFoldDB; Q5VQ78; -.
DR SMR; Q5VQ78; -.
DR STRING; 4530.OS06T0143900-01; -.
DR PaxDb; Q5VQ78; -.
DR PRIDE; Q5VQ78; -.
DR EnsemblPlants; Os06t0143900-01; Os06t0143900-01; Os06g0143900.
DR GeneID; 4340097; -.
DR Gramene; Os06t0143900-01; Os06t0143900-01; Os06g0143900.
DR KEGG; osa:4340097; -.
DR eggNOG; KOG0276; Eukaryota.
DR HOGENOM; CLU_005507_0_0_1; -.
DR InParanoid; Q5VQ78; -.
DR OMA; NTMERTK; -.
DR OrthoDB; 139008at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q5VQ78; baseline and differential.
DR Genevisible; Q5VQ78; OS.
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; -; 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; 4.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..907
FT /note="Coatomer subunit beta'-1"
FT /id="PRO_0000285607"
FT REPEAT 13..52
FT /note="WD 1"
FT REPEAT 55..94
FT /note="WD 2"
FT REPEAT 97..136
FT /note="WD 3"
FT REPEAT 140..180
FT /note="WD 4"
FT REPEAT 183..224
FT /note="WD 5"
FT REPEAT 227..266
FT /note="WD 6"
FT REPEAT 269..309
FT /note="WD 7"
FT REPEAT 351..389
FT /note="WD 8"
FT REPEAT 461..501
FT /note="WD 9"
FT REGION 850..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 542
FT /note="W -> R (in Ref. 4; AK111584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 102890 MW; A079EF9E899F3FA2 CRC64;
MPLRLEIKRK FAQRSERVKS VDLHPTEPWI LSSLYSGSVC IWDYQSQTMV KSFEVSELPV
RSAKFISRKQ WVVAGADDMF IRVYNYNTMD KVKVFEAHTD YIRCVAVHPT LPYVLSSSDD
MLIKLWDWDK GWMCTQIFEG HSHYVMQVTF NPKDTNTFAS ASLDRTTKIW SLGSPDPNFT
LDGHQKGVNC VDYFTGGDRP YLITGSDDST AKVWDYQTKS CVQTLEGHTH NISAVCFHPE
LPIIITGSED GTVRIWHSTT YRLENTLNYG LERVWAVGYM KGSRRMVIGY DEGTIMIKMG
REVPVASMDT SGKIIWAKHN EIQTVNIKTV GAGFEVTDGE RLPLAVKELG SCDLYPQSLK
HNPNGRFVVV CGDGEFIIYT ALAWRNRSFG SALEFVWSSE GEYAIRESTS RIKIFSKSFQ
EKKTIRPTFS AERIFGGILL AMCSSDFICF YDWADCRLIR RIDVNVKNLY WADSGDLVAI
ASDTSFYILK YNRDVVASYL ESGKPVDEEG VEDAFELLHE VNERVRTGIW VGDCFIYNNS
SWRLNYCVGG EVTTMYHLDR PMYLLGYLAN QSRVYLIDKE FNVMGYTLLL SLIEYKTLVM
RGDIERANDI LPSIPKAQYN NVAHFLESRG MLEEALEIAT DADYRFDLAV QLGKLEVAKA
IAMEAQSESK WKQLGELAMS TGKLDMAEEC LVQAKDLSGL LLLYSSLGDA EGIEKLASQA
KEHGKNNVAF LCLFMLGKLE DCIQLLIDSN RIPEAALMAR SYLPSKVSEI VAIWRNDLSK
VNPKAAESLA DPSEYPNLFE DWQVALTVEK NVASRRVHYP PADEYLNHAE KSDMTLVEAF
KRMQVIEDEE TEDALDENGE PDEEVLEENK VEESTDEAVE VDADEPEETV LVNGKEGEEQ
WVLTEHE
