COB21_ARATH
ID COB21_ARATH Reviewed; 920 AA.
AC Q9CAA0; F4HQE6; Q9SSD5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Coatomer subunit beta'-1;
DE AltName: Full=Beta'-coat protein 1;
DE Short=Beta'-COP 1;
GN OrderedLocusNames=At1g79990; ORFNames=F18B13.7, F19K16.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CAA0-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52258.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009322; AAD55465.1; -; Genomic_DNA.
DR EMBL; AC011717; AAG52258.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36339.2; -; Genomic_DNA.
DR EMBL; AY090955; AAM14001.1; -; mRNA.
DR PIR; C96831; C96831.
DR RefSeq; NP_001154478.1; NM_001161006.2. [Q9CAA0-1]
DR AlphaFoldDB; Q9CAA0; -.
DR SMR; Q9CAA0; -.
DR BioGRID; 29557; 11.
DR STRING; 3702.AT1G79990.1; -.
DR iPTMnet; Q9CAA0; -.
DR PaxDb; Q9CAA0; -.
DR ProteomicsDB; 241005; -. [Q9CAA0-1]
DR EnsemblPlants; AT1G79990.1; AT1G79990.1; AT1G79990. [Q9CAA0-1]
DR GeneID; 844339; -.
DR Gramene; AT1G79990.1; AT1G79990.1; AT1G79990. [Q9CAA0-1]
DR KEGG; ath:AT1G79990; -.
DR Araport; AT1G79990; -.
DR TAIR; locus:2016214; AT1G79990.
DR eggNOG; KOG0276; Eukaryota.
DR eggNOG; KOG4697; Eukaryota.
DR HOGENOM; CLU_005507_0_0_1; -.
DR PhylomeDB; Q9CAA0; -.
DR PRO; PR:Q9CAA0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAA0; baseline and differential.
DR Genevisible; Q9CAA0; AT.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..920
FT /note="Coatomer subunit beta'-1"
FT /id="PRO_0000285604"
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 350..392
FT /note="WD 7"
FT REPEAT 460..500
FT /note="WD 8"
FT REGION 850..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..876
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 103969 MW; 884892BAE643CC52 CRC64;
MPLRLEIKRK FAQRSERVKS VDLHPTEPWI LASLYSGTLC IWNYQTQTMV KSFDVTELPV
RSAKFIARKQ WVVAGADDMF IRVYNYNTMD KIKVFEAHAD YIRCVAVHPT LPYVLSSSDD
MLIKLWDWEK GWLCTQIFEG HSHYVMQVTF NPKDTNTFAS ASLDRTIKIW NLGSPDPNFT
LDAHLKGVNC VDYFTGGDKP YLITGSDDHT AKVWDYQTKS CVQTLEGHTH NVSAVSFHPE
LPIIITGSED GTVRIWHATT YRLENTLNYG LERVWAIGHI KGSRRVVIGY DEGSIMVKLG
REIPVASMDN SGKIIWAKHN EIHTVNIKSV GADEVTDGER LPLAVKELGT CDLYPQSLKH
NPNGRFVVVC GDGEYIIYTA LAWRNRSFGS ALEFVWSSDG EHAVRESSTK IKIFSKNFQE
KKTVRPTFSA EHIFGGTLLT MCSSDFICFY DWAECRLIRR IDVTVKNLYW ADSGDLVAIA
SDTSFYILKF NRDIVSSYFD GGKQIDEEGI EDAFELLNET NERVRTGLWV GDCFIYTNSS
WRLNYCVGGE VTTMYHLDRP MYLLGYLANQ SRVYLIDKEF NVIGYTLLLS LIEYKTLVMR
GDLEQANEVL PSIPKEHHNS VAHFLESRGM TEDALEVATD PDYRFELAIQ LGRLAVAKDI
AVEAQNESKW KQLGELAMSS GKLDMAEECM RHAMDLSGLL LLYSSLGDAD GMMKLAALAK
EQGKNNVAFL CLFMLGQVED CLHLLVESNR IPEAALMARS YLPSKVSEIV ALWRNDLTKI
SPKAAESLAD PEEYPNLFEE WQVALSLENR AAETRGVHPP AGDYCSHADR DHTTLVDAFR
IMQIEEEGRL EQGDVLDEVG EEGEDGEEEE EEDRQEESSD GRQQNVEEEA VVVDADSTDG
AVLVNGNESE EQWVLTPPQE
