COB22_ARATH
ID COB22_ARATH Reviewed; 926 AA.
AC Q9C827; Q8GX79;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Coatomer subunit beta'-2;
DE AltName: Full=Beta'-coat protein 2;
DE Short=Beta'-COP 2;
GN OrderedLocusNames=At1g52360; ORFNames=F19K6.16;
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] OF 337-926.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-926.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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=Q9C827-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC037424; AAG51545.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32792.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60541.1; -; Genomic_DNA.
DR EMBL; AK118389; BAC42999.1; ALT_INIT; mRNA.
DR EMBL; BT006480; AAP21288.1; -; mRNA.
DR PIR; G96563; G96563.
DR RefSeq; NP_001322821.1; NM_001333539.1. [Q9C827-1]
DR RefSeq; NP_175645.1; NM_104114.3. [Q9C827-1]
DR AlphaFoldDB; Q9C827; -.
DR SMR; Q9C827; -.
DR BioGRID; 26891; 2.
DR IntAct; Q9C827; 1.
DR STRING; 3702.AT1G52360.2; -.
DR iPTMnet; Q9C827; -.
DR MetOSite; Q9C827; -.
DR PaxDb; Q9C827; -.
DR PRIDE; Q9C827; -.
DR ProteomicsDB; 241136; -. [Q9C827-1]
DR EnsemblPlants; AT1G52360.1; AT1G52360.1; AT1G52360. [Q9C827-1]
DR EnsemblPlants; AT1G52360.4; AT1G52360.4; AT1G52360. [Q9C827-1]
DR GeneID; 841666; -.
DR Gramene; AT1G52360.1; AT1G52360.1; AT1G52360. [Q9C827-1]
DR Gramene; AT1G52360.4; AT1G52360.4; AT1G52360. [Q9C827-1]
DR KEGG; ath:AT1G52360; -.
DR Araport; AT1G52360; -.
DR eggNOG; KOG0276; Eukaryota.
DR HOGENOM; CLU_005507_0_0_1; -.
DR OMA; PAISMDV; -.
DR PhylomeDB; Q9C827; -.
DR PRO; PR:Q9C827; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C827; baseline and differential.
DR Genevisible; Q9C827; 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: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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein 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..926
FT /note="Coatomer subunit beta'-2"
FT /id="PRO_0000285605"
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..390
FT /note="WD 8"
FT REPEAT 461..501
FT /note="WD 9"
FT REGION 847..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 104467 MW; 3BD4F74AEEB76ECB CRC64;
MPLRLEIKRK LAQRSERVKS VDLHPTEPWI LASLYSGTLC IWNYQTQVMA KSFEVTELPV
RSAKFVARKQ WVVAGADDMY IRVYNYNTMD KVKVFEAHSD YIRCVAVHPT LPYVLSSSDD
MLIKLWDWEK GWACTQIFEG HSHYVMQVTF NPKDTNTFAS ASLDRTIKIW NLGSPDPNFT
LDAHQKGVNC VDYFTGGDKP YLITGSDDHT AKVWDYQTKS CVQTLEGHTH NVSAVCFHPE
LPIIITGSED GTVRIWHATT YRLENTLNYG LERVWAIGYI KSSRRVVIGY DEGTIMVKLG
REIPVASMDN TGKIIWAKHN EIQTANIKSI GADYEVTDGE RLPLSVKELG TCDLYPQSLK
HNPNGRFVVV CGDGEYIIYT ALAWRNRSFG SGLEFVWSSE GECAVRESSS KIKIFSKNFQ
EKRSIRPTFS AEKIFGGTLL AMCSSDFICF YDWAECRLIQ RIDVTVKNLY WADSGDLVAI
ASDTSFYILK FNRDLVTSHF DSGRPTEEEG VEDAFEVLHE NDERVRTGIW VGDCFIYNNS
SWKLNYCVGG EVTTMYHLDR PMYLLGYLAS QSRVFLVDKE FNVIGYTLLL SLIEYKTLVM
RGDLDKASEI LPTIPKDQHN SVAHFLESRG MIEDALEIAT DPDYRFELAI QLGRLEIAQE
IAVEVQSESK WKQLGELAMS SGKLQMAEEC MKYAMDLSGL LLLYSSLGDA EGVTKLATLA
KEQGKNNVAF LCLFMLGKLE DCLQLLVESN RIPEAALMAR SYLPSKVSEI VALWRKDLSK
VNSKAAESLA DPEEYSNLFE DWQVALSVEA KAVETRGVYT GAKDYPSHAD KSSMTLVEAF
RNLQVEEEES LENGDMDHEE VVAEENGNEQ RNEDDVAEHV EEHHEEKEAE EEEGIVDGDS
TDGAVLVNGS EADEEWGTNN EGNPSA
