COPB1_ARATH
ID COPB1_ARATH Reviewed; 948 AA.
AC Q9SV21;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Coatomer subunit beta-1;
DE AltName: Full=Beta-coat protein 1;
DE Short=Beta-COP 1;
GN OrderedLocusNames=At4g31480; ORFNames=F3L17.50;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAB45907.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB79866.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL080283; CAB45907.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161579; CAB79866.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE85918.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85919.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66443.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66444.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66445.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66446.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66449.1; -; Genomic_DNA.
DR PIR; T10678; T10678.
DR RefSeq; NP_001190880.1; NM_001203951.1.
DR RefSeq; NP_001320104.1; NM_001342082.1.
DR RefSeq; NP_001328337.1; NM_001342088.1.
DR RefSeq; NP_001328338.1; NM_001342084.1.
DR RefSeq; NP_001328339.1; NM_001342087.1.
DR RefSeq; NP_001328340.1; NM_001342086.1.
DR RefSeq; NP_001328341.1; NM_001342083.1.
DR RefSeq; NP_001328342.1; NM_001342085.1.
DR RefSeq; NP_194876.2; NM_119297.4.
DR AlphaFoldDB; Q9SV21; -.
DR SMR; Q9SV21; -.
DR BioGRID; 14561; 28.
DR STRING; 3702.AT4G31480.2; -.
DR iPTMnet; Q9SV21; -.
DR PaxDb; Q9SV21; -.
DR PRIDE; Q9SV21; -.
DR ProteomicsDB; 240944; -.
DR EnsemblPlants; AT4G31480.1; AT4G31480.1; AT4G31480.
DR EnsemblPlants; AT4G31480.2; AT4G31480.2; AT4G31480.
DR EnsemblPlants; AT4G31480.4; AT4G31480.4; AT4G31480.
DR EnsemblPlants; AT4G31480.5; AT4G31480.5; AT4G31480.
DR EnsemblPlants; AT4G31480.7; AT4G31480.7; AT4G31480.
DR EnsemblPlants; AT4G31480.8; AT4G31480.8; AT4G31480.
DR EnsemblPlants; AT4G31480.9; AT4G31480.9; AT4G31480.
DR GeneID; 829275; -.
DR Gramene; AT4G31480.1; AT4G31480.1; AT4G31480.
DR Gramene; AT4G31480.2; AT4G31480.2; AT4G31480.
DR Gramene; AT4G31480.4; AT4G31480.4; AT4G31480.
DR Gramene; AT4G31480.5; AT4G31480.5; AT4G31480.
DR Gramene; AT4G31480.7; AT4G31480.7; AT4G31480.
DR Gramene; AT4G31480.8; AT4G31480.8; AT4G31480.
DR Gramene; AT4G31480.9; AT4G31480.9; AT4G31480.
DR KEGG; ath:AT4G31480; -.
DR Araport; AT4G31480; -.
DR TAIR; locus:2125254; AT4G31480.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q9SV21; -.
DR OrthoDB; 195812at2759; -.
DR PhylomeDB; Q9SV21; -.
DR PRO; PR:Q9SV21; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV21; baseline and differential.
DR Genevisible; Q9SV21; 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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; IEA:InterPro.
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..948
FT /note="Coatomer subunit beta-1"
FT /id="PRO_0000285616"
FT REPEAT 49..87
FT /note="HEAT 1"
FT REPEAT 92..126
FT /note="HEAT 2"
FT REPEAT 127..164
FT /note="HEAT 3"
FT REPEAT 274..311
FT /note="HEAT 4"
FT REPEAT 312..349
FT /note="HEAT 5"
FT REPEAT 391..428
FT /note="HEAT 6"
SQ SEQUENCE 948 AA; 106145 MW; 67B45615854A8B97 CRC64;
MDKSSTMLVH YDKGTPAVAN EIKEALEGND VEAKVDAMKK AIMLLLNGET IPQLFITIIR
YVLPSEDHTI QKLLLLYLEL IEKTDSKGKV LPEMILICQN LRNNLQHPNE YIRGVTLRFL
CRMKETEIVE PLTPSVLQNL EHRHPFVRRN AILAIMSIYK LPQGDQLFVD APEMIEKVLS
TEQDPSAKRN AFLMLFTCAE ERAVNYLLSN VDKVSDWNES LQMVVLELIR SVCKTKPAEK
GKYIKIIISL LSATSSAVIY ECAGTLVSLS SAPTAIRAAA NTYCQLLLSQ SDNNVKLILL
DRLYELKTLH RDIMVELIID VLRALSSPNL DIRRKTLDIS LDLITHHNIN EVVQMLKKEV
VKTQSGELEK NGEYRQMLIQ AIHACAVKFP EVASTVVHLL MDFLGDSNVA SALDVVVFVR
EIIETNPKLR VSIITRLLDT FYQIRAGKVC PCALWIIGEY CLSLSEVESG ISTITQCLGE
LPFYSVSEES EPTETSKKIQ PTSSAMVSSR KPVILADGTY ATQSAASETT FSSPTVVQGS
LTSGNLRALL LTGDFFLGAV VACTLTKLVL RLEEVQSSKT EVNKTVTQAL LIMVSMLQLG
QSPVSPHPID NDSYERIVLC IKLLCHRNDE MKKIWLESCR QSFVKMISEK QLREMEELKA
KTQTTHAQPD DLIDFFHLKS RKGMSQLELE DQVQDDLKRA TGEFTKDEND ANKLNRILQL
TGFSDPVYAE AYVTVHHYDI ALEVTVINRT KETLQNLCLE LATMGDLKLV ERPQNYSLAP
ERSMQIKANI KVSSTETGVI FGNIVYETSN VMERNVVVLN DIHIDIMDYI SPAVCSEVAF
RTMWAEFEWE NKVAVNTTIQ NEREFLDHII KSTNMKCLTA PSAIEGECGF LAANLYAKSV
FGEDALVNVS IEKQTDGALS GYIRIRSKTQ GIALSLGDKI TLKQKGSS
