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COG2_ARATH
ID   COG2_ARATH              Reviewed;         756 AA.
AC   F4JRR1; Q9ASS9; Q9SZX4;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 2 {ECO:0000303|PubMed:27448097};
DE            Short=COG complex subunit 2 {ECO:0000303|PubMed:27448097};
DE   AltName: Full=Component of oligomeric Golgi complex 2 {ECO:0000303|PubMed:27448097};
GN   Name=COG2 {ECO:0000303|PubMed:27448097};
GN   OrderedLocusNames=At4g24840 {ECO:0000312|Araport:AT4G24840};
GN   ORFNames=F6I7.50 {ECO:0000312|EMBL:CAB41124.1};
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).
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [5]
RP   FUNCTION, INTERACTION WITH FPP3/VETH1 AND FPP2/VETH2, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=25541219; DOI=10.1093/pcp/pcu197;
RA   Oda Y., Iida Y., Nagashima Y., Sugiyama Y., Fukuda H.;
RT   "Novel coiled-coil proteins regulate exocyst association with cortical
RT   microtubules in xylem cells via the conserved oligomeric golgi-complex 2
RT   protein.";
RL   Plant Cell Physiol. 56:277-286(2015).
RN   [6]
RP   SUBUNIT, INTERACTION WITH COG3 AND COG4, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=27448097; DOI=10.1371/journal.pgen.1006140;
RA   Tan X., Cao K., Liu F., Li Y., Li P., Gao C., Ding Y., Lan Z., Shi Z.,
RA   Rui Q., Feng Y., Liu Y., Zhao Y., Wu C., Zhang Q., Li Y., Jiang L., Bao Y.;
RT   "Arabidopsis COG complex subunits COG3 and COG8 modulate golgi morphology,
RT   vesicle trafficking homeostasis and are essential for pollen tube growth.";
RL   PLoS Genet. 12:E1006140-E1006140(2016).
RN   [7]
RP   INTERACTION WITH SEC15B.
RC   STRAIN=cv. Columbia;
RX   PubMed=27801942; DOI=10.1111/nph.14267;
RA   Vukasinovic N., Oda Y., Pejchar P., Synek L., Pecenkova T., Rawat A.,
RA   Sekeres J., Potocky M., Zarsky V.;
RT   "Microtubule-dependent targeting of the exocyst complex is necessary for
RT   xylem development in Arabidopsis.";
RL   New Phytol. 213:1052-1067(2017).
CC   -!- FUNCTION: Required for normal Golgi morphology and function (By
CC       similarity). Ensures, when in complex with FPP3/VETH1 and FPP2/VETH2,
CC       the correct secondary cell wall (SCW) deposition pattern by recruiting
CC       exocyst components to cortical microtubules in xylem cells during
CC       secondary cell wall deposition (PubMed:25541219). {ECO:0000250,
CC       ECO:0000269|PubMed:25541219}.
CC   -!- SUBUNIT: Homodimer (PubMed:27448097). Component of the conserved
CC       oligomeric Golgi complex which is composed of eight different subunits
CC       and is required for normal Golgi morphology and localization
CC       (Probable). Binds to COG3 and COG4 (PubMed:27448097). Interacts with
CC       FPP3/VETH1 and FPP2/VETH2; this interaction promotes the association
CC       between cortical microtubules and EXO70A1 (PubMed:25541219). Binds to
CC       SEC15B, and, possibly, with EXO70A1, SEC3A and SEC10A
CC       (PubMed:27801942). {ECO:0000250, ECO:0000269|PubMed:25541219,
CC       ECO:0000269|PubMed:27448097, ECO:0000269|PubMed:27801942,
CC       ECO:0000305|PubMed:27448097}.
CC   -!- INTERACTION:
CC       F4JRR1; Q5ICL9: NPR4; NbExp=3; IntAct=EBI-4429018, EBI-1392093;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:O59705}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O59705}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O59705}. Note=Localized at vesicle-like small
CC       compartments at cortical microtubules. {ECO:0000269|PubMed:25541219}.
CC   -!- SIMILARITY: Belongs to the COG2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB41124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049657; CAB41124.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161562; CAB79394.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84970.1; -; Genomic_DNA.
DR   EMBL; AF367300; AAK32887.1; -; mRNA.
DR   EMBL; AY091689; AAM10288.1; -; mRNA.
DR   PIR; T06668; T06668.
DR   RefSeq; NP_567710.1; NM_118617.5.
DR   AlphaFoldDB; F4JRR1; -.
DR   IntAct; F4JRR1; 38.
DR   STRING; 3702.AT4G24840.1; -.
DR   TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   PaxDb; F4JRR1; -.
DR   PRIDE; F4JRR1; -.
DR   ProteomicsDB; 218394; -.
DR   EnsemblPlants; AT4G24840.1; AT4G24840.1; AT4G24840.
DR   GeneID; 828587; -.
DR   Gramene; AT4G24840.1; AT4G24840.1; AT4G24840.
DR   KEGG; ath:AT4G24840; -.
DR   Araport; AT4G24840; -.
DR   TAIR; locus:2126808; AT4G24840.
DR   eggNOG; KOG2307; Eukaryota.
DR   HOGENOM; CLU_005470_0_0_1; -.
DR   InParanoid; F4JRR1; -.
DR   OMA; CWAEGVY; -.
DR   OrthoDB; 190117at2759; -.
DR   PRO; PR:F4JRR1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JRR1; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017119; C:Golgi transport complex; IBA:GO_Central.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0060178; P:regulation of exocyst localization; IDA:UniProtKB.
DR   InterPro; IPR009316; COG2.
DR   InterPro; IPR024603; COG_complex_COG2_C.
DR   InterPro; IPR024602; COG_su2_N.
DR   PANTHER; PTHR12961; PTHR12961; 1.
DR   Pfam; PF06148; COG2; 1.
DR   Pfam; PF12022; DUF3510; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..756
FT                   /note="Conserved oligomeric Golgi complex subunit 2"
FT                   /id="PRO_0000448525"
FT   REGION          173..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          62..82
FT                   /evidence="ECO:0000255"
FT   CONFLICT        682
FT                   /note="L -> F (in Ref. 3; AAK32887/AAM10288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   756 AA;  84619 MW;  956A87FC4FDCAB8F CRC64;
     MSDLVATSPS PSSAPRSATD FFSDPYDSHP LWFKPSLFLS PNFDSESYIS ELRTFVPFDT
     LRSELRSHLA SLNRELVDLI NRDYADFVNL STKLVDIDAA VVRMRAPLLE LREKITGFRG
     SVEAALFALR NGLQQRSDAA AAREVLELLL DTFHVVSKVE KLIKVLPSTP SDWQNEDANS
     MGRSSMNDEN STQQDGTTMR ETQSMLLERI ASEMNRLKFY MAHAQNLPFI ENMEKRIQSA
     SVLLDASLGH CFIDGLNNSD TSVLYNCLRA YAAIDNTNAA EEIFRTTIVA PFIQKIITHE
     TTTNAAGTSE DELENDYKQI KHFIAKDCKM LLEISSTDKS GLHVFDFLAN SILKEVLWAI
     QKVKPGAFSP GRPTEFLKNY KASLDFLAYL EGYCPSRSAV TKFRAEAICV EFMKQWNVGV
     YFSLRFQEIA GALDSALTSP SLVFIQDSDK ESSLNLILRQ SDTLLECLRS CWKEDVLVFS
     AADKFLRLTL QLLSRYSFWV SSALNNRKSN ASPSPGCEWA VSATAEDFVY VIHDVNCLVS
     EVCGDYLGHI SQYLSSSSTE VLDVVRISIE QGGVSLEKVL PLLTKTIIDV IVDKSVEDLR
     QLRGITATFR MTNKPLPVRH SPYVVGLLRP VKAFLEGDKA RNYLTQKTKE ELLHGSVSEI
     TRRYYELAAD VVSVARKTQS SLQKLRQNAQ RRGGAASGVS DQNVSETDKM CMQLFLDIQE
     YGRNVSALGL KPADIPEYCS FWQCVAPADR QNSISV
 
 
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