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BAG3_ARATH
ID   BAG3_ARATH              Reviewed;         303 AA.
AC   Q9LYP4; Q8LFF2;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=BAG family molecular chaperone regulator 3;
DE   AltName: Full=Bcl-2-associated athanogene 3;
GN   Name=BAG3; OrderedLocusNames=At5g07220; ORFNames=T28J14_160;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   DOI=10.1016/S0168-9452(03)00121-3;
RA   Juqiang Y., Cixin H., Hong Z.;
RT   "The BAG-family proteins in Arabidopsis thaliana.";
RL   Plant Sci. 165:1-7(2003).
RN   [6]
RP   INTERACTION WITH HSP70-1.
RX   PubMed=16003391; DOI=10.1038/sj.cdd.4401712;
RA   Kang C.H., Jung W.Y., Kang Y.H., Kim J.Y., Kim D.G., Jeong J.C., Baek D.W.,
RA   Jin J.B., Lee J.Y., Kim M.O., Chung W.S., Mengiste T., Koiwa H., Kwak S.S.,
RA   Bahk J.D., Lee S.Y., Nam J.S., Yun D.J., Cho M.J.;
RT   "AtBAG6, a novel calmodulin-binding protein, induces programmed cell death
RT   in yeast and plants.";
RL   Cell Death Differ. 13:84-95(2006).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=16636050; DOI=10.1074/jbc.m511794200;
RA   Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J.,
RA   Dickman M.B.;
RT   "Identification and functional characterization of the BAG protein family
RT   in Arabidopsis thaliana.";
RL   J. Biol. Chem. 281:18793-18801(2006).
CC   -!- FUNCTION: Co-chaperone that regulates diverse cellular pathways, such
CC       as programmed cell death and stress responses. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones (By
CC       similarity). Interacts with HSP70-1. {ECO:0000250,
CC       ECO:0000269|PubMed:16003391}.
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DR   EMBL; AL163652; CAB87278.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91123.1; -; Genomic_DNA.
DR   EMBL; AF428411; AAL16179.1; -; mRNA.
DR   EMBL; AY084885; AAM61448.1; -; mRNA.
DR   PIR; T48493; T48493.
DR   RefSeq; NP_196339.1; NM_120804.3.
DR   PDB; 4HWF; X-ray; 2.00 A; A/B=135-220.
DR   PDBsum; 4HWF; -.
DR   AlphaFoldDB; Q9LYP4; -.
DR   SMR; Q9LYP4; -.
DR   IntAct; Q9LYP4; 1.
DR   STRING; 3702.AT5G07220.1; -.
DR   PaxDb; Q9LYP4; -.
DR   PRIDE; Q9LYP4; -.
DR   ProteomicsDB; 240845; -.
DR   EnsemblPlants; AT5G07220.1; AT5G07220.1; AT5G07220.
DR   GeneID; 830613; -.
DR   Gramene; AT5G07220.1; AT5G07220.1; AT5G07220.
DR   KEGG; ath:AT5G07220; -.
DR   Araport; AT5G07220; -.
DR   TAIR; locus:2182900; AT5G07220.
DR   eggNOG; KOG4361; Eukaryota.
DR   HOGENOM; CLU_043370_1_0_1; -.
DR   InParanoid; Q9LYP4; -.
DR   OMA; QTASWET; -.
DR   OrthoDB; 1266506at2759; -.
DR   PhylomeDB; Q9LYP4; -.
DR   PRO; PR:Q9LYP4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LYP4; baseline and differential.
DR   Genevisible; Q9LYP4; AT.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.58.120; -; 1.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12329; PTHR12329; 1.
DR   Pfam; PF02179; BAG; 1.
DR   SMART; SM00264; BAG; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF63491; SSF63491; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Phosphoprotein; Reference proteome.
FT   CHAIN           1..303
FT                   /note="BAG family molecular chaperone regulator 3"
FT                   /id="PRO_0000415523"
FT   DOMAIN          45..119
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          138..216
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0WUQ1"
FT   CONFLICT        45
FT                   /note="F -> I (in Ref. 4; AAM61448)"
FT                   /evidence="ECO:0000305"
FT   HELIX           135..161
FT                   /evidence="ECO:0007829|PDB:4HWF"
FT   HELIX           168..189
FT                   /evidence="ECO:0007829|PDB:4HWF"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:4HWF"
FT   HELIX           194..218
FT                   /evidence="ECO:0007829|PDB:4HWF"
SQ   SEQUENCE   303 AA;  34244 MW;  EB3464BD401A9D37 CRC64;
     MMKMNTGTSP SVIGGGTSGN EWESRPGGMV VQRRTDQNSD VPRVFRVRVK YGSVYHEINI
     NSQSSFGELK KMLSDQVGLH HEDMKVLYKD KERDSKMFLD LCGVKDRSKL VVKEDPISQE
     KRLLAKRKNA AIEKASKSIS DISFEVDRLA GQVSAFETVI NKGGKVEEKS LVNLIEMLMN
     QLLRLDAIIA DGDVKLMRKM QVQRVQKYVE ALDLLKVKNS AKKVEVNKSV RHKPQTQTRF
     EQRDLLSFVE EEEEEPRNSN ASSSSGTPAV VASKWEMFDS ASTAKAAETV KPVPPRFKWE
     FFD
 
 
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