CHIP_ARATH
ID CHIP_ARATH Reviewed; 278 AA.
AC Q9SRS9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase CHIP {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:16640601, ECO:0000269|PubMed:17241447};
DE AltName: Full=Carboxyl terminus of HSC70-interacting protein {ECO:0000303|PubMed:12805616};
DE Short=AtCHIP {ECO:0000303|PubMed:12805616};
DE AltName: Full=Plant U-box protein 61;
DE AltName: Full=RING-type E3 ubiquitin transferase CHIP {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 61;
GN Name=CHIP {ECO:0000303|PubMed:20028838}; Synonyms=PUB61;
GN OrderedLocusNames=At3g07370 {ECO:0000312|Araport:AT3G07370};
GN ORFNames=F21O3.8 {ECO:0000312|EMBL:AAF02162.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, AND INDUCTION BY ABIOTIC STRESSES.
RX PubMed=12805616; DOI=10.1104/pp.103.020800;
RA Yan J., Wang J., Li Q., Hwang J.R., Patterson C., Zhang H.;
RT "AtCHIP, a U-box-containing E3 ubiquitin ligase, plays a critical role in
RT temperature stress tolerance in Arabidopsis.";
RL Plant Physiol. 132:861-869(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH PP2AA1; PP2AA3;
RP PP2A5; UBC8; UBC9 AND UBC10.
RX PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x;
RA Luo J., Shen G., Yan J., He C., Zhang H.;
RT "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT subunits and alters plant response to abscisic acid treatment.";
RL Plant J. 46:649-657(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH CLPP4.
RX PubMed=17241447; DOI=10.1111/j.1365-313x.2006.02963.x;
RA Shen G., Yan J., Pasapula V., Luo J., He C., Clarke A.K., Zhang H.;
RT "The chloroplast protease subunit ClpP4 is a substrate of the E3 ligase
RT AtCHIP and plays an important role in chloroplast function.";
RL Plant J. 49:228-237(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH FTSH1 AND FTSH2.
RX PubMed=17714429; DOI=10.1111/j.1365-313x.2007.03239.x;
RA Shen G., Adam Z., Zhang H.;
RT "The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast
RT FtsH protease, and affects protein degradation in chloroplasts.";
RL Plant J. 52:309-321(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH HSC70-4.
RX PubMed=20028838; DOI=10.1105/tpc.109.071548;
RA Lee S., Lee D.W., Lee Y., Mayer U., Stierhof Y.D., Lee S., Jurgens G.,
RA Hwang I.;
RT "Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate
RT plastid-destined precursor degradation through the ubiquitin-26S proteasome
RT system in Arabidopsis.";
RL Plant Cell 21:3984-4001(2009).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity and may target
CC misfolded substrates towards proteasomal degradation. Regulates the
CC activity of some serine/threonine-protein phosphatases by E3 ubiquitin-
CC protein ligase activity. Required for responses to biotic and abiotic
CC stresses such as auxin, abscisic acid (ABA), low and high temperature
CC and darkness, probably through the activation of serine/threonine-
CC protein phosphatase and the subsequent modification of the plasma
CC membrane composition. Regulates the chloroplastic Clp proteolytic
CC activity in response to stresses. Ubiquitylates FtsH1, a component of
CC the chloroplast FtsH protease, and affects protein degradation in
CC chloroplasts. Mediates plastid precursor degradation to prevent
CC cytosolic precursor accumulation, together with the molecular chaperone
CC HSC70-4. Mediates ubiquitination of transit peptides and thereby led to
CC their degradation through the ubiquitin-proteasome system.
CC {ECO:0000269|PubMed:12805616, ECO:0000269|PubMed:16640601,
CC ECO:0000269|PubMed:17241447, ECO:0000269|PubMed:17714429,
CC ECO:0000269|PubMed:20028838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:16640601,
CC ECO:0000269|PubMed:17241447};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:16640601, ECO:0000269|PubMed:17241447}.
CC -!- SUBUNIT: Interacts with HSC70-4, PP2AA1, PP2AA3 and PP2A5, as well as
CC with UBC8, UBC9 and UBC10. Interacts also with the chloroplastic
CC proteolytic subunits ClpP4, FtsH1 and FtsH2.
CC {ECO:0000269|PubMed:16640601, ECO:0000269|PubMed:17241447,
CC ECO:0000269|PubMed:17714429, ECO:0000269|PubMed:20028838}.
CC -!- INDUCTION: By abiotic stresses such as chilling, heat-shock and salts
CC (selenate and NaCl). {ECO:0000269|PubMed:12805616}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:Q9WUD1}.
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DR EMBL; AC009853; AAF02162.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74535.1; -; Genomic_DNA.
DR EMBL; AY042807; AAK68747.1; -; mRNA.
DR EMBL; AY064647; AAL47358.1; -; mRNA.
DR RefSeq; NP_566305.1; NM_111616.3.
DR AlphaFoldDB; Q9SRS9; -.
DR SMR; Q9SRS9; -.
DR BioGRID; 5260; 17.
DR STRING; 3702.AT3G07370.1; -.
DR MetOSite; Q9SRS9; -.
DR PaxDb; Q9SRS9; -.
DR PRIDE; Q9SRS9; -.
DR ProteomicsDB; 245190; -.
DR EnsemblPlants; AT3G07370.1; AT3G07370.1; AT3G07370.
DR GeneID; 819925; -.
DR Gramene; AT3G07370.1; AT3G07370.1; AT3G07370.
DR KEGG; ath:AT3G07370; -.
DR Araport; AT3G07370; -.
DR TAIR; locus:2079716; AT3G07370.
DR eggNOG; KOG4642; Eukaryota.
DR HOGENOM; CLU_056455_0_0_1; -.
DR InParanoid; Q9SRS9; -.
DR OMA; FLEKNGW; -.
DR OrthoDB; 1422450at2759; -.
DR PhylomeDB; Q9SRS9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SRS9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRS9; baseline and differential.
DR Genevisible; Q9SRS9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0045862; P:positive regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:TAIR.
DR CDD; cd16654; RING-Ubox_CHIP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045200; CHIP/LubX.
DR InterPro; IPR045202; CHIP/LubX_RING-Ubox.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46803; PTHR46803; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome; Repeat; TPR repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..278
FT /note="E3 ubiquitin-protein ligase CHIP"
FT /id="PRO_0000308986"
FT REPEAT 10..43
FT /note="TPR 1"
FT REPEAT 45..77
FT /note="TPR 2"
FT REPEAT 78..111
FT /note="TPR 3"
FT DOMAIN 199..273
FT /note="U-box"
FT COILED 143..194
FT /evidence="ECO:0000255"
SQ SEQUENCE 278 AA; 31655 MW; 6F828206916394B9 CRC64;
MVTGVASAMA ERLKEDGNNC FKKERFGAAI DAYTEAIALS PNVPAYWTNR ALCHMKRKDW
TKVEEDCRKA IQLVHNSVKA HYMLGLALLQ KKEFTNGVKE LQRALDLGRC SNPTGYMVEE
IWEELSKAKY MEWELVSAMR SWELNSLKET CEAALNQQRA LDMSRTEESS DEAYTAHTER
LKALERVFKK AAEEDKPTEV PDYLCCNITL EIFRDPVISP SGVTYERAAI LEHLKKVGKF
DPITREKIDP ANLVPNLAIK EAVAAYLEKH VWAYKMGC
