位置:首页 > 蛋白库 > JAC1_ARATH
JAC1_ARATH
ID   JAC1_ARATH              Reviewed;         651 AA.
AC   Q9C9Q4;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 140.
DE   RecName: Full=J domain-containing protein required for chloroplast accumulation response 1;
GN   Name=JAC1; OrderedLocusNames=At1g75100; ORFNames=F9E10.5;
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 [MRNA], FUNCTION IN CHLOROPLAST MOVEMENTS, DISRUPTION
RP   PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=16113208; DOI=10.1104/pp.105.067371;
RA   Suetsugu N., Kagawa T., Wada M.;
RT   "An auxilin-like J-domain protein, JAC1, regulates phototropin-mediated
RT   chloroplast movement in Arabidopsis.";
RL   Plant Physiol. 139:151-162(2005).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   REVIEW.
RX   PubMed=17696776; DOI=10.1515/bc.2007.118;
RA   Suetsugu N., Wada M.;
RT   "Chloroplast photorelocation movement mediated by phototropin family
RT   proteins in green plants.";
RL   Biol. Chem. 388:927-935(2007).
RN   [6]
RP   FUNCTION IN ALUMINUM RESISTANCE.
RX   PubMed=17150990; DOI=10.1093/jxb/erl221;
RA   Ezaki B., Kiyohara H., Matsumoto H., Nakashima S.;
RT   "Overexpression of an auxilin-like gene (F9E10.5) can suppress Al uptake in
RT   roots of Arabidopsis.";
RL   J. Exp. Bot. 58:497-506(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   FUNCTION IN ACTIN FILAMENTS REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia GL1;
RX   PubMed=21737483; DOI=10.1093/pcp/pcr087;
RA   Ichikawa S., Yamada N., Suetsugu N., Wada M., Kadota A.;
RT   "Red light, Phot1 and JAC1 modulate Phot2-dependent reorganization of
RT   chloroplast actin filaments and chloroplast avoidance movement.";
RL   Plant Cell Physiol. 52:1422-1432(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 551-651, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF 614-HIS--ASP-616.
RX   PubMed=20562448; DOI=10.1093/pcp/pcq089;
RA   Takano A., Suetsugu N., Wada M., Kohda D.;
RT   "Crystallographic and functional analyses of J-domain of JAC1 essential for
RT   chloroplast photorelocation movement in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 51:1372-1376(2010).
CC   -!- FUNCTION: Required for chloroplast photorelocation movement;
CC       chloroplast accumulation upon low blue light and for chloroplast
CC       movement to the bottom of cells in darkness, by modulating chloroplast
CC       actin (Cp-actin) filaments distribution, appearance and disappearance.
CC       May mediate a slight resistance to aluminum in root hair cells.
CC       {ECO:0000269|PubMed:16113208, ECO:0000269|PubMed:17150990,
CC       ECO:0000269|PubMed:20562448, ECO:0000269|PubMed:21737483}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16113208}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and stems, but not in roots.
CC       {ECO:0000269|PubMed:16113208}.
CC   -!- DOMAIN: The J domain co-chaperone activity is required for chloroplast
CC       photorelocation movement. {ECO:0000269|PubMed:20562448}.
CC   -!- DISRUPTION PHENOTYPE: Lacks the chloroplast accumulation response under
CC       weak blue light and chloroplast movement in darkness, but shows a
CC       normal avoidance response under strong blue light. Non biased
CC       distribution of chloroplast actin (Cp-actin) filaments.
CC       {ECO:0000269|PubMed:16113208, ECO:0000269|PubMed:20562448,
CC       ECO:0000269|PubMed:21737483}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB158477; BAE44203.1; -; mRNA.
DR   EMBL; AC013258; AAG51921.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35672.1; -; Genomic_DNA.
DR   EMBL; AY057504; AAL09745.1; -; mRNA.
DR   EMBL; AY103303; AAM65355.1; -; mRNA.
DR   PIR; A96781; A96781.
DR   RefSeq; NP_565101.1; NM_106166.4.
DR   PDB; 3AG7; X-ray; 1.80 A; A=551-651.
DR   PDBsum; 3AG7; -.
DR   AlphaFoldDB; Q9C9Q4; -.
DR   SMR; Q9C9Q4; -.
DR   BioGRID; 29066; 3.
DR   IntAct; Q9C9Q4; 2.
DR   STRING; 3702.AT1G75100.1; -.
DR   iPTMnet; Q9C9Q4; -.
DR   PaxDb; Q9C9Q4; -.
DR   PRIDE; Q9C9Q4; -.
DR   ProteomicsDB; 238968; -.
DR   EnsemblPlants; AT1G75100.1; AT1G75100.1; AT1G75100.
DR   GeneID; 843847; -.
DR   Gramene; AT1G75100.1; AT1G75100.1; AT1G75100.
DR   KEGG; ath:AT1G75100; -.
DR   Araport; AT1G75100; -.
DR   TAIR; locus:2037256; AT1G75100.
DR   eggNOG; KOG0431; Eukaryota.
DR   HOGENOM; CLU_026675_0_0_1; -.
DR   InParanoid; Q9C9Q4; -.
DR   OMA; WNGFNEK; -.
DR   OrthoDB; 319959at2759; -.
DR   PhylomeDB; Q9C9Q4; -.
DR   EvolutionaryTrace; Q9C9Q4; -.
DR   PRO; PR:Q9C9Q4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9Q4; baseline and differential.
DR   Genevisible; Q9C9Q4; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR   GO; GO:0071483; P:cellular response to blue light; IMP:UniProtKB.
DR   GO; GO:0009904; P:chloroplast accumulation movement; IMP:TAIR.
DR   GO; GO:0009903; P:chloroplast avoidance movement; IMP:UniProtKB.
DR   GO; GO:0072318; P:clathrin coat disassembly; IBA:GO_Central.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR   GO; GO:0080183; P:response to photooxidative stress; IEP:TAIR.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   SUPFAM; SSF46565; SSF46565; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..651
FT                   /note="J domain-containing protein required for chloroplast
FT                   accumulation response 1"
FT                   /id="PRO_0000422083"
FT   DOMAIN          586..651
FT                   /note="J"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          532..562
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MUTAGEN         614..616
FT                   /note="HPD->AAA: Impaired chloroplast photorelocation
FT                   movement."
FT                   /evidence="ECO:0000269|PubMed:20562448"
FT   HELIX           551..564
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   TURN            565..569
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           571..575
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           576..580
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           593..595
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           599..613
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           615..620
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   HELIX           625..645
FT                   /evidence="ECO:0007829|PDB:3AG7"
FT   TURN            646..648
FT                   /evidence="ECO:0007829|PDB:3AG7"
SQ   SEQUENCE   651 AA;  71602 MW;  1FC2139336D27EEC CRC64;
     MQTLPSSETV LLGSNSAPPV LRSPGGDDVD IDFGDVFGGP PKRRSKVTSN EVTRHSFSES
     ALRRRDVIVD VGDLLPQDEK PVFGEDTSSV RRRFTTDDFF DDIFRVNESS SLPGSRILSP
     AHKPESSSGT SSPSQFSLPA KATEIPTFNL AATRSLNKNK ETVSSSPLSR TSSKADVVST
     AKSYSDDCDD PPQVFVTGKG RQFHFSIYKW PNKGVPVVIW GSSRLSSMSK AEETTPVPLS
     DYRKTSVVEK LGKNEEGDGK SGLSGLKDVK KTSLKRPGVQ TKEEKTETDL KSEQAFFGVS
     KAREANVKPL DSVESEQAFS GVSKAHEATT VKPLHSIFHE EDERQDEKIV SEREVRKGKS
     KAKNTRSFTE DSRTKKKSQG TKSSLDSSPI PDKSSFASSS AAPEVGKDGV KGKVSDFVKI
     FSKGASVGAG GESLGQSSRW RAKETPKTDI IHDGSNAKET VNIPDQQKKS TPDIPAMNRD
     QKPSQSTQKK DSDRESMNYK APGDTVQEER QEPSTTHTTS EDIDEPFHVN FDVEDITQDE
     NKMEEANKDA EEIKNIDAKI RKWSSGKSGN IRSLLSTLQY ILWSGSGWKP VPLMDMIEGN
     AVRKSYQRAL LILHPDKLQQ KGASANQKYM AEKVFELLQE AWDHFNTLGP V
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024