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CV_ARATH
ID   CV_ARATH                Reviewed;         152 AA.
AC   Q8S8K8; Q94CB8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Protein CHLOROPLAST VESICULATION {ECO:0000303|PubMed:25538186};
DE   Flags: Precursor;
GN   Name=CV {ECO:0000303|PubMed:25538186};
GN   OrderedLocusNames=At2g25625 {ECO:0000312|Araport:AT2G25625};
GN   ORFNames=F3N11 {ECO:0000312|EMBL:AAM15100.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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] (ISOFORM 2).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INTERACTION WITH
RP   PSBO1, INDUCTION BY SALT AND OXIDATIVE STRESS, REPRESSION BY CYTOKININ,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=25538186; DOI=10.1105/tpc.114.133116;
RA   Wang S., Blumwald E.;
RT   "Stress-induced chloroplast degradation in Arabidopsis is regulated via a
RT   process independent of autophagy and senescence-associated vacuoles.";
RL   Plant Cell 26:4875-4888(2014).
RN   [7]
RP   INDUCTION BY NAC072/RD26.
RC   STRAIN=cv. Columbia;
RX   PubMed=29659022; DOI=10.1111/nph.15127;
RA   Kamranfar I., Xue G.-P., Tohge T., Sedaghatmehr M., Fernie A.R.,
RA   Balazadeh S., Mueller-Roeber B.;
RT   "Transcription factor RD26 is a key regulator of metabolic reprogramming
RT   during dark-induced senescence.";
RL   New Phytol. 218:1543-1557(2018).
CC   -!- FUNCTION: Triggers stress-induced chloroplast degradation,
CC       independently of autophagy and senescence-associated vacuoles
CC       (PubMed:25538186). After targeting to the chloroplast, triggers its
CC       destabilization and subsequent disassembly, inducing the formation of
CC       CV-containing vesicles (CCVs) carrying stromal proteins, envelope
CC       membrane proteins, and thylakoid membrane proteins which are released
CC       from the chloroplasts and mobilized to the vacuole for proteolysis
CC       (PubMed:25538186). {ECO:0000269|PubMed:25538186}.
CC   -!- SUBUNIT: Interacts with the photosystem II subunit PsbO1 via its C-
CC       terminal region in the chloroplast thylakoid membrane and in CV-
CC       containing vesicles (CCVs). {ECO:0000269|PubMed:25538186}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:25538186}; Single-pass membrane protein
CC       {ECO:0000255}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:25538186}; Single-pass membrane protein
CC       {ECO:0000255}. Plastid, chloroplast envelope
CC       {ECO:0000269|PubMed:25538186}. Vacuole {ECO:0000269|PubMed:25538186}.
CC       Vesicle {ECO:0000269|PubMed:25538186}. Note=Present in vesicle-like
CC       spots observed in destabilized chloroplasts; these CV-containing
CC       vesicles (CCVs) carrying stromal proteins, envelope membrane proteins,
CC       and thylakoid membrane proteins translocate later to the cytosol before
CC       being mobilized to the vacuole for proteolysis.
CC       {ECO:0000269|PubMed:25538186}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8S8K8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8S8K8-2; Sequence=VSP_061274;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in senescent and mature leaves but
CC       not in young leaves. {ECO:0000269|PubMed:25538186}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during senescence.
CC       {ECO:0000269|PubMed:25538186}.
CC   -!- INDUCTION: Induced by abiotic stresses such as salt stress and methyl
CC       viologen (MV)-induced oxidative stress (PubMed:25538186). Triggered by
CC       NAC072/RD26 during senescence (PubMed:29659022). Down-regulated by
CC       cytokinin (PubMed:25538186). {ECO:0000269|PubMed:25538186,
CC       ECO:0000269|PubMed:29659022}.
CC   -!- DISRUPTION PHENOTYPE: Delayed chloroplast turnover and senescence
CC       induced by abiotic stress and associated with an enhanced tolerance to
CC       drought, salinity, and oxidative stress. {ECO:0000269|PubMed:25538186}.
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DR   EMBL; AC006053; AAM15100.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07726.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07727.1; -; Genomic_DNA.
DR   EMBL; AY034981; AAK59486.1; -; mRNA.
DR   EMBL; AY063071; AAL34245.1; -; mRNA.
DR   EMBL; AK227210; BAE99248.1; -; mRNA.
DR   EMBL; AY088242; AAM65783.1; -; mRNA.
DR   RefSeq; NP_850063.1; NM_179732.4.
DR   AlphaFoldDB; Q8S8K8; -.
DR   STRING; 3702.AT2G25625.1; -.
DR   PaxDb; Q8S8K8; -.
DR   PRIDE; Q8S8K8; -.
DR   EnsemblPlants; AT2G25625.1; AT2G25625.1; AT2G25625. [Q8S8K8-1]
DR   EnsemblPlants; AT2G25625.2; AT2G25625.2; AT2G25625. [Q8S8K8-2]
DR   GeneID; 817103; -.
DR   Gramene; AT2G25625.1; AT2G25625.1; AT2G25625. [Q8S8K8-1]
DR   Gramene; AT2G25625.2; AT2G25625.2; AT2G25625. [Q8S8K8-2]
DR   KEGG; ath:AT2G25625; -.
DR   Araport; AT2G25625; -.
DR   TAIR; locus:505006272; AT2G25625.
DR   eggNOG; ENOG502S9UX; Eukaryota.
DR   HOGENOM; CLU_118309_0_0_1; -.
DR   InParanoid; Q8S8K8; -.
DR   OMA; WRRTEDE; -.
DR   OrthoDB; 1501485at2759; -.
DR   PhylomeDB; Q8S8K8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8S8K8; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097708; C:intracellular vesicle; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:UniProtKB.
DR   GO; GO:1904821; P:chloroplast disassembly; IMP:TAIR.
DR   GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR   GO; GO:0009735; P:response to cytokinin; IEP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:1902074; P:response to salt; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW   Stress response; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   TRANSIT         1..22
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..152
FT                   /note="Protein CHLOROPLAST VESICULATION"
FT                   /id="PRO_0000454278"
FT   TRANSMEM        48..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          92..152
FT                   /note="Important for chloroplast destabilization and the
FT                   formation of CV-containing vesicles"
FT                   /evidence="ECO:0000269|PubMed:25538186"
FT   VAR_SEQ         34..35
FT                   /note="CR -> W (in isoform 2)"
FT                   /id="VSP_061274"
SQ   SEQUENCE   152 AA;  16218 MW;  8418841F044BBC38 CRC64;
     MAGRISCCLN LPPLDSNSAQ SLASLLKTTS KISCRRTENE TEPRKNKCSF VLGVAATVVI
     GGIQINDVAS VEAAVVKSPV EEMAAGVVPP RRWSDKRTCP PWLENSLETI VPENLPRPSA
     HRRLELAGLA KGDAPPVGVV MTRVNRGGCF SV
 
 
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