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PCC1_ARATH
ID   PCC1_ARATH              Reviewed;          81 AA.
AC   Q94C26; Q9LID9;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cysteine-rich and transmembrane domain-containing protein PCC1;
DE   AltName: Full=Protein PATHOGEN AND CIRCADIAN CONTROLLED 1;
GN   Name=PCC1; OrderedLocusNames=At3g22231; ORFNames=MKA23;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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].
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   FUNCTION, AND INDUCTION BY PATHOGEN.
RX   PubMed=14614626; DOI=10.1007/s00425-003-1143-z;
RA   Sauerbrunn N., Schlaich N.L.;
RT   "PCC1: a merging point for pathogen defence and circadian signalling in
RT   Arabidopsis.";
RL   Planta 218:552-561(2004).
RN   [6]
RP   TOPOLOGY, SUBCELLULAR LOCATION, AND GENE FAMILY.
RX   PubMed=19933165; DOI=10.1093/bioinformatics/btp647;
RA   Venancio T.M., Aravind L.;
RT   "CYSTM, a novel cysteine-rich transmembrane module with a role in stress
RT   tolerance across eukaryotes.";
RL   Bioinformatics 26:149-152(2010).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY UV, DEVELOPMENTAL STAGE, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=19781011; DOI=10.1111/j.1365-3040.2009.02045.x;
RA   Segarra S., Mir R., Martinez C., Leon J.;
RT   "Genome-wide analyses of the transcriptomes of salicylic acid-deficient
RT   versus wild-type plants uncover Pathogen and Circadian Controlled 1 (PCC1)
RT   as a regulator of flowering time in Arabidopsis.";
RL   Plant Cell Environ. 33:11-22(2010).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=22442409; DOI=10.1093/jxb/ers028;
RA   Guelette B.S., Benning U.F., Hoffmann-Benning S.;
RT   "Identification of lipids and lipid-binding proteins in phloem exudates
RT   from Arabidopsis thaliana.";
RL   J. Exp. Bot. 63:3603-3616(2012).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23833195; DOI=10.1093/jxb/ert177;
RA   Mir R., Hernandez M.L., Abou-Mansour E., Martinez-Rivas J.M., Mauch F.,
RA   Metraux J.-P., Leon J.;
RT   "Pathogen and Circadian Controlled 1 (PCC1) regulates polar lipid content,
RT   ABA-related responses, and pathogen defence in Arabidopsis thaliana.";
RL   J. Exp. Bot. 64:3385-3395(2013).
CC   -!- FUNCTION: Modulates resistance against pathogens including oomycetes
CC       (e.g. Hyaloperonospora parasitica and Phytophthora brassicae) and fungi
CC       (e.g. Phytophthora brassicae). Controls the abscisic acid-mediated
CC       (ABA) signaling pathways. Regulator of the flowering time in response
CC       to stress (e.g. UV-C). Regulates polar lipid content; promotes
CC       phosphatidylinositol (PI) and 18:0 but prevents 18:2 and 18:3 polar
CC       lipids accumulation. {ECO:0000269|PubMed:14614626,
CC       ECO:0000269|PubMed:19781011, ECO:0000269|PubMed:23833195}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19933165};
CC       Single-pass membrane protein {ECO:0000269|PubMed:19933165}.
CC   -!- TISSUE SPECIFICITY: Expressed at very low levels in seedlings and
CC       petioles, and at higher levels in leaves. Also present in phloem sap.
CC       {ECO:0000269|PubMed:19781011, ECO:0000269|PubMed:22442409}.
CC   -!- DEVELOPMENTAL STAGE: Low expression after germination followed by an
CC       abrupt level increase in 10-days old seedlings. Accumulates in
CC       senescent leaves. {ECO:0000269|PubMed:19781011}.
CC   -!- INDUCTION: Rapidly up-regulated after pathogen exposure (e.g. avirulent
CC       and virulent Pseudomonas syringae pv. tomato) in a salicylic acid (SA)
CC       defense-signaling pathway-dependent manner. Circadian-regulation with
CC       accumulation during the light period, peaks of expression at the end of
CC       the day, and low levels during the dark period. Up-regulated by UV-C
CC       light through a SA-dependent process and in a CONSTANS- (CO) dependent
CC       manner. {ECO:0000269|PubMed:14614626, ECO:0000269|PubMed:19781011}.
CC   -!- DISRUPTION PHENOTYPE: Late flowering and defective in UV-C light
CC       acceleration of flowering. Strong reduction of FLOWERING LOCUS T (FT)
CC       expression. Hypersensitivity to abscisic acid (ABA) and alterations in
CC       polar lipid contents and their corresponding fatty acids; reduced
CC       levels of phosphatidylinositol (PI) and of 18:0, but increased levels
CC       of 18:2 and 18:3 polar lipids. Increased susceptibility to the hemi-
CC       biotrophic oomycete pathogen Phytophthora brassicae but enhanced
CC       resistance to the necrotrophic fungal pathogen Botrytis cinerea.
CC       {ECO:0000269|PubMed:19781011, ECO:0000269|PubMed:23833195}.
CC   -!- SIMILARITY: Belongs to the CYSTM1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB03071.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP001306; BAB03071.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76608.1; -; Genomic_DNA.
DR   EMBL; AY037207; AAK59792.1; -; mRNA.
DR   EMBL; BT002668; AAO11584.1; -; mRNA.
DR   EMBL; AK316896; BAH19603.1; -; mRNA.
DR   EMBL; AK317758; BAH20414.1; -; mRNA.
DR   RefSeq; NP_566702.1; NM_113121.5.
DR   AlphaFoldDB; Q94C26; -.
DR   SMR; Q94C26; -.
DR   BioGRID; 7120; 3.
DR   STRING; 3702.AT3G22231.1; -.
DR   iPTMnet; Q94C26; -.
DR   PaxDb; Q94C26; -.
DR   PRIDE; Q94C26; -.
DR   ProteomicsDB; 236285; -.
DR   EnsemblPlants; AT3G22231.1; AT3G22231.1; AT3G22231.
DR   GeneID; 821788; -.
DR   Gramene; AT3G22231.1; AT3G22231.1; AT3G22231.
DR   KEGG; ath:AT3G22231; -.
DR   Araport; AT3G22231; -.
DR   TAIR; locus:505006361; AT3G22231.
DR   HOGENOM; CLU_128451_4_0_1; -.
DR   InParanoid; Q94C26; -.
DR   OMA; MECIFCC; -.
DR   OrthoDB; 1607719at2759; -.
DR   PhylomeDB; Q94C26; -.
DR   PRO; PR:Q94C26; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q94C26; baseline and differential.
DR   Genevisible; Q94C26; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0071494; P:cellular response to UV-C; IDA:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR   GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR   GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR   GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR   InterPro; IPR028144; CYSTM_dom.
DR   Pfam; PF12734; CYSTM; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Cell membrane; Lipid metabolism; Membrane;
KW   Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..81
FT                   /note="Cysteine-rich and transmembrane domain-containing
FT                   protein PCC1"
FT                   /id="PRO_0000430168"
FT   TRANSMEM        56..74
FT                   /note="Helical"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   81 AA;  8479 MW;  6DF1FB6388E2D25F CRC64;
     MNQSAQNYFS VQKPSETSSG PYTSPPPIGY PTRDAVVGDP PAAAVETNSK GVNPEAIMSC
     FSTCMECIFC CGVCSSLCTS E
 
 
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