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GRI_ARATH
ID   GRI_ARATH               Reviewed;         168 AA.
AC   Q9LNN7; Q6NQC7;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Protein GRIM REAPER {ECO:0000303|PubMed:19279211};
DE   AltName: Full=Stigma-specific STIG1-like protein GRI {ECO:0000303|PubMed:19279211};
DE   Contains:
DE     RecName: Full=GRIp {ECO:0000303|PubMed:25398910};
DE   Flags: Precursor;
GN   Name=GRI {ECO:0000303|PubMed:19279211};
GN   OrderedLocusNames=At1g53130 {ECO:0000312|Araport:AT1G53130};
GN   ORFNames=F8L10.2 {ECO:0000312|EMBL:AAF87867.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
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   [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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-168.
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   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GENE FAMILY.
RX   PubMed=19279211; DOI=10.1073/pnas.0808980106;
RA   Wrzaczek M., Brosche M., Kollist H., Kangasjarvi J.;
RT   "Arabidopsis GRI is involved in the regulation of cell death induced by
RT   extracellular ROS.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5412-5417(2009).
RN   [6]
RP   INTERACTION WITH PRK4 AND PRK5, AND PROTEOLYTIC PROCESSING OF GRIP.
RX   PubMed=25398910; DOI=10.15252/embj.201488582;
RA   Wrzaczek M., Vainonen J.P., Stael S., Tsiatsiani L., Help-Rinta-Rahko H.,
RA   Gauthier A., Kaufholdt D., Bollhoener B., Lamminmaeki A., Staes A.,
RA   Gevaert K., Tuominen H., Van Breusegem F., Helariutta Y., Kangasjaervi J.;
RT   "GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in
RT   Arabidopsis.";
RL   EMBO J. 34:55-66(2015).
CC   -!- FUNCTION: Involved in the regulation of cell death induced by
CC       extracellular reactive oxygen species (PubMed:19279211,
CC       PubMed:25398910). Only the processed peptide, and not the full length
CC       GRI can bind in vivo to the extracellular domain of the receptor PRK5
CC       (PubMed:25398910). The GRIp-induced cell death is superoxide and
CC       salicylic acid dependent (PubMed:19279211).
CC       {ECO:0000269|PubMed:19279211, ECO:0000269|PubMed:25398910}.
CC   -!- SUBUNIT: Interacts with PRK5 and to a lower extent with PRK4.
CC       {ECO:0000269|PubMed:25398910}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:19279211}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers, and at very low levels
CC       in leaves. {ECO:0000269|PubMed:19279211}.
CC   -!- SIMILARITY: Belongs to the STIG1 family. {ECO:0000305}.
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DR   EMBL; AC022520; AAF87867.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32894.1; -; Genomic_DNA.
DR   EMBL; AK176040; BAD43803.1; -; mRNA.
DR   EMBL; BT010530; AAQ65153.1; -; mRNA.
DR   PIR; H96571; H96571.
DR   RefSeq; NP_175721.1; NM_104192.3.
DR   AlphaFoldDB; Q9LNN7; -.
DR   STRING; 3702.AT1G53130.1; -.
DR   PaxDb; Q9LNN7; -.
DR   PRIDE; Q9LNN7; -.
DR   ProteomicsDB; 247220; -.
DR   EnsemblPlants; AT1G53130.1; AT1G53130.1; AT1G53130.
DR   GeneID; 841747; -.
DR   Gramene; AT1G53130.1; AT1G53130.1; AT1G53130.
DR   KEGG; ath:AT1G53130; -.
DR   Araport; AT1G53130; -.
DR   TAIR; locus:2037037; AT1G53130.
DR   eggNOG; ENOG502S52A; Eukaryota.
DR   HOGENOM; CLU_111795_1_1_1; -.
DR   InParanoid; Q9LNN7; -.
DR   OMA; KCEYGYC; -.
DR   OrthoDB; 1509365at2759; -.
DR   PhylomeDB; Q9LNN7; -.
DR   PRO; PR:Q9LNN7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LNN7; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0010942; P:positive regulation of cell death; IMP:TAIR.
DR   GO; GO:0080141; P:regulation of jasmonic acid biosynthetic process; IMP:TAIR.
DR   GO; GO:0080142; P:regulation of salicylic acid biosynthetic process; IMP:TAIR.
DR   GO; GO:0010193; P:response to ozone; IMP:TAIR.
DR   GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0048316; P:seed development; IMP:TAIR.
DR   InterPro; IPR006969; Stig1.
DR   PANTHER; PTHR33227; PTHR33227; 1.
DR   Pfam; PF04885; Stig1; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Glycoprotein; Plant defense; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..168
FT                   /note="Protein GRIM REAPER"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431926"
FT   PEPTIDE         68..78
FT                   /note="GRIp"
FT                   /id="PRO_0000431927"
FT   SITE            67..68
FT                   /note="Cleavage; by AMC9"
FT                   /evidence="ECO:0000269|PubMed:25398910"
FT   SITE            78..79
FT                   /note="Cleavage; by AMC9"
FT                   /evidence="ECO:0000269|PubMed:25398910"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   168 AA;  18607 MW;  B5079E3CEC668A09 CRC64;
     MVIKIPNTFI KATSLLSLIL YFLIIATSKS NSVLADEVVD QEDDPEYYIL DETPSILSNV
     TISSKTRLLV SHYKKIKKGM RCHVESYNIC NGVKANKGTS LLHCCKKHCR NVLGDRNNCG
     RCGHKCGFGQ RCCGGVCTYV NFNPNHCGKC TRKCASGVKC EYGYCGYA
 
 
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