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AFP1_ARATH
ID   AFP1_ARATH              Reviewed;         345 AA.
AC   Q9LQ98; Q8L8S9; Q9C980;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ninja-family protein AFP1;
DE   AltName: Full=ABI five-binding protein 1;
DE            Short=ABI5-binding protein 1;
GN   Name=AFP1; Synonyms=AFP; OrderedLocusNames=At1g69260;
GN   ORFNames=F23O10.16, F4N2.22;
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=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;
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].
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, INTERACTION
RP   WITH ABI5/DPBF1, AND DISRUPTION PHENOTYPE.
RX   PubMed=12569131; DOI=10.1101/gad.1055803;
RA   Lopez-Molina L., Mongrand S., Kinoshita N., Chua N.-H.;
RT   "AFP is a novel negative regulator of ABA signaling that promotes ABI5
RT   protein degradation.";
RL   Genes Dev. 17:410-418(2003).
RN   [6]
RP   GENE FAMILY, NOMENCLATURE, SUBUNIT, INTERACTION WITH ABI5/DPBF1; DPBF2;
RP   AREB3/DPBF3; ABF1; ABF3/DPBF5 AND ABF4/AREB2, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18484180; DOI=10.1007/s11103-008-9344-2;
RA   Garcia M.E., Lynch T.J., Peeters J., Snowden C., Finkelstein R.R.;
RT   "A small plant-specific protein family of ABI five binding proteins (AFPs)
RT   regulates stress response in germinating Arabidopsis seeds and seedlings.";
RL   Plant Mol. Biol. 67:643-658(2008).
CC   -!- FUNCTION: Acts as a negative regulator of abscisic acid (ABA) response
CC       during germination through the ubiquitin-mediated proteolysis of
CC       ABI5/DPBF1. {ECO:0000269|PubMed:12569131}.
CC   -!- SUBUNIT: Forms a heterodimer with AFP2. Interacts with ABI5/DPBF1,
CC       DPBF2, AREB3/DPBF3, ABF1, ABF3/DPBF5 and ABF4/AREB2.
CC       {ECO:0000269|PubMed:12569131, ECO:0000269|PubMed:18484180}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12569131}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo during the latest stages of
CC       seed maturation. {ECO:0000269|PubMed:12569131}.
CC   -!- INDUCTION: Up-regulated by abscisic acid (ABA), glucose and salt.
CC       {ECO:0000269|PubMed:12569131, ECO:0000269|PubMed:18484180}.
CC   -!- DISRUPTION PHENOTYPE: Exhibits slight hypersensitivity to abscisic acid
CC       (ABA), salt and osmotic stress. {ECO:0000269|PubMed:12569131,
CC       ECO:0000269|PubMed:18484180}.
CC   -!- SIMILARITY: Belongs to the Ninja family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52486.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAM67141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC008262; AAF27062.1; -; Genomic_DNA.
DR   EMBL; AC018364; AAG52486.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE34903.1; -; Genomic_DNA.
DR   EMBL; AY136357; AAM97023.1; -; mRNA.
DR   EMBL; BT000199; AAN15518.1; -; mRNA.
DR   EMBL; AY088834; AAM67141.1; ALT_INIT; mRNA.
DR   PIR; F96716; F96716.
DR   RefSeq; NP_564956.1; NM_105593.5.
DR   AlphaFoldDB; Q9LQ98; -.
DR   IntAct; Q9LQ98; 10.
DR   STRING; 3702.AT1G69260.1; -.
DR   iPTMnet; Q9LQ98; -.
DR   PaxDb; Q9LQ98; -.
DR   PRIDE; Q9LQ98; -.
DR   ProteomicsDB; 244843; -.
DR   EnsemblPlants; AT1G69260.1; AT1G69260.1; AT1G69260.
DR   GeneID; 843257; -.
DR   Gramene; AT1G69260.1; AT1G69260.1; AT1G69260.
DR   KEGG; ath:AT1G69260; -.
DR   Araport; AT1G69260; -.
DR   TAIR; locus:2026413; AT1G69260.
DR   eggNOG; ENOG502QW6K; Eukaryota.
DR   HOGENOM; CLU_034695_0_0_1; -.
DR   InParanoid; Q9LQ98; -.
DR   OMA; CVCHANF; -.
DR   OrthoDB; 1080495at2759; -.
DR   PhylomeDB; Q9LQ98; -.
DR   PRO; PR:Q9LQ98; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQ98; baseline and differential.
DR   Genevisible; Q9LQ98; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
DR   InterPro; IPR032310; NINJA_B.
DR   InterPro; IPR031307; Ninja_fam.
DR   InterPro; IPR012463; Ninja_motif.
DR   InterPro; IPR032308; TDBD.
DR   PANTHER; PTHR31413; PTHR31413; 1.
DR   Pfam; PF07897; EAR; 1.
DR   Pfam; PF16136; NINJA_B; 1.
DR   Pfam; PF16135; TDBD; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Ninja-family protein AFP1"
FT                   /id="PRO_0000369614"
FT   REGION          114..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        84..85
FT                   /note="HH -> R (in Ref. 4; AAM67141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="L -> F (in Ref. 4; AAM67141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="G -> V (in Ref. 4; AAM67141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="T -> N (in Ref. 4; AAM67141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="P -> Q (in Ref. 4; AAM67141)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  37531 MW;  61E74572437E332A CRC64;
     MAEANERSKE MARSNSCVFP RDLLQRFISN SVEGEDDDEE EDDDEIELNL GLSLGGRFGV
     DKSNKLVRSS SVVVTMPLFR EDHHHHQAAA MITTKVSTET VAGATRGTGL MRTTSLPAES
     EEEWRKRKEM QTLRRMAAKR RRSEKLRTGV GGGNSNNPEE AATATASRRR GRPSSGLPRW
     SATANKSGLL RQHSAGLDSL QVSGESLGGG RAAGSSSSVS ELETKASSDE ARSLPSTTQP
     QQETTTKPTN RLRRLSSVDM NMKMEPQGKG KSEMPCVFTK GDGPNGKRVD GILYRYGSGE
     EVRIMCVCHG DFLSPADFVK HAGGPHVDHP LRHIVVNTSS PSNLL
 
 
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