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NSP1_MEDTR
ID   NSP1_MEDTR              Reviewed;         554 AA.
AC   Q4VYC8; G7L7I4; Q4VYC5; Q4VYC6;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Protein NODULATION SIGNALING PATHWAY 1 {ECO:0000303|PubMed:15961669};
GN   Name=NSP1 {ECO:0000303|PubMed:15961669};
GN   OrderedLocusNames=MTR_8g020840 {ECO:0000312|EMBL:AET01770.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF
RP   240-ARG--GLU-554 AND 488-TRP--GLU-554, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15961669; DOI=10.1126/science.1111025;
RA   Smit P., Raedts J., Portyanko V., Debelle F., Gough C., Bisseling T.,
RA   Geurts R.;
RT   "NSP1 of the GRAS protein family is essential for rhizobial Nod factor-
RT   induced transcription.";
RL   Science 308:1789-1791(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA   Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA   Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA   De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA   Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA   Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA   Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA   Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA   Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA   Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA   Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA   Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA   Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA   O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA   Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA   Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA   Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA   Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA   White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA   Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA   Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=23077241; DOI=10.1104/pp.112.203190;
RA   Cerri M.R., Frances L., Laloum T., Auriac M.C., Niebel A., Oldroyd G.E.,
RA   Barker D.G., Fournier J., de Carvalho-Niebel F.;
RT   "Medicago truncatula ERN transcription factors: regulatory interplay with
RT   NSP1/NSP2 GRAS factors and expression dynamics throughout rhizobial
RT   infection.";
RL   Plant Physiol. 160:2155-2172(2012).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22039214; DOI=10.1105/tpc.111.089771;
RA   Liu W., Kohlen W., Lillo A., Op den Camp R., Ivanov S., Hartog M.,
RA   Limpens E., Jamil M., Smaczniak C., Kaufmann K., Yang W.C., Hooiveld G.J.,
RA   Charnikhova T., Bouwmeester H.J., Bisseling T., Geurts R.;
RT   "Strigolactone biosynthesis in Medicago truncatula and rice requires the
RT   symbiotic GRAS-type transcription factors NSP1 and NSP2.";
RL   Plant Cell 23:3853-3865(2011).
RN   [6]
RP   FUNCTION.
RX   PubMed=26503135; DOI=10.1186/s12870-015-0651-x;
RA   van Zeijl A., Liu W., Xiao T.T., Kohlen W., Yang W.C., Bisseling T.,
RA   Geurts R.;
RT   "The strigolactone biosynthesis gene DWARF27 is co-opted in rhizobium
RT   symbiosis.";
RL   BMC Plant Biol. 15:260-260(2015).
CC   -!- FUNCTION: Transcriptional regulator essential for Nod-factor-induced
CC       gene expression (PubMed:15961669). Acts downstream of calcium spiking
CC       (PubMed:15961669). May be a target of DMI3, a calcium/calmodulin-
CC       dependent protein kinase (CCaMK) (PubMed:15961669). Is essential for
CC       Nod factor-elicited expression of ERN1 (PubMed:23077241). Transcription
CC       factor involved in the control of strigolactone biosynthesis in roots
CC       through the activation of the beta-carotene isomerase D27, which
CC       participates in a pathway leading to biosynthesis of strigolactones
CC       (PubMed:22039214, PubMed:26503135). {ECO:0000269|PubMed:15961669,
CC       ECO:0000269|PubMed:22039214, ECO:0000269|PubMed:23077241,
CC       ECO:0000269|PubMed:26503135}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in epidermal and cortical root cells.
CC       {ECO:0000269|PubMed:15961669}.
CC   -!- INDUCTION: Not induced after treatment with Sinorhizobium meliloti.
CC       {ECO:0000269|PubMed:15961669}.
CC   -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000305}.
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DR   EMBL; AJ972478; CAJ00010.1; -; Genomic_DNA.
DR   EMBL; AJ972473; CAJ00005.1; -; Genomic_DNA.
DR   EMBL; AJ972480; CAJ00012.1; -; Genomic_DNA.
DR   EMBL; AJ972481; CAJ00013.1; -; Genomic_DNA.
DR   EMBL; CM001224; AET01770.1; -; Genomic_DNA.
DR   RefSeq; XP_003627294.1; XM_003627246.2.
DR   AlphaFoldDB; Q4VYC8; -.
DR   SMR; Q4VYC8; -.
DR   STRING; 3880.AET01770; -.
DR   PRIDE; Q4VYC8; -.
DR   EnsemblPlants; AET01770; AET01770; MTR_8g020840.
DR   GeneID; 11434050; -.
DR   Gramene; AET01770; AET01770; MTR_8g020840.
DR   KEGG; mtr:MTR_8g020840; -.
DR   eggNOG; ENOG502QSHA; Eukaryota.
DR   HOGENOM; CLU_011924_5_1_1; -.
DR   OMA; TEPRFFQ; -.
DR   OrthoDB; 454341at2759; -.
DR   Proteomes; UP000002051; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR   InterPro; IPR030015; SCL29/NSP1.
DR   InterPro; IPR005202; TF_GRAS.
DR   PANTHER; PTHR31636; PTHR31636; 1.
DR   PANTHER; PTHR31636:SF243; PTHR31636:SF243; 1.
DR   Pfam; PF03514; GRAS; 1.
DR   PROSITE; PS50985; GRAS; 1.
PE   1: Evidence at protein level;
KW   Nodulation; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..554
FT                   /note="Protein NODULATION SIGNALING PATHWAY 1"
FT                   /id="PRO_0000132232"
FT   DOMAIN          159..548
FT                   /note="GRAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          76..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..227
FT                   /note="Leucine repeat I (LRI)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          246..315
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          331..373
FT                   /note="Leucine repeat II (LRII)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          383..468
FT                   /note="PFYRE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          471..548
FT                   /note="SAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           281..285
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   COMPBIAS        76..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         240..554
FT                   /note="Missing: In nsp1-1; loss of nodulation."
FT                   /evidence="ECO:0000269|PubMed:15961669"
FT   MUTAGEN         488..554
FT                   /note="Missing: In nsp1-2; loss of nodulation."
FT                   /evidence="ECO:0000269|PubMed:15961669"
SQ   SEQUENCE   554 AA;  61827 MW;  B87E941794563923 CRC64;
     MTMEPNPTSD HILDWLEGSV SFFPSFLDDP YNNGYIHEYE IWNQNQDISN QYQIDANTNS
     SNATNSTTNI VAASTTTSTT SLEPNSFNNI PFSDLPKKRN AEDELSLKKQ PQNQKNKRLK
     SRPMNESDNG DAALEGTVVR KSGGNKKGAA KANGSNSNNG NNKDGRWAEQ LLNPCAVAIT
     GGNLNRVQHL LYVLHELAST TGDANHRLAA HGLRALTHHL SSSSSSTPSG TITFASTEPR
     FFQKSLLKFY EFSPWFSFPN NIANASILQV LAEEPNNLRT LHILDIGVSH GVQWPTFLEA
     LSRRPGGPPP LVRLTVVNAS SSTENDQNME TPFSIGPCGD TFSSGLLGYA QSLNVNLQIK
     KLDNHPLQTL NAKSVDTSSD ETLIVCAQFR LHHLNHNNPD ERSEFLKVLR GMEPKGVILS
     ENNMECCCSS CGDFATGFSR RVEYLWRFLD STSSAFKNRD SDERKMMEGE AAKALTNQRE
     MNERREKWCE RMKEAGFAGE VFGEDAIDGG RALLRKYDNN WEMKVEENST SVELWWKSQP
     VSFCSLWKLD KQPE
 
 
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