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NLTL1_ORYSJ
ID   NLTL1_ORYSJ             Reviewed;         178 AA.
AC   Q6ASY2; A0A0P0VYZ1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Non-specific lipid transfer protein-like 1;
DE            Short=OsLTPL1;
DE   Flags: Precursor;
GN   Name=LTPL1; OrderedLocusNames=Os03g0385400, LOC_Os03g26820;
GN   ORFNames=B1246D11.7;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-38 AND 120-134, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Koshihikari; TISSUE=Aleurone;
RX   PubMed=15653800; DOI=10.1093/pcp/pch208;
RA   Mashiguchi K., Yamaguchi I., Suzuki Y.;
RT   "Isolation and identification of glycosylphosphatidylinositol-anchored
RT   arabinogalactan proteins and novel beta-glucosyl Yariv-reactive proteins
RT   from seeds of rice (Oryza sativa).";
RL   Plant Cell Physiol. 45:1817-1829(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain membrane {ECO:0000305};
CC       Lipid-anchor, GPI-anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       seeds. {ECO:0000269|PubMed:15653800}.
CC   -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC       residues are glycosylated with arabinogalactan. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; EU282465; ABX83037.1; -; mRNA.
DR   EMBL; AC146521; AAT85306.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF96304.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12166.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS84470.1; -; Genomic_DNA.
DR   EMBL; AK068223; BAG90809.1; -; mRNA.
DR   EMBL; AK070241; BAG91850.1; -; mRNA.
DR   RefSeq; XP_015633082.1; XM_015777596.1.
DR   AlphaFoldDB; Q6ASY2; -.
DR   PaxDb; Q6ASY2; -.
DR   PRIDE; Q6ASY2; -.
DR   EnsemblPlants; Os03t0385400-01; Os03t0385400-01; Os03g0385400.
DR   GeneID; 4332993; -.
DR   Gramene; Os03t0385400-01; Os03t0385400-01; Os03g0385400.
DR   KEGG; osa:4332993; -.
DR   eggNOG; ENOG502R3GD; Eukaryota.
DR   HOGENOM; CLU_089796_5_2_1; -.
DR   InParanoid; Q6ASY2; -.
DR   OMA; KCLAPAP; -.
DR   OrthoDB; 1614569at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q6ASY2; OS.
DR   GO; GO:0032578; C:aleurone grain membrane; IDA:UniProtKB.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR043325; LTSS.
DR   PANTHER; PTHR33044; PTHR33044; 1.
DR   Pfam; PF14368; LTP_2; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Hydrolase; Hydroxylation; Lipid-binding; Lipoprotein; Membrane; Protease;
KW   Proteoglycan; Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:15653800"
FT   CHAIN           27..149
FT                   /note="Non-specific lipid transfer protein-like 1"
FT                   /id="PRO_0000397898"
FT   PROPEP          150..178
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000397899"
FT   LIPID           149
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..68
FT                   /evidence="ECO:0000255"
FT   DISULFID        69..110
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   178 AA;  16899 MW;  D1F60224FF88B7B7 CRC64;
     MAVAARAAAV ACLLVVGLAA VAGVDGATAS SPAPAPAVDC TAEALKLADC LDYVTPGKTA
     PSRPSKLCCG EVKGALKDSA AVGCLCAAFT SKTLPLPINI TRALHLPAAC GADASAFSKC
     LAPAPSPSVA PGTSSGSGGA AAAPAKGAAA ARSPMASTTA VLVVAAAVAA PLLAFFHF
 
 
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