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UniProtKB/Swiss-Prot entry Q0JF21


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AGI_ORYSJ
Primary accession number Q0JF21
Secondary accession numbers P11219 Q7FZU3 Q7XRY8 Q9SBW5 Q9XFF3 Q9XFF4
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on October 3, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 17)
Name and origin of the protein
Protein name Lectin [Precursor]
Synonym Agglutinin
Contains Lectin 10 kDa peptide
Lectin 8 kDa peptide
Gene name
OrderedLocusNames: Os04g0173800, LOC_Os04g09390
ORFNames: OSJNBb0015C06.8
From
Oryza sativa subsp. japonica (Rice) [TaxID: 39947] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Ehrhartoideae; Oryzeae; Oryza.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
STRAIN=cv. Lemont;
DOI=10.1105/tpc.1.5.541; PubMed=2535550 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkins T.A., Raikhel N.V.;
"Expression of rice lectin is governed by two temporally and spatially regulated mRNAs in developing embryos.";
Plant Cell 1:541-549(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1038/nature01183; PubMed=12447439 [NCBI, ExPASy, EBI, Israel, Japan]
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B.;
"Sequence and analysis of rice chromosome 4.";
Nature 420:316-320(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1038/nature03895; PubMed=16100779 [NCBI, ExPASy, EBI, Israel, Japan]
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
DOI=10.1101/gr.5509507; PubMed=17210932 [NCBI, ExPASy, EBI, Israel, Japan]
The rice annotation project (RAP);
"Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana.";
Genome Res. 17:175-183(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-227.
Hao Z., Liu Q., Shen D.;
"Molecular evolution of lectin gene in the genus Oryza.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
PRELIMINARY PROTEIN SEQUENCE OF 123-157.
Chapot M.-P., Peumans W.J., Strosberg A.D.;
"Extensive homologies between lectins from non-leguminous plants.";
FEBS Lett. 195:231-234(1986).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M24504; AAA20873.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662990; CAE02230.2; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008210; BAF14066.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF140679; AAD27887.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF140682; AAD27890.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23616; A23616.
JQ1102; LNRZ.
RefSeq NP_001052152.1; -.
UniGene Os.54304
3D structure databases
HSSP P10968; 2CWG. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR Q0JF21; 29-197.
ModBase Q0JF21.
Organism-specific databases
Gramene P11219; -.
Family and domain databases
InterPro IPR001002; Chitin_bd_1.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.30.60.10; Chitin_bd_1; 4.
PANTHER PTHR22595; Glyco_hydro_19_cat; 1.
Pfam PF00187; Chitin_bind_1; 4.
Pfam graphical view of domain structure.
PRINTS PR00451; CHITINBINDNG.
ProDom PD000609; Chitin_binding_1; 4.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00270; ChtBD1; 4.
SMART graphical view of domain structure.
PROSITE PS00026; CHIT_BIND_I_1; 4.
PS50941; CHIT_BIND_I_2; 4.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q0JF21.
Genome annotation databases
GeneID 4335068; -.
KEGG osa:4335068; -.
Other
ProtoNet Q0JF21.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chitin-binding; Direct protein sequencing; Glycoprotein; Lectin; Pyrrolidone carboxylic acid; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28      
CHAIN   29   201  173     Lectin. PRO_0000005262
CHAIN   29   122  94     Lectin 10 kDa peptide. PRO_0000005263
CHAIN   123   201  79     Lectin 8 kDa peptide. PRO_0000005264
PROPEP   202   227  26      PRO_0000005265
DOMAIN   29    70  42     Chitin-binding type-1 1. 
DOMAIN   71   113  43     Chitin-binding type-1 2. 
DOMAIN   114   156  43     Chitin-binding type-1 3. 
DOMAIN   157   199  43     Chitin-binding type-1 4. 
REGION   38    40  3     Substrate binding (By similarity). 
REGION   90   101  12     Substrate binding (By similarity). 
REGION   142   143  2     Substrate binding (By similarity). 
MOD_RES   29    29        Pyrrolidone carboxylic acid. 
CARBOHYD   211   211        N-linked (GlcNAc...) (Potential). 
DISULFID   31    46        By similarity. 
DISULFID   40    52        By similarity. 
DISULFID   45    59        By similarity. 
DISULFID   63    68        By similarity. 
DISULFID   74    89        By similarity. 
DISULFID   83    95        By similarity. 
DISULFID   88   102        By similarity. 
DISULFID   106   111        By similarity. 
DISULFID   117   132        By similarity. 
DISULFID   126   138        By similarity. 
DISULFID   131   145        By similarity. 
DISULFID   149   154        By similarity. 
DISULFID   160   175        By similarity. 
DISULFID   169   181        By similarity. 
DISULFID   174   188        By similarity. 
DISULFID   192   197        By similarity. 
CONFLICT   119   119        R -> S (in Ref. 5; AAD27887). 
Sequence information
Length: 227 AA [This is the length of the unprocessed precursor] Molecular weight: 22796 Da [This is the MW of the unprocessed precursor] CRC64: 691EB39F6690BAF1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTMTSTTTKA MAMAAAVLAA AAVAATNAQT CGKQNDGMIC PHNLCCSQFG YCGLGRDYCG 

        70         80         90        100        110        120 
TGCQSGACCS SQRCGSQGGG ATCSNNQCCS QYGYCGFGSE YCGSGCQNGP CRADIKCGRN 

       130        140        150        160        170        180 
ANGELCPNNM CCSQWGYCGL GSEFCGNGCQ SGACCPEKRC GKQAGGDKCP NNFCCSAGGY 

       190        200        210        220 
CGLGGNYCGS GCQSGGCYKG GDGMAAILAN NQSVSFEGII ESVAELV 

Q0JF21 in FASTA format

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