AGI_ORYSI
ID AGI_ORYSI Reviewed; 227 AA.
AC Q01MB6; A2XQZ8; P11219; Q7FZU3; Q7XRY8; Q9SBW5; Q9XFF3; Q9XFF4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Lectin;
DE AltName: Full=Agglutinin;
DE Contains:
DE RecName: Full=Lectin 10 kDa peptide;
DE Contains:
DE RecName: Full=Lectin 8 kDa peptide;
DE Flags: Precursor;
GN ORFNames=OsI_014491, OSIGBa0132O24;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-227.
RA Hao Z., Liu Q., Shen D.;
RT "Molecular evolution of lectin gene in the genus Oryza.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: N-acetyl-D-glucosamine binding lectin.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH66099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR855052; CAH66099.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF140681; AAD27889.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01MB6; -.
DR SMR; Q01MB6; -.
DR STRING; 39946.Q01MB6; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR EnsemblPlants; BGIOSGA015997-TA; BGIOSGA015997-PA; BGIOSGA015997.
DR Gramene; BGIOSGA015997-TA; BGIOSGA015997-PA; BGIOSGA015997.
DR HOGENOM; CLU_112193_0_0_1; -.
DR OMA; AGNCGPQ; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 4.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR Pfam; PF00187; Chitin_bind_1; 4.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 4.
DR SUPFAM; SSF57016; SSF57016; 4.
DR PROSITE; PS00026; CHIT_BIND_I_1; 4.
DR PROSITE; PS50941; CHIT_BIND_I_2; 4.
PE 3: Inferred from homology;
KW Chitin-binding; Disulfide bond; Glycoprotein; Lectin;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..201
FT /note="Lectin"
FT /id="PRO_0000293087"
FT CHAIN 29..122
FT /note="Lectin 10 kDa peptide"
FT /id="PRO_0000293088"
FT CHAIN 123..201
FT /note="Lectin 8 kDa peptide"
FT /id="PRO_0000293089"
FT PROPEP 202..227
FT /evidence="ECO:0000250"
FT /id="PRO_0000293090"
FT DOMAIN 29..70
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 71..113
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 114..156
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 157..199
FT /note="Chitin-binding type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142..143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 40..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 45..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 63..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 74..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 83..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 88..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 106..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 117..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 126..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 131..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 149..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 160..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 169..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 174..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 192..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT CONFLICT 119
FT /note="S -> R (in Ref. 3; AAD27889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 22726 MW; 0273048317C0AEA0 CRC64;
MTMTSTTTKA MAMAAAVLAA AAVAATNAQT CGKQNDGMIC PHNLCCSQFG YCGLGRDYCG
TGCQSGACCS SQRCGSQGGG ATCSNNQCCS QYGYCGFGSE YCGSGCQNGP CRADIKCGSN
ANGELCPNNM CCSQWGYCGL GSEFCGNGCQ SGACCPEKRC GKQAGGDKCP NNFCCSAGGY
CGLGGNYCGS GCQSGGCYKG GDGMAAILAN NQSVSFEGII ESVAELV
