JAL27_ARATH
ID JAL27_ARATH Reviewed; 467 AA.
AC O04318; Q8GX12;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Nitrile-specifier protein 3;
DE Short=AtNSP3;
DE AltName: Full=Jacalin-related lectin 27;
GN Name=NSP3; Synonyms=JAL27; OrderedLocusNames=At3g16390; ORFNames=T02O04.12;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 369-467.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-467.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18987211; DOI=10.1104/pp.108.130732;
RA Burow M., Losansky A., Muller R., Plock A., Kliebenstein D.J.,
RA Wittstock U.;
RT "The genetic basis of constitutive and herbivore-induced ESP-independent
RT nitrile formation in Arabidopsis.";
RL Plant Physiol. 149:561-574(2009).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18467340; DOI=10.1093/pcp/pcn075;
RA Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.;
RT "Antagonistic jacalin-related lectins regulate the size of ER body-type
RT beta-glucosidase complexes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:969-980(2008).
CC -!- FUNCTION: Promotes simple nitriles, but not epithionitrile or
CC thiocyanate formation. Converts allylglucosinolate and
CC benzylglucosinolate to their corresponding simple nitriles in the
CC presence of myrosinase. {ECO:0000269|PubMed:18987211}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18987211}.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC001645; AAB63639.1; -; Genomic_DNA.
DR EMBL; AP000373; BAB01137.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75806.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65032.1; -; Genomic_DNA.
DR EMBL; AK118502; BAC43106.1; ALT_INIT; mRNA.
DR EMBL; BT004661; AAO42907.1; -; mRNA.
DR RefSeq; NP_001327031.1; NM_001338231.1.
DR RefSeq; NP_566545.1; NM_112510.3.
DR AlphaFoldDB; O04318; -.
DR SMR; O04318; -.
DR STRING; 3702.AT3G16390.1; -.
DR iPTMnet; O04318; -.
DR MetOSite; O04318; -.
DR PaxDb; O04318; -.
DR PRIDE; O04318; -.
DR ProteomicsDB; 232290; -.
DR EnsemblPlants; AT3G16390.1; AT3G16390.1; AT3G16390.
DR EnsemblPlants; AT3G16390.2; AT3G16390.2; AT3G16390.
DR GeneID; 820886; -.
DR Gramene; AT3G16390.1; AT3G16390.1; AT3G16390.
DR Gramene; AT3G16390.2; AT3G16390.2; AT3G16390.
DR KEGG; ath:AT3G16390; -.
DR Araport; AT3G16390; -.
DR TAIR; locus:2088289; AT3G16390.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_030461_2_0_1; -.
DR InParanoid; O04318; -.
DR OMA; WIKVEQN; -.
DR OrthoDB; 277265at2759; -.
DR PhylomeDB; O04318; -.
DR PRO; PR:O04318; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O04318; baseline and differential.
DR Genevisible; O04318; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0019762; P:glucosinolate catabolic process; IDA:TAIR.
DR GO; GO:0080028; P:nitrile biosynthetic process; IDA:TAIR.
DR CDD; cd09612; Jacalin; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR035429; NSP1/2/3.
DR Pfam; PF01419; Jacalin; 1.
DR Pfam; PF01344; Kelch_1; 3.
DR PIRSF; PIRSF038118; Myrosinase-db_jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Kelch repeat; Lectin; Reference proteome; Repeat.
FT CHAIN 1..467
FT /note="Nitrile-specifier protein 3"
FT /id="PRO_0000363144"
FT DOMAIN 2..143
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REPEAT 47..93
FT /note="Kelch 1"
FT REPEAT 177..225
FT /note="Kelch 2"
FT REPEAT 230..276
FT /note="Kelch 3"
FT REPEAT 280..329
FT /note="Kelch 4"
FT REPEAT 331..375
FT /note="Kelch 5"
FT REPEAT 379..434
FT /note="Kelch 6"
SQ SEQUENCE 467 AA; 51232 MW; 6B65312E9B563AE5 CRC64;
MAQKLVAQGG ETGDVWDDGV YDNVTKVYVG QGQYGIAFVK FEYANGSEVV VGDEHGEKTE
LGVEEFEIDS DDYIVYVEGY REKVSDMTSE MITFLSFKTS KGKTSQPIVK KPGVKFVLHG
GKIVGFHGRS TDVLHSLGAY VSLPSTPKLL GNWIKVEQNG EGPGLRCSHG IAQVGNKIYS
FGGELIPNQP IDKHLYVFDL ETRTWSIAPA TGDVPHLSCL GVRMVSVGST LYTFGGRDFS
RQYNGFYSFD TTTNEWKLLT PVEEGPTPRS FHSMAADEEN VYVFGGVGAM DRIKTLDSYN
IVDKTWFHCS NPGDSFSIRG GAGLEVVQGK VWIVYGFNGC EVDDVHFYDP AEDKWTQVET
FGVKPNERSV FASAAIGKHI VIFGGEIAMD PRAHVGPGQL IDGTFALDTE TLQWERLDKF
EGTPSSRGWT ASTTGTIDGK KGLVMHGGKA PTNDRFDDLF FYGIDSV
