JAL21_ARATH
ID JAL21_ARATH Reviewed; 471 AA.
AC O49326; F4IUU4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Nitrile-specifier protein 2;
DE Short=AtNSP2;
DE AltName: Full=Jacalin-related lectin 21;
GN Name=NSP2; Synonyms=JAL21; OrderedLocusNames=At2g33070; ORFNames=F25I18.19;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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).
RN [5]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O49326-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O49326-2; Sequence=VSP_056709;
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}.
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DR EMBL; AC002334; AAC04913.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08780.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08781.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08782.1; -; Genomic_DNA.
DR EMBL; AY070077; AAL49772.1; -; mRNA.
DR EMBL; AY091331; AAM14270.1; -; mRNA.
DR PIR; A84741; A84741.
DR RefSeq; NP_001031468.1; NM_001036391.1. [O49326-1]
DR RefSeq; NP_001189663.1; NM_001202734.1. [O49326-2]
DR RefSeq; NP_180866.1; NM_128867.3. [O49326-1]
DR AlphaFoldDB; O49326; -.
DR SMR; O49326; -.
DR STRING; 3702.AT2G33070.3; -.
DR iPTMnet; O49326; -.
DR PaxDb; O49326; -.
DR PRIDE; O49326; -.
DR ProteomicsDB; 250656; -. [O49326-1]
DR EnsemblPlants; AT2G33070.1; AT2G33070.1; AT2G33070. [O49326-1]
DR EnsemblPlants; AT2G33070.2; AT2G33070.2; AT2G33070. [O49326-1]
DR EnsemblPlants; AT2G33070.3; AT2G33070.3; AT2G33070. [O49326-2]
DR GeneID; 817869; -.
DR Gramene; AT2G33070.1; AT2G33070.1; AT2G33070. [O49326-1]
DR Gramene; AT2G33070.2; AT2G33070.2; AT2G33070. [O49326-1]
DR Gramene; AT2G33070.3; AT2G33070.3; AT2G33070. [O49326-2]
DR KEGG; ath:AT2G33070; -.
DR Araport; AT2G33070; -.
DR TAIR; locus:2046560; AT2G33070.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; O49326; -.
DR OMA; FCGRELD; -.
DR OrthoDB; 933937at2759; -.
DR PhylomeDB; O49326; -.
DR PRO; PR:O49326; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O49326; baseline and differential.
DR Genevisible; O49326; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; 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; 1.
DR PIRSF; PIRSF038118; Myrosinase-db_jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Kelch repeat; Lectin; Reference proteome; Repeat.
FT CHAIN 1..471
FT /note="Nitrile-specifier protein 2"
FT /id="PRO_0000363143"
FT DOMAIN 2..144
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REPEAT 47..94
FT /note="Kelch 1"
FT REPEAT 178..226
FT /note="Kelch 2"
FT REPEAT 231..277
FT /note="Kelch 3"
FT REPEAT 281..330
FT /note="Kelch 4"
FT REPEAT 332..379
FT /note="Kelch 5"
FT REPEAT 381..435
FT /note="Kelch 6"
FT VAR_SEQ 156
FT /note="K -> KVV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056709"
SQ SEQUENCE 471 AA; 51215 MW; 880B8B24E24E2BD8 CRC64;
MVQKVEARGG EIGDVWDDGA YDGVRKVYVG QGEDGIAFVK FEYVNGSQEV VGDERGKKTL
LGAEEFEVDP DDYIVYVEGY HEKVFGVTTK EIISTLTFKT YKGKTSPPFG IVSGTKFVLQ
GGKIVGFHGR STDVLHSLGA YISSPATPKL RGKWIKVEQK GEGPGPRCSH DIAQVGNKIF
SFGGELTPNQ PIDKHLYVFD LETRTWSISP ATGDVPNLSC LGVRMVSIGS SLYVFGGRDA
SRKYNGFYSF DTTKNEWKLL TPVEQGPTPR SFHSMTADEN NVYVFGGVSA TVRLKTLDAY
NIVDHKWVQC STPGGSCSVR GGAGLEVVQG KVWVVYGFNG CEVDDVHCYD PAQDKWTQVE
TFGEKPCARS VFASAVVGKH ILVFGGEIAM DPKAHEGPGQ LSGGTFALDT ETLKWEKLDK
LGEEEETPSI RGWSASTTGT IDGKKGLVMF GGKAQTNDRF GDLFFYGVDS A
