JAL33_ARATH
ID JAL33_ARATH Reviewed; 300 AA.
AC O04311;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Jacalin-related lectin 33;
GN Name=JAL33; OrderedLocusNames=At3g16450; ORFNames=MDC8.8, T02O04.5;
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=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 [2]
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 [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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP IDENTIFICATION IN THE PYK10 COMPLEX, 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 [7]
RP STRUCTURE BY NMR OF 2-300, AND FUNCTION.
RX PubMed=19021763; DOI=10.1111/j.1742-4658.2008.06717.x;
RA Takeda M., Sugimori N., Torizawa T., Terauchi T., Ono A.M., Yagi H.,
RA Yamaguchi Y., Kato K., Ikeya T., Jee J., Guntert P., Aceti D.J.,
RA Markley J.L., Kainosho M.;
RT "Structure of the putative 32 kDa myrosinase-binding protein from
RT Arabidopsis (At3g16450.1) determined by SAIL-NMR.";
RL FEBS J. 275:5873-5884(2008).
CC -!- FUNCTION: Sugar-binding protein showing significant affinity for (Glc
CC alpha(1-4)Glc)(3) maltohexaose, (Glc alpha(1-6)Glc)(3) isomaltohexaose,
CC Gal alpha(1-4)Gal beta(1-4)Glc, GalNAc alpha(1-3)(Fuc alpha(1-2)) and
CC Gal beta(1-3)(Fuc alpha(1-4))GlcNAc beta(1-3)Gal beta(1-4)Glc.
CC {ECO:0000269|PubMed:19021763}.
CC -!- SUBUNIT: Component of the PYK10 complex, at least composed of
CC PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23, PBP1/JAL30, PBP2/JAL31,
CC JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.
CC {ECO:0000269|PubMed:18467340}.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
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DR EMBL; AP000373; BAB01144.1; -; Genomic_DNA.
DR EMBL; AC001645; AAB63632.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75817.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75818.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75819.1; -; Genomic_DNA.
DR EMBL; AF380655; AAK55736.1; -; mRNA.
DR EMBL; AY133546; AAM91376.1; -; mRNA.
DR EMBL; AK317360; BAH20032.1; -; mRNA.
DR RefSeq; NP_001030711.1; NM_001035634.3.
DR RefSeq; NP_188266.1; NM_112516.5.
DR RefSeq; NP_850596.1; NM_180265.4.
DR PDB; 2JZ4; NMR; -; A=2-300.
DR PDBsum; 2JZ4; -.
DR AlphaFoldDB; O04311; -.
DR BMRB; O04311; -.
DR SMR; O04311; -.
DR BioGRID; 6227; 2.
DR IntAct; O04311; 1.
DR STRING; 3702.AT3G16450.2; -.
DR PaxDb; O04311; -.
DR PRIDE; O04311; -.
DR ProteomicsDB; 250663; -.
DR EnsemblPlants; AT3G16450.1; AT3G16450.1; AT3G16450.
DR EnsemblPlants; AT3G16450.2; AT3G16450.2; AT3G16450.
DR EnsemblPlants; AT3G16450.3; AT3G16450.3; AT3G16450.
DR GeneID; 820893; -.
DR Gramene; AT3G16450.1; AT3G16450.1; AT3G16450.
DR Gramene; AT3G16450.2; AT3G16450.2; AT3G16450.
DR Gramene; AT3G16450.3; AT3G16450.3; AT3G16450.
DR KEGG; ath:AT3G16450; -.
DR Araport; AT3G16450; -.
DR TAIR; locus:2088369; AT3G16450.
DR HOGENOM; CLU_019384_1_0_1; -.
DR InParanoid; O04311; -.
DR OMA; VYAKDSQ; -.
DR OrthoDB; 980803at2759; -.
DR PhylomeDB; O04311; -.
DR EvolutionaryTrace; O04311; -.
DR PRO; PR:O04311; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O04311; baseline and differential.
DR Genevisible; O04311; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR CDD; cd09612; Jacalin; 2.
DR Gene3D; 2.100.10.30; -; 2.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 2.
DR SMART; SM00915; Jacalin; 2.
DR SUPFAM; SSF51101; SSF51101; 2.
DR PROSITE; PS51752; JACALIN_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Lectin; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9FGC5"
FT CHAIN 2..300
FT /note="Jacalin-related lectin 33"
FT /id="PRO_0000430392"
FT DOMAIN 2..146
FT /note="Jacalin-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT DOMAIN 154..297
FT /note="Jacalin-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9FGC5"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2JZ4"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 280..293
FT /evidence="ECO:0007829|PDB:2JZ4"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:2JZ4"
SQ SEQUENCE 300 AA; 32023 MW; 7548BE7F2CD206F7 CRC64;
MAQKVEAGGG AGGASWDDGV HDGVRKVHVG QGQDGVSSIN VVYAKDSQDV EGGEHGKKTL
LGFETFEVDA DDYIVAVQVT YDNVFGQDSD IITSITFNTF KGKTSPPYGL ETQKKFVLKD
KNGGKLVGFH GRAGEALYAL GAYFATTTTP VTPAKKLSAI GGDEGTAWDD GAYDGVKKVY
VGQGQDGISA VKFEYNKGAE NIVGGEHGKP TLLGFEEFEI DYPSEYITAV EGTYDKIFGS
DGLIITMLRF KTNKQTSAPF GLEAGTAFEL KEEGHKIVGF HGKASELLHQ FGVHVMPLTN
