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JAL36_ARATH
ID   JAL36_ARATH             Reviewed;         460 AA.
AC   Q9LIF8; Q6NQJ9;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Jacalin-related lectin 36;
GN   Name=JAL36; OrderedLocusNames=At3g21380; ORFNames=MHC9.6;
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   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].
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA   Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA   Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA   Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-460.
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   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   -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01088, ECO:0000305}.
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DR   EMBL; AP001305; BAB03051.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76503.1; -; Genomic_DNA.
DR   EMBL; AK221897; BAD94257.1; -; mRNA.
DR   EMBL; AK229853; BAF01682.1; -; mRNA.
DR   EMBL; BT010454; AAQ62874.1; -; mRNA.
DR   RefSeq; NP_001319607.1; NM_001338529.1.
DR   AlphaFoldDB; Q9LIF8; -.
DR   SMR; Q9LIF8; -.
DR   STRING; 3702.AT3G21380.1; -.
DR   iPTMnet; Q9LIF8; -.
DR   PaxDb; Q9LIF8; -.
DR   PRIDE; Q9LIF8; -.
DR   ProMEX; Q9LIF8; -.
DR   ProteomicsDB; 232291; -.
DR   EnsemblPlants; AT3G21380.1; AT3G21380.1; AT3G21380.
DR   GeneID; 821692; -.
DR   Gramene; AT3G21380.1; AT3G21380.1; AT3G21380.
DR   KEGG; ath:AT3G21380; -.
DR   Araport; AT3G21380; -.
DR   TAIR; locus:2089443; AT3G21380.
DR   HOGENOM; CLU_041730_0_0_1; -.
DR   InParanoid; Q9LIF8; -.
DR   OMA; FSIHAPK; -.
DR   OrthoDB; 596228at2759; -.
DR   PhylomeDB; Q9LIF8; -.
DR   PRO; PR:Q9LIF8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIF8; baseline and differential.
DR   Genevisible; Q9LIF8; AT.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd09612; Jacalin; 3.
DR   Gene3D; 2.100.10.30; -; 3.
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; 3.
DR   SMART; SM00915; Jacalin; 3.
DR   SUPFAM; SSF51101; SSF51101; 3.
DR   PROSITE; PS51752; JACALIN_LECTIN; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Lectin; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FGC5"
FT   CHAIN           2..460
FT                   /note="Jacalin-related lectin 36"
FT                   /id="PRO_0000430394"
FT   DOMAIN          1..131
FT                   /note="Jacalin-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   DOMAIN          145..289
FT                   /note="Jacalin-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   DOMAIN          313..457
FT                   /note="Jacalin-type lectin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT   REGION          34..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FGC5"
SQ   SEQUENCE   460 AA;  49724 MW;  5769468489DB48CA CRC64;
     MAAATMSWDD GKHMKVKRVQ ITYEDVINSI EAEYDGDTHN PHHHGTPGKK SDGVSLSPDE
     YITDVTGYYK TTGAEDAIAA LAFKTNKTEY GPYGNKTRNQ FSIHAPKDNQ IAGFQGISSN
     VLNSIDVHFA PLPSSSSSSS SLSQANKVDA QGGKGGTSWD DGAHDHVRRV YIGQGDSGVT
     YVKFEYEKDD KKESREHGKK TLLGAEVFEV DPDDYITSVE VQSDRIFGQD TEVITSLIFK
     TSKGKFSPPF GLEGSQKYEL KDKNGGKLVG FHGRVGGELL NALGAYFAPS SGRGTPSATQ
     PPGSAQPTGS AGAKKLEAKG GNVGNPWDDG PHEGVRKVYI GQGDSGVSYV KFVYDKDSKE
     VPGNDHGKRT LLAPEEFLLE YPNEYITSVE LNYDKIFGTE GEIITMLRFT TNKRTSPPFG
     LEGAKSVLLK EDGHKIVGFH GKAGADIIHQ VGVHVKPISK
 
 
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