SSL7_ARATH
ID SSL7_ARATH Reviewed; 371 AA.
AC Q9SD04;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein STRICTOSIDINE SYNTHASE-LIKE 7 {ECO:0000303|PubMed:10777701};
DE Short=AtSSL7 {ECO:0000303|PubMed:10777701};
DE Flags: Precursor;
GN Name=SSL7 {ECO:0000303|PubMed:10777701};
GN OrderedLocusNames=At3g51450 {ECO:0000312|Araport:AT3G51450};
GN ORFNames=F26O13.90 {ECO:0000312|EMBL:CAB63009.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10777701; DOI=10.1006/bbrc.2000.2598;
RA Fabbri M., Delp G., Schmidt O., Theopold U.;
RT "Animal and plant members of a gene family with similarity to alkaloid-
RT synthesizing enzymes.";
RL Biochem. Biophys. Res. Commun. 271:191-196(2000).
RN [7]
RP INDUCTION BY BIOTIC AND ABIOTIC STRESSES, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=19121120; DOI=10.1111/j.1438-8677.2008.00139.x;
RA Sohani M.M., Schenk P.M., Schultz C.J., Schmidt O.;
RT "Phylogenetic and transcriptional analysis of a strictosidine synthase-like
RT gene family in Arabidopsis thaliana reveals involvement in plant defence
RT responses.";
RL Plant Biol. 11:105-117(2009).
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- INDUCTION: By salicylic acid (SA), jasmonic acid (MJ), ethylene (ET),
CC wounding, and infection with the fungal pathogen A.brassicicola and
CC cucumber mosaic virus (CMV), both in local and systemic tissues.
CC {ECO:0000269|PubMed:19121120}.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
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DR EMBL; AL133452; CAB63009.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78794.1; -; Genomic_DNA.
DR EMBL; AY075676; AAL77683.1; -; mRNA.
DR EMBL; AY143926; AAN28865.1; -; mRNA.
DR EMBL; AK175245; BAD43008.1; -; mRNA.
DR EMBL; AK175564; BAD43327.1; -; mRNA.
DR EMBL; AY087851; AAM65404.1; -; mRNA.
DR PIR; T45776; T45776.
DR RefSeq; NP_190713.1; NM_115004.5.
DR AlphaFoldDB; Q9SD04; -.
DR SMR; Q9SD04; -.
DR IntAct; Q9SD04; 3.
DR STRING; 3702.AT3G51450.1; -.
DR PaxDb; Q9SD04; -.
DR PRIDE; Q9SD04; -.
DR ProteomicsDB; 245208; -.
DR EnsemblPlants; AT3G51450.1; AT3G51450.1; AT3G51450.
DR GeneID; 824308; -.
DR Gramene; AT3G51450.1; AT3G51450.1; AT3G51450.
DR KEGG; ath:AT3G51450; -.
DR Araport; AT3G51450; -.
DR TAIR; locus:2081875; AT3G51450.
DR eggNOG; KOG1520; Eukaryota.
DR HOGENOM; CLU_023267_0_2_1; -.
DR InParanoid; Q9SD04; -.
DR OMA; HDHKISH; -.
DR OrthoDB; 757814at2759; -.
DR PhylomeDB; Q9SD04; -.
DR BRENDA; 4.3.3.2; 399.
DR PRO; PR:Q9SD04; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD04; baseline and differential.
DR Genevisible; Q9SD04; AT.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR Pfam; PF03088; Str_synth; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Phosphoprotein; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..371
FT /note="Protein STRICTOSIDINE SYNTHASE-LIKE 7"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431594"
FT MOD_RES 303
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9SD07"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 371 AA; 41124 MW; 9A8921BBA1B35113 CRC64;
MPVLFSSRSL ILSIIVPLLI SIALYKLDTF DPAIVPSDAF TSSATSLPPL INDEFLTGAE
FIGVGLLNIP EDIAYHKESN LIYTGCVDGW VKRVKVADSV NDSVVEDWVN TGGRPLGIAF
GIHGEVIVAD VHKGLLNISG DGKKTELLTD EADGVKFKLT DAVTVADNGV LYFTDASYKY
TLNQLSLDML EGKPFGRLLS FDPTTRVTKV LLKDLYFANG ITISPDQTHL IFCETPMKRC
SKYYISEERV EVFTQSLPGY PDNIRYDGDG HYWIALPSGV TTLWNISLKY PFLRKLTAMV
AKYGVDLMFM ENAGVLQVDL DGNPIAYYHD PKLSHIATCD KIGKYLYCGS LSQSHILRLD
LLKYPAQNKK L
