ID   SSL12_ARATH             Reviewed;         335 AA.
AC   P94111; Q9C9C3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Protein STRICTOSIDINE SYNTHASE-LIKE 12 {ECO:0000303|PubMed:10777701};
DE            Short=AtSSL12 {ECO:0000303|PubMed:10777701};
DE            EC=3.5.99.13;
DE   AltName: Full=Strictosidine synthase 1;
DE            Short=SS-1;
DE   AltName: Full=Strictosidine synthase 13 {ECO:0000303|PubMed:19121120};
DE            Short=AtSS13 {ECO:0000303|PubMed:19121120};
DE   Flags: Precursor;
GN   Name=SSL12 {ECO:0000303|PubMed:10777701};
GN   Synonyms=SS1, SS13 {ECO:0000303|PubMed:19121120};
GN   OrderedLocusNames=At1g74020 {ECO:0000312|Araport:AT1G74020};
GN   ORFNames=F2P9.11 {ECO:0000312|EMBL:AAG52513.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Jain A.K., Nessler C.L.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [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 POTASSIUM STARVATION.
RC   STRAIN=cv. Wassilewskija-2;
RX   PubMed=15489280; DOI=10.1104/pp.104.046672;
RA   Hampton C.R., Bowen H.C., Broadley M.R., Hammond J.P., Mead A., Payne K.A.,
RA   Pritchard J., White P.J.;
RT   "Cesium toxicity in Arabidopsis.";
RL   Plant Physiol. 136:3824-3837(2004).
RN   [8]
RP   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   -!- FUNCTION: Catalyzes the stereospecific condensation of tryptamine with
CC       secologanin to form strictosidine, the key intermediate of indole
CC       alkaloid biosynthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha(S)-strictosidine + H2O = secologanin + tryptamine;
CC         Xref=Rhea:RHEA:15013, ChEBI:CHEBI:15377, ChEBI:CHEBI:18002,
CC         ChEBI:CHEBI:57887, ChEBI:CHEBI:58193; EC=3.5.99.13;
CC   -!- PATHWAY: Alkaloid biosynthesis; 3alpha(S)-strictosidine biosynthesis;
CC       3alpha(S)-strictosidine from secologanin and tryptamine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- INDUCTION: Upon potassium (K) starvation.
CC       {ECO:0000269|PubMed:15489280}.
CC   -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; U43945; AAB40594.1; -; mRNA.
DR   EMBL; U43713; AAB40593.1; -; Genomic_DNA.
DR   EMBL; AC016662; AAG52513.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35538.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7033253.1; -; Genomic_DNA.
DR   EMBL; AY034970; AAK59475.1; -; mRNA.
DR   EMBL; AY062976; AAL34150.1; -; mRNA.
DR   PIR; A96768; A96768.
DR   AlphaFoldDB; P94111; -.
DR   SMR; P94111; -.
DR   FunCoup; P94111; 78.
DR   STRING; 3702.P94111; -.
DR   GlyCosmos; P94111; 1 site, No reported glycans.
DR   GlyGen; P94111; 2 sites.
DR   PaxDb; 3702-P94111; -.
DR   ProteomicsDB; 228377; -.
DR   GeneID; 843740; -.
DR   KEGG; ath:AT1G74020; -.
DR   Araport; AT1G74020; -.
DR   TAIR; AT1G74020; SS2.
DR   eggNOG; KOG1520; Eukaryota.
DR   HOGENOM; CLU_023267_2_1_1; -.
DR   InParanoid; P94111; -.
DR   OMA; SWCDGVV; -.
DR   OrthoDB; 5307922at2759; -.
DR   PhylomeDB; P94111; -.
DR   BioCyc; ARA:AT1G74020-MONOMER; -.
DR   UniPathway; UPA00311; UER00447.
DR   PRO; PR:P94111; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P94111; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0051365; P:cellular response to potassium ion starvation; IEP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   FunFam; 2.120.10.30:FF:000084; Protein STRICTOSIDINE SYNTHASE-LIKE 12; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR   PANTHER; PTHR10426:SF132; PROTEIN STRICTOSIDINE SYNTHASE-LIKE 12; 1.
DR   PANTHER; PTHR10426; STRICTOSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF03088; Str_synth; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   2: Evidence at transcript level;
KW   Alkaloid metabolism; Glycoprotein; Hydrolase; Reference proteome; Signal;
KW   Vacuole.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..335
FT                   /note="Protein STRICTOSIDINE SYNTHASE-LIKE 12"
FT                   /id="PRO_0000033330"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        19
FT                   /note="A -> P (in Ref. 1; AAB40594/AAB40593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="L -> I (in Ref. 1; AAB40594/AAB40593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  35293 MW;  C1382BF040A72849 CRC64;
     MTSFCSMISL LLLLSLSSAV FSDDASFQKL PVPETRSGPE AFAFDSTGKG FYTGVSGGKI
     LKYLPETGYV DFAQITESSN SSWCDGTIGT ALAGRCGRPA GIAFNEKTGD LYVADAPLGL
     HVISPAGGLA TKITDSVDGK PFKFLDGLDV DPTTGVVYFT SFSSRFSPIQ VLIALGLKDA
     TGKLYKYDPS TKVVTVLMEG LSGSAGCAVS SDGSFVLVSQ FTKSNIKRYW IKGPKAGSSE
     DFTNSVSNPD NIKRIGSTGN FWVASVVNKI IVPTNPSAVK VNSNGEVLQT IPLKDKFGDT
     LLSEVNEFEG NLYIGTLTGP FAGILKLEKG SCPAT
//