SSL13_ARATH
ID SSL13_ARATH Reviewed; 403 AA.
AC Q9M1B4; Q84J97;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein STRICTOSIDINE SYNTHASE-LIKE 13 {ECO:0000303|PubMed:10777701};
DE Short=AtSSL13 {ECO:0000303|PubMed:10777701};
DE AltName: Full=Protein LESS ADHERENT POLLEN 3 {ECO:0000303|PubMed:20033437};
DE AltName: Full=Strictosidine synthase 11 {ECO:0000303|PubMed:19121120};
DE Short=AtSS11 {ECO:0000303|PubMed:19121120};
DE Flags: Precursor;
GN Name=SSL13 {ECO:0000303|PubMed:10777701};
GN Synonyms=LAP3 {ECO:0000303|PubMed:20033437},
GN SS11 {ECO:0000303|PubMed:19121120};
GN OrderedLocusNames=At3g59530 {ECO:0000312|Araport:AT3G59530};
GN ORFNames=T16L24.80 {ECO:0000312|EMBL:CAB75450.1};
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] (ISOFORM 2).
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=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 [5]
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).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLU-89, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=20033437; DOI=10.1007/s00497-009-0101-8;
RA Dobritsa A.A., Nishikawa S., Preuss D., Urbanczyk-Wochniak E., Sumner L.W.,
RA Hammond A., Carlson A.L., Swanson R.J.;
RT "LAP3, a novel plant protein required for pollen development, is essential
RT for proper exine formation.";
RL Sex. Plant Reprod. 22:167-177(2009).
CC -!- FUNCTION: Required for the exine formation during pollen development.
CC {ECO:0000269|PubMed:20033437}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M1B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M1B4-2; Sequence=VSP_057337;
CC -!- DISRUPTION PHENOTYPE: Abnormal stigma binding and male sterility.
CC Abnormal pollen exine which is thinner, weaker, and missing some
CC connections between their roof-like tectum structures. Content
CC modification of a broad range of metabolic compounds, such as
CC nonacosane and naringenin chalcone. {ECO:0000269|PubMed:20033437}.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
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DR EMBL; AL138659; CAB75450.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79936.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79937.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63538.1; -; Genomic_DNA.
DR EMBL; BT004209; AAO42227.1; -; mRNA.
DR EMBL; BT005675; AAO64095.1; -; mRNA.
DR PIR; T49294; T49294.
DR RefSeq; NP_001325620.1; NM_001339986.1. [Q9M1B4-1]
DR RefSeq; NP_191512.1; NM_115815.6. [Q9M1B4-1]
DR RefSeq; NP_974462.1; NM_202733.3. [Q9M1B4-1]
DR AlphaFoldDB; Q9M1B4; -.
DR SMR; Q9M1B4; -.
DR IntAct; Q9M1B4; 2.
DR STRING; 3702.AT3G59530.1; -.
DR PaxDb; Q9M1B4; -.
DR PRIDE; Q9M1B4; -.
DR ProteomicsDB; 228378; -. [Q9M1B4-1]
DR EnsemblPlants; AT3G59530.1; AT3G59530.1; AT3G59530. [Q9M1B4-1]
DR EnsemblPlants; AT3G59530.2; AT3G59530.2; AT3G59530. [Q9M1B4-1]
DR EnsemblPlants; AT3G59530.3; AT3G59530.3; AT3G59530. [Q9M1B4-1]
DR GeneID; 825122; -.
DR Gramene; AT3G59530.1; AT3G59530.1; AT3G59530. [Q9M1B4-1]
DR Gramene; AT3G59530.2; AT3G59530.2; AT3G59530. [Q9M1B4-1]
DR Gramene; AT3G59530.3; AT3G59530.3; AT3G59530. [Q9M1B4-1]
DR KEGG; ath:AT3G59530; -.
DR Araport; AT3G59530; -.
DR TAIR; locus:2097488; AT3G59530.
DR eggNOG; KOG1520; Eukaryota.
DR HOGENOM; CLU_023267_2_0_1; -.
DR InParanoid; Q9M1B4; -.
DR OMA; ERLWENQ; -.
DR OrthoDB; 757814at2759; -.
DR PhylomeDB; Q9M1B4; -.
DR BioCyc; ARA:AT3G59530-MON; -.
DR PRO; PR:Q9M1B4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1B4; baseline and differential.
DR Genevisible; Q9M1B4; AT.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0010584; P:pollen exine formation; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Glycoprotein;
KW Reference proteome; Signal; Vacuole.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..403
FT /note="Protein STRICTOSIDINE SYNTHASE-LIKE 13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431598"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 380
FT /note="M -> MKLVSEVREVQG (in isoform 2)"
FT /id="VSP_057337"
FT MUTAGEN 89
FT /note="E->K: In lap3-1; abnormal pollen exine."
FT /evidence="ECO:0000269|PubMed:20033437"
SQ SEQUENCE 403 AA; 45629 MW; 2D5E5701DE4340DB CRC64;
MEKKGQHGTY ESMMTHHPIL CIIALSVLFI AIDPFHMSPI GGREFKPVKH EVAPYKEVMG
SWPRDNLSRL GNHGKLEFVD QVFGPESLEF DSLGRGPYTG LADGRVVRWM GEAIGWETFS
VVTSKWSEEA CVRGVDSTTN KQWKHEKLCG RPLGLRFHKE TGNLYIADAY YGLLVVGPEG
GIATPLATHV EGKPILFAND LDIHRNGSIF FTDTSKRYDR ANHFFILLEG ESTGRLLRYD
PPTKTTHIVL EGLAFPNGIQ LSKDQSFLLF TETTNCRLVK YWLEGPKMGE VEVVADLPGF
PDNVRINEEG QFWVAIDCCR TPAQEVLTNN PWIRSIYFRL PIPMKLLAKT MGMRMYTVIS
RFDEEGKVLE VLEDRQGKVM KLWIGTVAHN HIATLPYPLT MNQ
