ACL5_ARATH
ID ACL5_ARATH Reviewed; 339 AA.
AC Q9S7X6; A8MSC8; C0Z321; Q8VWK6; Q8W3K7; Q8W3K8; Q8W3K9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Thermospermine synthase ACAULIS5;
DE EC=2.5.1.79;
GN Name=ACL5; Synonyms=TKV; OrderedLocusNames=At5g19530; ORFNames=T20D1.50;
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] (ISOFORM 1), MUTAGENESIS OF
RP GLU-123, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10944107; DOI=10.1093/emboj/19.16.4248;
RA Hanzawa Y., Takahashi T., Michael A.J., Burtin D., Long D., Pineiro M.,
RA Coupland G., Komeda Y.;
RT "ACAULIS5, an Arabidopsis gene required for stem elongation, encodes a
RT spermine synthase.";
RL EMBO J. 19:4248-4256(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ag-0, cv. Bl-1, cv. Bus-1, cv. Ci-0, cv. Cvi-0, cv. Dra-0,
RC cv. Edi-0, cv. Hau-0, cv. In-0, cv. Ita-0, cv. Kas-1, cv. Mr-0, cv. Nok-4,
RC cv. Ost-0, cv. Pog-0, cv. Rou-0, cv. Shokei, cv. Su-0, cv. Ts-1, and
RC cv. Wassilewskija;
RX PubMed=12655134; DOI=10.1266/ggs.78.11;
RA Yoshida K., Kamiya T., Kawabe A., Miyashita N.T.;
RT "DNA polymorphism at the ACAULIS5 locus of the wild plant Arabidopsis
RT thaliana.";
RL Genes Genet. Syst. 78:11-21(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
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 [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15894745; DOI=10.1104/pp.104.055756;
RA Clay N.K., Nelson T.;
RT "Arabidopsis thickvein mutation affects vein thickness and organ
RT vascularization, and resides in a provascular cell-specific spermine
RT synthase involved in vein definition and in polar auxin transport.";
RL Plant Physiol. 138:767-777(2005).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17560575; DOI=10.1016/j.febslet.2007.05.074;
RA Knott J.M., Romer P., Sumper M.;
RT "Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis
RT thaliana synthesize thermospermine rather than spermine.";
RL FEBS Lett. 581:3081-3086(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18599510; DOI=10.1242/dev.019349;
RA Muniz L., Minguet E.G., Singh S.K., Pesquet E., Vera-Sirera F.,
RA Moreau-Courtois C.L., Carbonell J., Blazquez M.A., Tuominen H.;
RT "ACAULIS5 controls Arabidopsis xylem specification through the prevention
RT of premature cell death.";
RL Development 135:2573-2582(2008).
RN [11]
RP FUNCTION, AND INDUCTION BY THERMOSPERMINE.
RX PubMed=18669523; DOI=10.1093/pcp/pcn109;
RA Kakehi J., Kuwashiro Y., Niitsu M., Takahashi T.;
RT "Thermospermine is required for stem elongation in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:1342-1349(2008).
RN [12]
RP INDUCTION BY SALT.
RX PubMed=20137962; DOI=10.1016/j.plaphy.2010.01.013;
RA Naka Y., Watanabe K., Sagor G.H., Niitsu M., Pillai M.A., Kusano T.,
RA Takahashi Y.;
RT "Quantitative analysis of plant polyamines including thermospermine during
RT growth and salinity stress.";
RL Plant Physiol. Biochem. 48:527-533(2010).
CC -!- FUNCTION: Required for correct xylem specification through regulation
CC of the lifetime of the xylem elements. Prevents premature death of the
CC xylem vessel elements. {ECO:0000269|PubMed:10944107,
CC ECO:0000269|PubMed:17560575, ECO:0000269|PubMed:18599510,
CC ECO:0000269|PubMed:18669523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) +
CC S-methyl-5'-thioadenosine + thermospermine; Xref=Rhea:RHEA:30515,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:59903; EC=2.5.1.79;
CC Evidence={ECO:0000269|PubMed:17560575};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9S7X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S7X6-2; Sequence=VSP_039690;
CC Name=3;
CC IsoId=Q9S7X6-3; Sequence=VSP_039689;
CC -!- TISSUE SPECIFICITY: Highly expressed in stem internodes and roots.
CC Lower levels in young seedlings before flowering and rosette leaves.
CC Expressed in the vascular tissues. Restricted to procambial and/or
CC provascular cells during primary root development and early leaves
CC development. {ECO:0000269|PubMed:10944107,
CC ECO:0000269|PubMed:15894745}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout early globular-staged embryos
CC and during embryogenesis. {ECO:0000269|PubMed:15894745}.
CC -!- INDUCTION: Up-regulated by auxin (IAA), but not by abscisic acid (ABA),
CC brassinolid (BR), gibberelic acid (GA3)or benzyl aminopurine (BA).
CC Down-regulated by salt stress and thermospermine.
CC {ECO:0000269|PubMed:10944107, ECO:0000269|PubMed:18669523,
CC ECO:0000269|PubMed:20137962}.
CC -!- DISRUPTION PHENOTYPE: Severe reduction in the length of stem
CC internodes. Increased thickness of veins in leaves and inflorescence
CC stems. Altered morphology of xylem vessel elements.
CC {ECO:0000269|PubMed:15894745, ECO:0000269|PubMed:18599510}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF184094; AAF01312.1; -; mRNA.
DR EMBL; AF184093; AAF01311.1; -; Genomic_DNA.
DR EMBL; AB076723; BAB83633.1; -; Genomic_DNA.
DR EMBL; AB076724; BAB83634.1; -; Genomic_DNA.
DR EMBL; AB076725; BAB83635.1; -; Genomic_DNA.
DR EMBL; AB076726; BAB83636.1; -; Genomic_DNA.
DR EMBL; AB076727; BAB83637.1; -; Genomic_DNA.
DR EMBL; AB076728; BAB83638.1; -; Genomic_DNA.
DR EMBL; AB076729; BAB83639.1; -; Genomic_DNA.
DR EMBL; AB076730; BAB83640.1; -; Genomic_DNA.
DR EMBL; AB076731; BAB83641.1; -; Genomic_DNA.
DR EMBL; AB076732; BAB83642.1; -; Genomic_DNA.
DR EMBL; AB076733; BAB83643.1; -; Genomic_DNA.
DR EMBL; AB076734; BAB83644.1; -; Genomic_DNA.
DR EMBL; AB076735; BAB83645.1; -; Genomic_DNA.
DR EMBL; AB076736; BAB83646.1; -; Genomic_DNA.
DR EMBL; AB076737; BAB83647.1; -; Genomic_DNA.
DR EMBL; AB076739; BAB83649.1; -; Genomic_DNA.
DR EMBL; AB076740; BAB83650.1; -; Genomic_DNA.
DR EMBL; AB076741; BAB83651.1; -; Genomic_DNA.
DR EMBL; AB076742; BAB83652.1; -; Genomic_DNA.
DR EMBL; AB076743; BAB83653.1; -; Genomic_DNA.
DR EMBL; AB076738; BAB83648.1; -; Genomic_DNA.
DR EMBL; AF296830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92721.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92722.1; -; Genomic_DNA.
DR EMBL; AY127003; AAM83230.1; -; mRNA.
DR EMBL; BT002254; AAN72265.1; -; mRNA.
DR EMBL; AY087927; AAM65477.1; -; mRNA.
DR EMBL; AK318985; BAH57100.1; -; mRNA.
DR RefSeq; NP_001078605.1; NM_001085136.1. [Q9S7X6-2]
DR RefSeq; NP_568376.1; NM_121958.4. [Q9S7X6-1]
DR AlphaFoldDB; Q9S7X6; -.
DR SMR; Q9S7X6; -.
DR STRING; 3702.AT5G19530.1; -.
DR iPTMnet; Q9S7X6; -.
DR PaxDb; Q9S7X6; -.
DR PRIDE; Q9S7X6; -.
DR ProteomicsDB; 244691; -. [Q9S7X6-1]
DR EnsemblPlants; AT5G19530.1; AT5G19530.1; AT5G19530. [Q9S7X6-1]
DR EnsemblPlants; AT5G19530.2; AT5G19530.2; AT5G19530. [Q9S7X6-2]
DR GeneID; 832073; -.
DR Gramene; AT5G19530.1; AT5G19530.1; AT5G19530. [Q9S7X6-1]
DR Gramene; AT5G19530.2; AT5G19530.2; AT5G19530. [Q9S7X6-2]
DR KEGG; ath:AT5G19530; -.
DR Araport; AT5G19530; -.
DR TAIR; locus:2180816; AT5G19530.
DR eggNOG; KOG1562; Eukaryota.
DR InParanoid; Q9S7X6; -.
DR OMA; WIPSFGY; -.
DR OrthoDB; 1059849at2759; -.
DR PhylomeDB; Q9S7X6; -.
DR BioCyc; MetaCyc:MON-15365; -.
DR BRENDA; 2.5.1.79; 399.
DR PRO; PR:Q9S7X6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7X6; baseline and differential.
DR Genevisible; Q9S7X6; AT.
DR GO; GO:0005737; C:cytoplasm; TAS:TAIR.
DR GO; GO:0016768; F:spermine synthase activity; IDA:TAIR.
DR GO; GO:0010487; F:thermospermine synthase activity; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0048759; P:xylem vessel member cell differentiation; IMP:TAIR.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..339
FT /note="Thermospermine synthase ACAULIS5"
FT /id="PRO_0000397674"
FT DOMAIN 33..270
FT /note="PABS"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039689"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039690"
FT VARIANT 17
FT /note="H -> L (in strain: cv. Bus-1, cv. Ci-0, cv. Cvi-0,
FT cv. Edi-0, cv. Kas-1 and cv. Ost-0)"
FT VARIANT 63
FT /note="D -> N (in strain: cv. Pog-0)"
FT VARIANT 240
FT /note="N -> S (in strain: cv. Bl-1)"
FT VARIANT 259
FT /note="F -> L (in strain: cv. Edi-0)"
FT MUTAGEN 123
FT /note="E->K: In acl5-1; loss of function."
FT /evidence="ECO:0000269|PubMed:10944107"
SQ SEQUENCE 339 AA; 38547 MW; 2DB97B1E9DB447F9 CRC64;
MGEAVEVMFG NGFPEIHKAT SPTQTLHSNQ QDCHWYEETI DDDLKWSFAL NSVLHQGTSE
YQDIALLDTK RFGKVLVIDG KMQSAERDEF IYHECLIHPA LLFHPNPKTV FIMGGGEGSA
AREILKHTTI EKVVMCDIDQ EVVDFCRRFL TVNSDAFCNK KLELVIKDAK AELEKREEKF
DIIVGDLADP VEGGPCYQLY TKSFYQNILK PKLSPNGIFV TQAGPAGIFT HKEVFTSIYN
TMKQVFKYVK AYTAHVPSFA DTWGWVMASD HEFDVEVDEM DRRIEERVNG ELMYLNAPSF
VSAATLNKTI SLALEKETEV YSEENARFIH GHGVAYRHI