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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}.
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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
 
 
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