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SUS5_ARATH
ID   SUS5_ARATH              Reviewed;         836 AA.
AC   F4K5W8; Q9FHU4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Sucrose synthase 5;
DE            Short=AtSUS5;
DE            EC=2.4.1.13;
DE   AltName: Full=Sucrose-UDP glucosyltransferase 5;
GN   Name=SUS5; OrderedLocusNames=At5g37180; ORFNames=MJG14.25;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
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   GENE FAMILY, AND TISSUE SPECIFICITY.
RX   PubMed=14739263; DOI=10.1093/jxb/erh047;
RA   Baud S., Vaultier M.N., Rochat C.;
RT   "Structure and expression profile of the sucrose synthase multigene family
RT   in Arabidopsis.";
RL   J. Exp. Bot. 55:397-409(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17257168; DOI=10.1111/j.1365-313x.2006.03011.x;
RA   Bieniawska Z., Paul Barratt D.H., Garlick A.P., Thole V., Kruger N.J.,
RA   Martin C., Zrenner R., Smith A.M.;
RT   "Analysis of the sucrose synthase gene family in Arabidopsis.";
RL   Plant J. 49:810-828(2007).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=18635527; DOI=10.1093/jxb/ern180;
RA   Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.;
RT   "Localization of sucrose synthase in developing seed and siliques of
RT   Arabidopsis thaliana reveals diverse roles for SUS during development.";
RL   J. Exp. Bot. 59:3283-3295(2008).
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=19470642; DOI=10.1073/pnas.0900689106;
RA   Barratt D.H., Derbyshire P., Findlay K., Pike M., Wellner N., Lunn J.,
RA   Feil R., Simpson C., Maule A.J., Smith A.M.;
RT   "Normal growth of Arabidopsis requires cytosolic invertase but not sucrose
RT   synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:13124-13129(2009).
CC   -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC       fructose for various metabolic pathways. Functions in callose synthesis
CC       at the site of phloem sieve elements. {ECO:0000269|PubMed:19470642}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC         diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:19470642}.
CC   -!- TISSUE SPECIFICITY: Detected in the whole plant but more precisely
CC       confined to the vasculature in cotyledons, leaves, petals, anthers and
CC       roots. Also detected in developing siliques, young immature rosette and
CC       cauline leaves. {ECO:0000269|PubMed:14739263,
CC       ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:18635527,
CC       ECO:0000269|PubMed:19470642}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:17257168}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11375.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB017068; BAB11375.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F4K5W8; -.
DR   SMR; F4K5W8; -.
DR   STRING; 3702.AT5G37180.1; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; F4K5W8; -.
DR   PRIDE; F4K5W8; -.
DR   ProteomicsDB; 228312; -.
DR   Araport; AT5G37180; -.
DR   TAIR; locus:2166203; AT5G37180.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_019158_1_0_1; -.
DR   InParanoid; F4K5W8; -.
DR   BioCyc; MetaCyc:AT5G37180-MON; -.
DR   BRENDA; 2.4.1.13; 399.
DR   PRO; PR:F4K5W8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4K5W8; baseline and differential.
DR   Genevisible; F4K5W8; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016157; F:sucrose synthase activity; IDA:TAIR.
DR   GO; GO:0080165; P:callose deposition in phloem sieve plate; IMP:TAIR.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR000368; Sucrose_synth.
DR   InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR   PANTHER; PTHR45839; PTHR45839; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   TIGRFAMs; TIGR02470; sucr_synth; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Glycosyltransferase; Reference proteome; Secreted; Transferase.
FT   CHAIN           1..836
FT                   /note="Sucrose synthase 5"
FT                   /id="PRO_0000418804"
FT   REGION          270..748
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250"
FT   REGION          805..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  94905 MW;  761DC9728DFDE252 CRC64;
     MEMTSGSLGN GIPEAMGQNR GNIKRCLEKY IENGRRVMKL NELMDEMEIV INDVTQRRRV
     MEGDLGKILC FTQAVVIPPN VAFAVRGTPG NWQYVKVNSS NLSVEALSST QYLKLKEFLF
     DENWANDENA LEVDFGALDF TLPWLSLSSS IGNGLSFVSS KLGGRLNDNP QSLVDYLLSL
     EHQGEKLMMN ETLNTARKLE MSLILADVFL SELPKDTPFQ AFELRFKECG FEKGWGESAG
     RVKETMRILS EILQAPDPQN IDRFFARVPR IFNVVIFSVH GYFGQTDVLG LPDTGGQVVY
     ILDQVKALED ELLQRINSQG LNFKPQILVV TRLIPDAKKT KCNQELEPIF GTKYSNILRI
     PFVTENGILR RWVSRFDIYP YLERFTKDAT TKILDILEGK PDLIIGNYTD GNLVASLMAN
     KLGITQATIA HALEKTKYED SDIKWKEFDP KYHFSSQFTA DLISMNSADF IIASTYQEIA
     GSKERAGQYE SHMSFTVPGL YRVVSGINVF DPRFNIAAPG ADDSIYFPFT AQDRRFTKFY
     TSIDELLYSQ SENDEHIGYL VDKKKPIIFS MARLDVVKNL TGLTEWYAKN KRLRDLVNLV
     IVGGFFDASK SKDREEISEI KKMHSLIEKY QLKGQFRWIT AQTDRTRNGE LYRSIADTRG
     AFVQPAHYEA FGLTVIEAMS CGLVTFATNQ GGPAEIIVDG VSGFHIDPSN GEESSDKIAD
     FFEKSGMDPD YWNMFSNEGL QRINECYTWK IYANKVINMG STYSYWRHLN KDQKLAKQRY
     IHSFYNLQYR NLVKTIPILS DIPEPPPLPP KPLVKPSASK GSKRTQPRLS FRLFGA
 
 
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