SUC9_ARATH
ID SUC9_ARATH Reviewed; 491 AA.
AC Q9FG00;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sucrose transport protein SUC9;
DE AltName: Full=Sucrose permease 9;
DE AltName: Full=Sucrose-proton symporter 9;
GN Name=SUC9; OrderedLocusNames=At5g06170; ORFNames=MBL20.5;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=15361146; DOI=10.1111/j.1365-313x.2004.02196.x;
RA Sauer N., Ludwig A., Knoblauch A., Rothe P., Gahrtz M., Klebl F.;
RT "AtSUC8 and AtSUC9 encode functional sucrose transporters, but the closely
RT related AtSUC6 and AtSUC7 genes encode aberrant proteins in different
RT Arabidopsis ecotypes.";
RL Plant J. 40:120-130(2004).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17098854; DOI=10.1104/pp.106.089003;
RA Sivitz A.B., Reinders A., Johnson M.E., Krentz A.D., Grof C.P.,
RA Perroux J.M., Ward J.M.;
RT "Arabidopsis sucrose transporter AtSUC9. High-affinity transport activity,
RT intragenic control of expression, and early flowering mutant phenotype.";
RL Plant Physiol. 143:188-198(2007).
CC -!- FUNCTION: High-affinity sucrose transporter. Responsible for the
CC transport of sucrose into the cell, with the concomitant uptake of
CC protons (symport system). Can also transport a wide range of
CC glucosides, such as helicin, salicin, arbutin, maltose, fraxin,
CC esculin, uranose, alpha-methylglucoside, alpha-phenylglucoside and
CC beta-phenylglucoside. Plays a role in flowering time transition delay.
CC {ECO:0000269|PubMed:15361146, ECO:0000269|PubMed:17098854}.
CC -!- ACTIVITY REGULATION: Inhibited by protonophores (e.g. carbonyl cyanide
CC m-chlorophenyl-hydrazone (CCCP)) and SH group inhibitors (e.g. p-
CC chloromercuribenzene sulphonic acid (PCMBS)).
CC {ECO:0000269|PubMed:15361146}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=66 uM for sucrose (at pH 5.0) {ECO:0000269|PubMed:15361146,
CC ECO:0000269|PubMed:17098854};
CC KM=150 uM for salicin (at pH 5.0) {ECO:0000269|PubMed:15361146,
CC ECO:0000269|PubMed:17098854};
CC KM=560 uM for arbutin (at pH 5.0) {ECO:0000269|PubMed:15361146,
CC ECO:0000269|PubMed:17098854};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17098854};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17098854}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15361146,
CC ECO:0000269|PubMed:17098854}.
CC -!- DISRUPTION PHENOTYPE: Early flowering phenotype under short-day
CC conditions. {ECO:0000269|PubMed:17098854}.
CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC symporter transporter (TC 2.A.2.4) family. {ECO:0000305}.
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DR EMBL; AP002544; BAB09682.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90978.1; -; Genomic_DNA.
DR RefSeq; NP_196235.1; NM_120699.1.
DR AlphaFoldDB; Q9FG00; -.
DR BioGRID; 15783; 6.
DR IntAct; Q9FG00; 1.
DR STRING; 3702.AT5G06170.1; -.
DR PaxDb; Q9FG00; -.
DR PRIDE; Q9FG00; -.
DR ProteomicsDB; 245355; -.
DR EnsemblPlants; AT5G06170.1; AT5G06170.1; AT5G06170.
DR GeneID; 830504; -.
DR Gramene; AT5G06170.1; AT5G06170.1; AT5G06170.
DR KEGG; ath:AT5G06170; -.
DR Araport; AT5G06170; -.
DR TAIR; locus:2160732; AT5G06170.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_025234_3_0_1; -.
DR InParanoid; Q9FG00; -.
DR OMA; AWSSFIW; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; Q9FG00; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q9FG00; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG00; baseline and differential.
DR Genevisible; Q9FG00; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0042951; F:arbutin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005364; F:maltose:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0042950; F:salicin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008515; F:sucrose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IBA:GO_Central.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0042946; P:glucoside transport; IDA:TAIR.
DR GO; GO:0015768; P:maltose transport; IDA:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005989; Suc_symporter_pln.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR01301; GPH_sucrose; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="Sucrose transport protein SUC9"
FT /id="PRO_0000122530"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..468
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q39232"
SQ SEQUENCE 491 AA; 52578 MW; AA89091CB7146352 CRC64;
MSDIQAKEDA APVDRQSSSS VVVPDEPSPL RKMISVASIA AGIQFGWALQ LSLLTPYVQL
LGVPHKWSSF IWLCGPISGL LVQPTVGYFS DRCKSRFGRR RPFIATGALL VALAVILIGF
AADFGHTMGD KLDEAVKIRA VGFFVVGFWI LDVANNTLQG PCRAFLGDLA AGDAKKTRTA
NAIFSFFMAV GNVLGYAAGS YTNLHKIFPF TVTKACDIYC ANLKSCFIIS ITLLIVLTII
ALWYVEDKQW SPNADSDNEK TPFFGEIFGA FKVMKRPMWM LLAVTALNWI AWFPFLLYDT
DWMGREVYGG DSAGDDKMKK LYNHGIQVGS LGLMLNSIVL GVMSLVIGVI SKKIGAKRLW
GAVNIILAVC LAMTVLVTKK AEEHRKIAGR MALPTNAIRD GALSLFAILG IPLAITFSIP
FALASIISSS SGAGQGLSLG VLNMAIVIPQ MIVSFGVGPI DALFGGGNLP GFVVGAIAAL
ISSVVALTVL P
