SUC4_ARATH
ID SUC4_ARATH Reviewed; 510 AA.
AC Q9FE59; O04516; Q9M3R4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sucrose transport protein SUC4;
DE AltName: Full=Sucrose permease 4;
DE AltName: Full=Sucrose transporter 4;
DE AltName: Full=Sucrose-proton symporter 4;
GN Name=SUC4; Synonyms=SUT4; OrderedLocusNames=At1g09960; ORFNames=F21M12.35;
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], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10948254; DOI=10.2307/3871134;
RA Weise A., Barker L., Kuehn C., Lalonde S., Buschmann H., Frommer W.B.,
RA Ward J.M.;
RT "A new subfamily of sucrose transporters, SUT4, with low affinity/high
RT capacity localized in enucleate sieve elements of plants.";
RL Plant Cell 12:1345-1355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sauer N.K.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 TISSUE SPECIFICITY, HOMODIMERIZATION, AND INTERACTION WITH SUC2 AND SUC3.
RX PubMed=12689351; DOI=10.1186/1471-2091-4-3;
RA Schulze W.X., Reinders A., Ward J., Lalonde S., Frommer W.B.;
RT "Interactions between co-expressed Arabidopsis sucrose transporters in the
RT split-ubiquitin system.";
RL BMC Biochem. 4:3-3(2003).
RN [7]
RP INDUCTION.
RX PubMed=12529515; DOI=10.1104/pp.008037;
RA Juergensen K., Scholz-Starke J., Sauer N., Hess P., van Bel A.J.E.,
RA Grundler F.M.W.;
RT "The companion cell-specific Arabidopsis disaccharide carrier AtSUC2 is
RT expressed in nematode-induced syncytia.";
RL Plant Physiol. 131:61-69(2003).
CC -!- FUNCTION: Responsible for the transport of sucrose into the cell, with
CC the concomitant uptake of protons (symport system). Can also transport
CC maltose at a lesser rate. May also transport biotin.
CC {ECO:0000269|PubMed:10948254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 mM for sucrose (at pH 4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10948254};
CC KM=6 mM for sucrose (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10948254};
CC pH dependence:
CC Optimum pH is 4-5. {ECO:0000269|PubMed:10948254};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBUNIT: Homodimer. Interacts with SUC2 and SUC3.
CC {ECO:0000269|PubMed:12689351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in sink tissues, mostly in minor veins of
CC sink leaves. Localized in companion cells.
CC {ECO:0000269|PubMed:10948254, ECO:0000269|PubMed:12689351}.
CC -!- DEVELOPMENTAL STAGE: Also present in inflorescence axil branches and in
CC anther and pistil of developing flowers. At anthesis, restricted to
CC anthers. {ECO:0000269|PubMed:10948254}.
CC -!- INDUCTION: Specifically induced by H.schachtii (cyst nematodes) in
CC nematode-induced syncytia. {ECO:0000269|PubMed:12529515}.
CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC symporter transporter (TC 2.A.2.4) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF175322; AAG09192.1; -; Genomic_DNA.
DR EMBL; AF175321; AAG09191.1; -; mRNA.
DR EMBL; AJ289166; CAB92308.1; -; mRNA.
DR EMBL; AC000132; AAB60751.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28521.1; -; Genomic_DNA.
DR EMBL; AY072092; AAL59915.1; -; mRNA.
DR EMBL; BT004418; AAO42412.1; -; mRNA.
DR PIR; A86234; A86234.
DR RefSeq; NP_172467.1; NM_100870.3.
DR AlphaFoldDB; Q9FE59; -.
DR BioGRID; 22771; 17.
DR IntAct; Q9FE59; 10.
DR STRING; 3702.AT1G09960.1; -.
DR TCDB; 2.A.2.4.6; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR PaxDb; Q9FE59; -.
DR PRIDE; Q9FE59; -.
DR ProteomicsDB; 228279; -.
DR EnsemblPlants; AT1G09960.1; AT1G09960.1; AT1G09960.
DR GeneID; 837530; -.
DR Gramene; AT1G09960.1; AT1G09960.1; AT1G09960.
DR KEGG; ath:AT1G09960; -.
DR Araport; AT1G09960; -.
DR TAIR; locus:2024422; AT1G09960.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_025234_3_0_1; -.
DR InParanoid; Q9FE59; -.
DR OMA; INVSMEP; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; Q9FE59; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q9FE59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FE59; baseline and differential.
DR Genevisible; Q9FE59; AT.
DR GO; GO:0005801; C:cis-Golgi network; IDA:TAIR.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IEA:EnsemblPlants.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0008515; F:sucrose transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005989; Suc_symporter_pln.
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..510
FT /note="Sucrose transport protein SUC4"
FT /id="PRO_0000122525"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q39232"
FT CONFLICT 12
FT /note="V -> A (in Ref. 1; AAG09192/AAG09191)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="A -> P (in Ref. 1; AAG09192/AAG09191)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="T -> N (in Ref. 1; AAG09192/AAG09191)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> P (in Ref. 1; AAG09192/AAG09191)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> T (in Ref. 1; AAG09192/AAG09191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 54784 MW; 3AF99CF2D48ACBD4 CRC64;
MATSDQDRRH RVTRNRPPIA RPSTSSSRPV VSPPRSKVSK RVLLRVASVA CGIQFGWALQ
LSLLTPYVQE LGIPHAWASV IWLCGPLSGL FVQPLVGHSS DRCTSKYGRR RPFIVAGAVA
ISISVMVIGH AADIGWAFGD REGKIKPRAI VAFVLGFWIL DVANNMTQGP CRALLADLTE
NDNRRTRVAN GYFSLFMAVG NVLGYATGSY NGWYKIFTFT KTVACNVECA NLKSAFYIDV
VFIAITTILS VSAAHEVPLA SLASEAHGQT SGTDEAFLSE IFGTFRYFPG NVWIILLVTA
LTWIGWFPFI LFDTDWMGRE IYGGEPNIGT SYSAGVSMGA LGLMLNSVFL GITSVLMEKL
CRKWGAGFVW GISNILMAIC FLGMIITSFV ASHLGYIGHE QPPASIVFAA VLIFTILGIP
LAITYSVPYA LISIRIESLG LGQGLSLGVL NLAIVIPQVI VSVGSGPWDQ LFGGGNSPAL
AVGAATGFIG GIVAILALPR TRIQKPIPLP
