SUC2_ARATH
ID SUC2_ARATH Reviewed; 512 AA.
AC Q39231; O80550; Q8RWQ6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sucrose transport protein SUC2;
DE AltName: Full=Sucrose permease 2;
DE AltName: Full=Sucrose transporter 1;
DE AltName: Full=Sucrose-proton symporter 2;
GN Name=SUC2; Synonyms=SUT1; OrderedLocusNames=At1g22710; ORFNames=T22J18.12;
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7920705; DOI=10.1046/j.1365-313x.1994.6010067.x;
RA Sauer N., Stolz J.;
RT "SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana;
RT expression and characterization in baker's yeast and identification of the
RT histidine-tagged protein.";
RL Plant J. 6:67-77(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7647685; DOI=10.1007/bf00203657;
RA Truernit E., Sauer N.;
RT "The promoter of the Arabidopsis thaliana SUC2 sucrose-H(+) symporter gene
RT directs expression of beta-glucuronidase to the phloem: evidence for phloem
RT loading and unloading by SUC2.";
RL Planta 196:564-570(1995).
RN [7]
RP TISSUE SPECIFICITY.
RA Stadler R., Sauer N.;
RT "The Arabidopsis thaliana AtSUC2 gene is specifically expressed in
RT companion cells.";
RL Bot. Acta 109:299-306(1996).
RN [8]
RP FUNCTION.
RX PubMed=11087840; DOI=10.1073/pnas.250473797;
RA Gottwald J.R., Krysan P.J., Young J.C., Evert R.F., Sussman M.R.;
RT "Genetic evidence for the in planta role of phloem-specific plasma membrane
RT sucrose transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13979-13984(2000).
RN [9]
RP INDUCTION.
RX PubMed=11673631; DOI=10.1093/pcp/pce150;
RA Furuichi T., Mori I.C., Takahashi K., Muto S.;
RT "Sugar-induced increase in cytosolic Ca(2+) in Arabidopsis thaliana whole
RT plants.";
RL Plant Cell Physiol. 42:1149-1155(2001).
RN [10]
RP TISSUE SPECIFICITY, HOMODIMERIZATION, AND INTERACTION WITH SUC3 AND SUC4.
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 [11]
RP FUNCTION.
RX PubMed=12954621; DOI=10.1074/jbc.m308490200;
RA Chandran D., Reinders A., Ward J.M.;
RT "Substrate specificity of the Arabidopsis thaliana sucrose transporter
RT AtSUC2.";
RL J. Biol. Chem. 278:44320-44325(2003).
RN [12]
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 other glucosides such as maltose, arbutin (hydroquinone-beta-D-
CC glucoside), salicin (2-(hydroxymethyl)phenyl-beta-D-glucoside), alpha-
CC phenylglucoside, beta-phenylglucoside, alpha-paranitrophenylglucoside,
CC beta-paranitrophenylglucoside, and paranitrophenyl-beta-thioglucoside.
CC May also transport biotin. Required for apoplastic phloem sucrose
CC loading in source tissues (e.g. leaves) in order to transport it to
CC sink tissues (e.g. roots, flowers). {ECO:0000269|PubMed:11087840,
CC ECO:0000269|PubMed:12954621, ECO:0000269|PubMed:7920705}.
CC -!- ACTIVITY REGULATION: Inhibited by protonophores (e.g. dinitrophenol and
CC carbonyl cyanide m-chlorophenyl-hydrazone (CCCP)) and SH group
CC inhibitors (e.g. N-ethylmaleimide (NEM) and p-chloromercuriphenyl
CC sulphonic acid (PCMPS)). {ECO:0000269|PubMed:7920705}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=530 uM for sucrose (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:7920705};
CC Vmax=12 umol/h/g enzyme (without glucose)
CC {ECO:0000269|PubMed:7920705};
CC Vmax=77 umol/h/g enzyme (in the presence of 10 mM glucose)
CC {ECO:0000269|PubMed:7920705};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:7920705};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBUNIT: Homodimer. Interacts with SUC3 and SUC4.
CC {ECO:0000269|PubMed:12689351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and, to a lower extent, in
CC roots, flowers and stems. Highly specific to the phloem, exclusively
CC localized in companion cells (at protein level).
CC {ECO:0000269|PubMed:12689351, ECO:0000269|PubMed:7647685,
CC ECO:0000269|PubMed:7920705, ECO:0000269|Ref.7}.
CC -!- DEVELOPMENTAL STAGE: First seen in the tips of young rosette leaves. In
CC older leaves and during their concomitant sink/source transition,
CC expression proceeded from the tips to the bases of the leaves.
CC {ECO:0000269|PubMed:7647685}.
CC -!- INDUCTION: Induced by sucrose depletion. Specifically induced by
CC H.schachtii (cyst nematodes) in nematode-induced syncytia.
CC {ECO:0000269|PubMed:11673631, 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}.
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DR EMBL; X75382; CAA53150.1; -; mRNA.
DR EMBL; AC003979; AAC25515.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30276.1; -; Genomic_DNA.
DR EMBL; AY091774; AAM10322.1; -; mRNA.
DR EMBL; AY048256; AAK82518.1; -; mRNA.
DR EMBL; AY050986; AAK93663.1; -; mRNA.
DR EMBL; AY113946; AAM44994.1; -; mRNA.
DR EMBL; BT000684; AAN31829.1; -; mRNA.
DR EMBL; AY088566; AAM66097.1; -; mRNA.
DR PIR; G86360; G86360.
DR PIR; S38196; S38196.
DR RefSeq; NP_173685.1; NM_102118.4.
DR AlphaFoldDB; Q39231; -.
DR BioGRID; 24116; 16.
DR IntAct; Q39231; 15.
DR STRING; 3702.AT1G22710.1; -.
DR PaxDb; Q39231; -.
DR PRIDE; Q39231; -.
DR ProteomicsDB; 245228; -.
DR EnsemblPlants; AT1G22710.1; AT1G22710.1; AT1G22710.
DR GeneID; 838877; -.
DR Gramene; AT1G22710.1; AT1G22710.1; AT1G22710.
DR KEGG; ath:AT1G22710; -.
DR Araport; AT1G22710; -.
DR TAIR; locus:2199633; AT1G22710.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_025234_3_0_1; -.
DR InParanoid; Q39231; -.
DR OMA; NCFICIP; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; Q39231; -.
DR BioCyc; MetaCyc:AT1G22710-MON; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q39231; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39231; baseline and differential.
DR Genevisible; Q39231; 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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
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; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Sucrose transport protein SUC2"
FT /id="PRO_0000122523"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 221
FT /note="N -> S (in Ref. 4; AAM10322)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> G (in Ref. 1; CAA53150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 54547 MW; F412AFF8474FC12A CRC64;
MVSHPMEKAA NGASALETQT GELDQPERLR KIISVSSIAA GVQFGWALQL SLLTPYVQLL
GIPHKWASLI WLCGPISGML VQPIVGYHSD RCTSRFGRRR PFIVAGAGLV TVAVFLIGYA
ADIGHSMGDQ LDKPPKTRAI AIFALGFWIL DVANNTLQGP CRAFLADLSA GNAKKTRTAN
AFFSFFMAVG NVLGYAAGSY RNLYKVVPFT MTESCDLYCA NLKTCFFLSI TLLLIVTFVS
LCYVKEKPWT PEPTADGKAS NVPFFGEIFG AFKELKRPMW MLLIVTALNW IAWFPFLLFD
TDWMGREVYG GNSDATATAA SKKLYNDGVR AGALGLMLNA IVLGFMSLGV EWIGRKLGGA
KRLWGIVNFI LAICLAMTVV VTKQAENHRR DHGGAKTGPP GNVTAGALTL FAILGIPQAI
TFSIPFALAS IFSTNSGAGQ GLSLGVLNLA IVVPQMVISV GGGPFDELFG GGNIPAFVLG
AIAAAVSGVL ALTVLPSPPP DAPAFKATMG FH
