SUC3_ARATH
ID SUC3_ARATH Reviewed; 594 AA.
AC O80605;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Sucrose transport protein SUC3;
DE AltName: Full=Sucrose permease 3;
DE AltName: Full=Sucrose transporter 2;
DE AltName: Full=Sucrose-proton symporter 3;
GN Name=SUC3; Synonyms=SUT2; OrderedLocusNames=At2g02860; ORFNames=T17M13.3;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Flower;
RX PubMed=11135120; DOI=10.1046/j.1365-313x.2000.00934.x;
RA Meyer S., Melzer M., Truernit E., Huemmer C., Besenbeck R., Stadler R.,
RA Sauer N.;
RT "AtSUC3, a gene encoding a new Arabidopsis sucrose transporter, is
RT expressed in cells adjacent to the vascular tissue and in a carpel cell
RT layer.";
RL Plant J. 24:869-882(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 TISSUE SPECIFICITY.
RX PubMed=10899981; DOI=10.2307/3871262;
RA Barker L., Kuehn C., Weise A., Schulz A., Gebhardt C., Hirner B.,
RA Hellmann H., Schulze W., Ward J.M., Frommer W.B.;
RT "SUT2, a putative sucrose sensor in sieve elements.";
RL Plant Cell 12:1153-1164(2000).
RN [5]
RP TISSUE SPECIFICITY, HOMODIMERIZATION, AND INTERACTION WITH SUC2 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 [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=14739351; DOI=10.1104/pp.103.033399;
RA Meyer S., Lauterbach C., Niedermeier M., Barth I., Sjolund R.D., Sauer N.;
RT "Wounding enhances expression of AtSUC3, a sucrose transporter from
RT Arabidopsis sieve elements and sink tissues.";
RL Plant Physiol. 134:684-693(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Probably involved
CC in carpel maturation that leads to pod shatter and seed dispersal.
CC {ECO:0000269|PubMed:11135120}.
CC -!- ACTIVITY REGULATION: Inhibited by protonophores (e.g. dinitrophenol and
CC carbonyl cyanide m-chlorophenyl-hydrazone (CCCP)) and SH group
CC inhibitors (e.g. p-chloromercuribenzene sulphonic acid (PCMBS)).
CC {ECO:0000269|PubMed:11135120}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for sucrose {ECO:0000269|PubMed:11135120};
CC KM=1.6 mM for maltose {ECO:0000269|PubMed:11135120};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBUNIT: Homodimer. Interacts with SUC2 and SUC4.
CC {ECO:0000269|PubMed:12689351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O80605-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly localized in parenchymatic cells next to
CC vascular tissues (at protein level). Present in stipules, trichomes,
CC hydathodes and guard cells of source leaves, as well as in lateral root
CC tips and flowers. {ECO:0000269|PubMed:10899981,
CC ECO:0000269|PubMed:11135120, ECO:0000269|PubMed:12689351,
CC ECO:0000269|PubMed:14739351}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pollen and pollen tubes, as well as
CC in seed coats. Specific increase of expression in innermost layer cells
CC of the mesocarp (cells located between the outer epidermis (exocarp)
CC and the inner epidermis (endocarp) of the carpel) during carpel
CC maturation (at protein level). Present in suspensor of embryos and in
CC embryos root tips. Absent in very young organs, but levels increase as
CC they mature. {ECO:0000269|PubMed:11135120,
CC ECO:0000269|PubMed:14739351}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:14739351}.
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; AJ289165; CAB92307.1; -; mRNA.
DR EMBL; AC004138; AAC32907.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05635.1; -; Genomic_DNA.
DR PIR; G84441; G84441.
DR RefSeq; NP_178389.1; NM_126341.3. [O80605-1]
DR AlphaFoldDB; O80605; -.
DR BioGRID; 219; 20.
DR IntAct; O80605; 17.
DR STRING; 3702.AT2G02860.1; -.
DR TCDB; 2.A.2.4.3; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR iPTMnet; O80605; -.
DR PaxDb; O80605; -.
DR PRIDE; O80605; -.
DR ProteomicsDB; 228278; -. [O80605-1]
DR EnsemblPlants; AT2G02860.1; AT2G02860.1; AT2G02860. [O80605-1]
DR GeneID; 814817; -.
DR Gramene; AT2G02860.1; AT2G02860.1; AT2G02860. [O80605-1]
DR KEGG; ath:AT2G02860; -.
DR Araport; AT2G02860; -.
DR TAIR; locus:2056675; AT2G02860.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_025234_1_0_1; -.
DR InParanoid; O80605; -.
DR OMA; GMIVQFA; -.
DR PhylomeDB; O80605; -.
DR SABIO-RK; O80605; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:O80605; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80605; baseline and differential.
DR Genevisible; O80605; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
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:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015770; P:sucrose transport; TAS:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..594
FT /note="Sucrose transport protein SUC3"
FT /id="PRO_0000122524"
FT TOPO_DOM 2..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..555
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 594 AA; 63973 MW; DF075A3601299DA0 CRC64;
MSDSVSISVP YRNLRKEIEL ETVTKHRQNE SGSSSFSESA SPSNHSDSAD GESVSKNCSL
VTLVLSCTVA AGVQFGWALQ LSLLTPYIQT LGISHAFSSF IWLCGPITGL VVQPFVGIWS
DKCTSKYGRR RPFILVGSFM ISIAVIIIGF SADIGYLLGD SKEHCSTFKG TRTRAAVVFI
IGFWLLDLAN NTVQGPARAL LADLSGPDQR NTANAVFCLW MAIGNILGFS AGASGKWQEW
FPFLTSRACC AACGNLKAAF LLAVVFLTIC TLVTIYFAKE IPFTSNKPTR IQDSAPLLDD
LQSKGLEHSK LNNGTANGIK YERVERDTDE QFGNSENEHQ DETYVDGPGS VLVNLLTSLR
HLPPAMHSVL IVMALTWLSW FPFFLFDTDW MGREVYHGDP TGDSLHMELY DQGVREGALG
LLLNSVVLGI SSFLIEPMCQ RMGARVVWAL SNFTVFACMA GTAVISLMSL SDDKNGIEYI
MRGNETTRTA AVIVFALLGF PLAITYSVPF SVTAEVTADS GGGQGLAIGV LNLAIVIPQM
IVSLGAGPWD QLFGGGNLPA FVLASVAAFA AGVIALQRLP TLSSSFKSTG FHIG
