SUC5_ARATH
ID SUC5_ARATH Reviewed; 512 AA.
AC Q9C8X2; Q9FNY9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sucrose transport protein SUC5;
DE AltName: Full=Sucrose permease 5;
DE AltName: Full=Sucrose-proton symporter 5;
GN Name=SUC5; OrderedLocusNames=At1g71890; ORFNames=F17M19.4;
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. Landsberg erecta; TISSUE=Seedling;
RX PubMed=11115131; DOI=10.1046/j.1365-313x.2000.00900.x;
RA Ludwig A., Stolz J., Sauer N.;
RT "Plant sucrose-H(+) symporters mediate the transport of vitamin H.";
RL Plant J. 24:503-509(2000).
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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=16146522; DOI=10.1111/j.1365-313x.2005.02496.x;
RA Baud S., Wuilleme S., Lemoine R., Kronenberger J., Caboche M., Lepiniec L.,
RA Rochat C.;
RT "The AtSUC5 sucrose transporter specifically expressed in the endosperm is
RT involved in early seed development in Arabidopsis.";
RL Plant J. 43:824-836(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23031218; DOI=10.1111/tpj.12037;
RA Pommerrenig B., Popko J., Heilmann M., Schulmeister S., Dietel K.,
RA Schmitt B., Stadler R., Feussner I., Sauer N.;
RT "SUCROSE TRANSPORTER 5 supplies Arabidopsis embryos with biotin and affects
RT triacylglycerol accumulation.";
RL Plant J. 73:392-404(2013).
CC -!- FUNCTION: Responsible in a heterologous system for the transport of
CC sucrose into the cell, with the concomitant uptake of protons (symport
CC system). Can also transport biotin, and probably maltose at a lesser
CC rate. In planta, the role of SUC5 for the transport of sucrose seems to
CC be negligible. Plays a role in the nutrition of the filial tissues
CC during early seed development and is probably involved in the import of
CC biotin into the endosperm and the embryo epidermis.
CC {ECO:0000269|PubMed:11115131, ECO:0000269|PubMed:16146522,
CC ECO:0000269|PubMed:23031218}.
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:11115131}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for sucrose (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11115131};
CC Note=KM for biotin could not determined because the concentration of
CC biotin needed to saturate the transporter was slightly below the
CC upper limit of biotin solubility in water.;
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23031218};
CC Multi-pass membrane protein {ECO:0000305|PubMed:23031218}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the endosperm and on
CC the epidermis of the outer surface of the cotyledons of torpedo-stage
CC or older embryos. {ECO:0000269|PubMed:11115131,
CC ECO:0000269|PubMed:23031218}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds 3 to 4 days after
CC flowering (DAF) in the micropylar region of the endosperm. At 6 DAF,
CC expressed the micropylar pole. At the globular stage of embryo
CC development, expressed specifically in the endosperm and then extends
CC to the chalazal pole of the endosperm at the torpedo stage. The
CC expression decreases at the upturned-U stage, 9 DAF, as the endosperm
CC becomes limited to a few cell layers embedding the maturing embryo.
CC Expressed in the embryo at the later stages of development.
CC {ECO:0000269|PubMed:16146522, ECO:0000269|PubMed:23031218}.
CC -!- DISRUPTION PHENOTYPE: Significant but transient reduction in fatty acid
CC concentration in developing seeds. Slight delay in embryo development.
CC {ECO:0000269|PubMed:16146522}.
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; AJ252133; CAC19851.1; -; mRNA.
DR EMBL; AC021665; AAG52226.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35248.1; -; Genomic_DNA.
DR PIR; F96741; F96741.
DR RefSeq; NP_177334.1; NM_105847.3.
DR AlphaFoldDB; Q9C8X2; -.
DR STRING; 3702.AT1G71890.1; -.
DR TCDB; 2.A.2.4.12; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR iPTMnet; Q9C8X2; -.
DR PaxDb; Q9C8X2; -.
DR PRIDE; Q9C8X2; -.
DR ProteomicsDB; 245353; -.
DR EnsemblPlants; AT1G71890.1; AT1G71890.1; AT1G71890.
DR GeneID; 843520; -.
DR Gramene; AT1G71890.1; AT1G71890.1; AT1G71890.
DR KEGG; ath:AT1G71890; -.
DR Araport; AT1G71890; -.
DR TAIR; locus:2016074; AT1G71890.
DR eggNOG; KOG0637; Eukaryota.
DR HOGENOM; CLU_025234_3_0_1; -.
DR InParanoid; Q9C8X2; -.
DR OMA; RVANECF; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; Q9C8X2; -.
DR SABIO-RK; Q9C8X2; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q9C8X2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8X2; baseline and differential.
DR Genevisible; Q9C8X2; 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:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IBA:GO_Central.
DR GO; GO:0048316; P:seed development; IMP:UniProtKB.
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..512
FT /note="Sucrose transport protein SUC5"
FT /id="PRO_0000122526"
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..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..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 REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q39232"
FT CONFLICT 26
FT /note="G -> S (in Ref. 1; CAC19851)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="V -> I (in Ref. 1; CAC19851)"
FT /evidence="ECO:0000305"
FT CONFLICT 510..512
FT /note="Missing (in Ref. 1; CAC19851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 54834 MW; 633E80B65739E363 CRC64;
MGALEAERAA NNATALETQS SPEDLGQPSP LRKIISVASI AAGVQFGWAL QLSLLTPYIQ
LLGIPHKWSS YMWLCGPISG MIVQPIVGYH SDRCESRFGR RRPFIAAGVA LVAVSVFLIG
FAADMGHSFG DKLENKVRTR AIIIFLTGFW FLDVANNTLQ GPCRAFLADL AAGDAKKTRV
ANACFSFFMA VGNVLGYAAG SYTNLHKMFP FTMTKACDIY CANLKTCFFL SITLLLIVTF
SSLWYVKDKQ WSPPQGDKEE KTSSLFFFGE IFGAVRHMKR PMVMLLIVTV INWIAWFPFI
LYDTDWMGRE VYGGNSDGDE RSKKLYDQGV QAGALGLMFN SILLGFVSLG VESIGRKMGG
AKRLWGCVNF ILAIGLAMTV LVTKSAEHHR EIAGPLAGPS SGIKAGVFSL FTVLGIPLAI
TYSIPFALAS IFSTNSGAGQ GLSLGVLNIA ICIPQMIVSF SSGPLDAQFG GGNLPSFVVG
AIAAAVSGVL ALTVLPSPPP DAPAMSGAMG FH
