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Sucrose transport protein SUC1 (Sucrose permease 1) (Sucrose-proton symporter 1)

 SUC1_ARATH              Reviewed;         513 AA.
Q39232;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 120.
RecName: Full=Sucrose transport protein SUC1;
AltName: Full=Sucrose permease 1;
AltName: Full=Sucrose-proton symporter 1;
Name=SUC1; OrderedLocusNames=At1g71880; ORFNames=F17M19.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND ENZYME REGULATION.
STRAIN=cv. Columbia;
PubMed=7920705; DOI=10.1046/j.1365-313X.1994.6010067.x;
Sauer N., Stolz J.;
"SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana;
expression and characterization in baker's yeast and identification of
the histidine-tagged protein.";
Plant J. 6:67-77(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION.
PubMed=9307438; DOI=10.1007/s002329900275;
Zhou J.-J., Theodoulou F., Sauer N., Sanders D., Miller A.J.;
"A kinetic model with ordered cytoplasmic dissociation for SUC1, an
Arabidopsis H(+)/sucrose cotransporter expressed in Xenopus oocytes.";
J. Membr. Biol. 159:113-125(1997).
[7]
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND MUTAGENESIS OF
HIS-65.
PubMed=9671798; DOI=10.1073/pnas.95.15.9025;
Lu J.M.-Y., Bush D.R.;
"His-65 in the proton-sucrose symporter is an essential amino acid
whose modification with site-directed mutagenesis increases transport
activity.";
Proc. Natl. Acad. Sci. U.S.A. 95:9025-9030(1998).
[8]
FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=10476074; DOI=10.1046/j.1365-313X.1999.00527.x;
Stadler R., Truernit E., Gahrtz M., Sauer N.;
"The AtSUC1 sucrose carrier may represent the osmotic driving force
for anther dehiscence and pollen tube growth in Arabidopsis.";
Plant J. 19:269-278(1999).
[9]
INDUCTION.
PubMed=11673631; DOI=10.1093/pcp/pce150;
Furuichi T., Mori I.C., Takahashi K., Muto S.;
"Sugar-induced increase in cytosolic Ca(2+) in Arabidopsis thaliana
whole plants.";
Plant Cell Physiol. 42:1149-1155(2001).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Seedling;
PubMed=17586839; DOI=10.1074/mcp.M700164-MCP200;
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,
Schulze W.X.;
"Temporal analysis of sucrose-induced phosphorylation changes in
plasma membrane proteins of Arabidopsis.";
Mol. Cell. Proteomics 6:1711-1726(2007).
[11]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=18359840; DOI=10.1104/pp.108.118992;
Sivitz A.B., Reinders A., Ward J.M.;
"Arabidopsis sucrose transporter AtSUC1 is important for pollen
germination and sucrose-induced anthocyanin accumulation.";
Plant Physiol. 147:92-100(2008).
-!- FUNCTION: Responsible for the transport of sucrose into the cell,
with the concomitant uptake of protons (symport system). This
transport is both voltage- and energy-dependent. Can also
transport other glucosides such as maltose, alpha-phenylglucoside
and beta-phenylglucoside. May also transport biotin. Required for
normal pollen germination and anthocyanin accumulation induced by
sucrose. {ECO:0000269|PubMed:10476074,
ECO:0000269|PubMed:18359840, ECO:0000269|PubMed:7920705,
ECO:0000269|PubMed:9307438}.
-!- ENZYME REGULATION: Inhibited by DEPC, protonophores (e.g.
dinitrophenol and carbonyl cyanide m-chlorophenyl-hydrazone
(CCCP)), and SH group inhibitors (e.g. N-ethylmaleimide (NEM) and
p-chloromercuriphenyl sulphonic acid (PCMPS)).
{ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=450 uM for sucrose (at pH 5.5 and 30 degrees Celsius)
{ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
Vmax=45 umol/h/g enzyme (without glucose)
{ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
Vmax=154 umol/h/g enzyme (in the presence of 10 mM glucose)
{ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
pH dependence:
Optimum pH is 5-6. {ECO:0000269|PubMed:7920705,
ECO:0000269|PubMed:9671798};
-!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in flowers (at protein level).
Highly expressed in pollen. Expressed in pollen tubes and root
vascular cylinder, pericycle and endodermis.
{ECO:0000269|PubMed:10476074, ECO:0000269|PubMed:18359840}.
-!- DEVELOPMENTAL STAGE: Transcripts accumulate in mature pollen
before and during germination, but translation starts only when
pollen germination initiates, and continues in pollen tubes.
Expressed in cells surrounding the vascular bundle of the anther
connective tissue, mostly at the dehiscence time. Also present in
a ring of parenchymatic cells between the xylem vessels of the
style (upper end of the transmitting tract toward which pollen
tubes grow). Expressed in the epidermal cell layers of funiculi
(at protein level). {ECO:0000269|PubMed:10476074}.
-!- INDUCTION: By exogenous sucrose in roots. Induced by sucrose
depletion. {ECO:0000269|PubMed:11673631,
ECO:0000269|PubMed:18359840}.
-!- DISRUPTION PHENOTYPE: Defective pollen with low rate of
germination. Reduction of anthocyanin accumulation in response to
exogenous sucrose or maltose. {ECO:0000269|PubMed:18359840}.
-!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH)
cation symporter transporter (TC 2.A.2.4) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X75365; CAA53147.1; -; mRNA.
EMBL; AC021665; AAG52225.1; -; Genomic_DNA.
EMBL; CP002684; AEE35247.1; -; Genomic_DNA.
EMBL; AY049275; AAK83617.1; -; mRNA.
EMBL; BT020416; AAV97807.1; -; mRNA.
PIR; S38197; S38197.
RefSeq; NP_177333.1; NM_105846.4.
UniGene; At.23741; -.
ProteinModelPortal; Q39232; -.
BioGrid; 28739; 4.
STRING; 3702.AT1G71880.1; -.
TCDB; 2.A.2.4.1; the glycoside-pentoside-hexuronide (gph):cation symporter family.
iPTMnet; Q39232; -.
PaxDb; Q39232; -.
PRIDE; Q39232; -.
EnsemblPlants; AT1G71880.1; AT1G71880.1; AT1G71880.
GeneID; 843519; -.
Gramene; AT1G71880.1; AT1G71880.1; AT1G71880.
KEGG; ath:AT1G71880; -.
Araport; AT1G71880; -.
TAIR; locus:2016069; AT1G71880.
eggNOG; KOG0637; Eukaryota.
eggNOG; ENOG410XPTR; LUCA.
HOGENOM; HOG000239187; -.
InParanoid; Q39232; -.
KO; K15378; -.
OMA; GIAWAGM; -.
OrthoDB; EOG09360EF1; -.
PhylomeDB; Q39232; -.
BioCyc; MetaCyc:AT1G71880-MONOMER; -.
Reactome; R-ATH-70153; Glucose transport.
SABIO-RK; Q39232; -.
UniPathway; UPA00238; -.
PRO; PR:Q39232; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q39232; baseline and differential.
Genevisible; Q39232; AT.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0008506; F:sucrose:proton symporter activity; IDA:TAIR.
GO; GO:0009846; P:pollen germination; IMP:TAIR.
GO; GO:0009624; P:response to nematode; IEP:TAIR.
GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
CDD; cd06174; MFS; 1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005989; Suc_symporter_pln.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR01301; GPH_sucrose; 1.
1: Evidence at protein level;
Complete proteome; Membrane; Phosphoprotein; Reference proteome;
Sugar transport; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 513 Sucrose transport protein SUC1.
/FTId=PRO_0000122522.
TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.
TRANSMEM 33 53 Helical. {ECO:0000255}.
TOPO_DOM 54 67 Extracellular. {ECO:0000255}.
TRANSMEM 68 88 Helical. {ECO:0000255}.
TOPO_DOM 89 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 122 Helical. {ECO:0000255}.
TOPO_DOM 123 139 Extracellular. {ECO:0000255}.
TRANSMEM 140 160 Helical. {ECO:0000255}.
TOPO_DOM 161 178 Cytoplasmic. {ECO:0000255}.
TRANSMEM 179 199 Helical. {ECO:0000255}.
TOPO_DOM 200 224 Extracellular. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
TOPO_DOM 246 282 Cytoplasmic. {ECO:0000255}.
TRANSMEM 283 303 Helical. {ECO:0000255}.
TOPO_DOM 304 334 Extracellular. {ECO:0000255}.
TRANSMEM 335 355 Helical. {ECO:0000255}.
TOPO_DOM 356 365 Cytoplasmic. {ECO:0000255}.
TRANSMEM 366 386 Helical. {ECO:0000255}.
TOPO_DOM 387 408 Extracellular. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 441 Cytoplasmic. {ECO:0000255}.
TRANSMEM 442 462 Helical. {ECO:0000255}.
TOPO_DOM 463 474 Extracellular. {ECO:0000255}.
TRANSMEM 475 495 Helical. {ECO:0000255}.
TOPO_DOM 496 513 Cytoplasmic. {ECO:0000255}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:17586839}.
MUTAGEN 65 65 H->C: No sucrose transport activity, high
instability.
{ECO:0000269|PubMed:9671798}.
MUTAGEN 65 65 H->D,G,L,Y: Reduced sucrose transport
activity. {ECO:0000269|PubMed:9671798}.
MUTAGEN 65 65 H->K: Enhanced sucrose transport
activity. {ECO:0000269|PubMed:9671798}.
MUTAGEN 65 65 H->Q: Reduced sensitivity to DEPC.
{ECO:0000269|PubMed:9671798}.
MUTAGEN 65 65 H->R: Enhanced sucrose transport
activity, reduced sensitivity to DEPC.
{ECO:0000269|PubMed:9671798}.
MUTAGEN 65 65 H->S: Reduced sucrose transport activity,
reduced sensitivity to DEPC.
{ECO:0000269|PubMed:9671798}.
SEQUENCE 513 AA; 54858 MW; 3F44FE0B318D5250 CRC64;
MGAYETEKPT KDAAALETQS PEDFDQPSPL RKIISVASIA AGVQFGWALQ LSLLTPYVQL
LGIPHKWSSL IWLCGPVSGM IVQPIVGFHS DRCRSKFGRR RPFIATGAAL VAVAVFLIGY
AADFGYKMGD KLEEKVKVRA IGIFALGFWI LDVANNTLQG PCRAFLADLA AGDAKRTRVA
NAFFSFFMAV GNVLGYAAGS YTNLHKMFPF TMTKACDIYC ANLKTCFFLS ITLLLIVTVT
SLWYVNDKQW SPPPRNADDD EKTSSVPLFG EIFGAFKVMK RPMWMLLIVT ALNWIAWFPF
LLFDTDWMGR EVFGGDSDGN ERSKKLYSLG VQSGAMGLMF NSIVLGFMSL GVEWIGRKLG
GAKRLWGIVN FILAAGLAMT VLVTKFAEDH RKTAGDLAGP SASVKAGALS LFAVLGIPLA
ITFSTPFALA SIFSSCSGAG QGLSLGVLNL AIVIPQMIVS LGGGPFDALF GGGNLPAFIV
AAIAAAISGV LALTVLPSPP PDAPKATTMG GFH


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