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SUC1_ARATH
ID   SUC1_ARATH              Reviewed;         513 AA.
AC   Q39232;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Sucrose transport protein SUC1;
DE   AltName: Full=Sucrose permease 1;
DE   AltName: Full=Sucrose-proton symporter 1;
GN   Name=SUC1; OrderedLocusNames=At1g71880; ORFNames=F17M19.3;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
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].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=9307438; DOI=10.1007/s002329900275;
RA   Zhou J.-J., Theodoulou F., Sauer N., Sanders D., Miller A.J.;
RT   "A kinetic model with ordered cytoplasmic dissociation for SUC1, an
RT   Arabidopsis H(+)/sucrose cotransporter expressed in Xenopus oocytes.";
RL   J. Membr. Biol. 159:113-125(1997).
RN   [7]
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   HIS-65.
RX   PubMed=9671798; DOI=10.1073/pnas.95.15.9025;
RA   Lu J.M.-Y., Bush D.R.;
RT   "His-65 in the proton-sucrose symporter is an essential amino acid whose
RT   modification with site-directed mutagenesis increases transport activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9025-9030(1998).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=10476074; DOI=10.1046/j.1365-313x.1999.00527.x;
RA   Stadler R., Truernit E., Gahrtz M., Sauer N.;
RT   "The AtSUC1 sucrose carrier may represent the osmotic driving force for
RT   anther dehiscence and pollen tube growth in Arabidopsis.";
RL   Plant J. 19:269-278(1999).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Seedling;
RX   PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA   Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT   "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT   membrane proteins of Arabidopsis.";
RL   Mol. Cell. Proteomics 6:1711-1726(2007).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18359840; DOI=10.1104/pp.108.118992;
RA   Sivitz A.B., Reinders A., Ward J.M.;
RT   "Arabidopsis sucrose transporter AtSUC1 is important for pollen germination
RT   and sucrose-induced anthocyanin accumulation.";
RL   Plant Physiol. 147:92-100(2008).
CC   -!- FUNCTION: Responsible for the transport of sucrose into the cell, with
CC       the concomitant uptake of protons (symport system). This transport is
CC       both voltage- and energy-dependent. Can also transport other glucosides
CC       such as maltose, alpha-phenylglucoside and beta-phenylglucoside. May
CC       also transport biotin. Required for normal pollen germination and
CC       anthocyanin accumulation induced by sucrose.
CC       {ECO:0000269|PubMed:10476074, ECO:0000269|PubMed:18359840,
CC       ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9307438}.
CC   -!- ACTIVITY REGULATION: Inhibited by DEPC, protonophores (e.g.
CC       dinitrophenol and carbonyl cyanide m-chlorophenyl-hydrazone (CCCP)),
CC       and SH group inhibitors (e.g. N-ethylmaleimide (NEM) and p-
CC       chloromercuriphenyl sulphonic acid (PCMPS)).
CC       {ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=450 uM for sucrose (at pH 5.5 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
CC         Vmax=45 umol/h/g enzyme (without glucose)
CC         {ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
CC         Vmax=154 umol/h/g enzyme (in the presence of 10 mM glucose)
CC         {ECO:0000269|PubMed:7920705, ECO:0000269|PubMed:9671798};
CC       pH dependence:
CC         Optimum pH is 5-6. {ECO:0000269|PubMed:7920705,
CC         ECO:0000269|PubMed:9671798};
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers (at protein level). Highly
CC       expressed in pollen. Expressed in pollen tubes and root vascular
CC       cylinder, pericycle and endodermis. {ECO:0000269|PubMed:10476074,
CC       ECO:0000269|PubMed:18359840}.
CC   -!- DEVELOPMENTAL STAGE: Transcripts accumulate in mature pollen before and
CC       during germination, but translation starts only when pollen germination
CC       initiates, and continues in pollen tubes. Expressed in cells
CC       surrounding the vascular bundle of the anther connective tissue, mostly
CC       at the dehiscence time. Also present in a ring of parenchymatic cells
CC       between the xylem vessels of the style (upper end of the transmitting
CC       tract toward which pollen tubes grow). Expressed in the epidermal cell
CC       layers of funiculi (at protein level). {ECO:0000269|PubMed:10476074}.
CC   -!- INDUCTION: By exogenous sucrose in roots. Induced by sucrose depletion.
CC       {ECO:0000269|PubMed:11673631, ECO:0000269|PubMed:18359840}.
CC   -!- DISRUPTION PHENOTYPE: Defective pollen with low rate of germination.
CC       Reduction of anthocyanin accumulation in response to exogenous sucrose
CC       or maltose. {ECO:0000269|PubMed:18359840}.
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; X75365; CAA53147.1; -; mRNA.
DR   EMBL; AC021665; AAG52225.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35247.1; -; Genomic_DNA.
DR   EMBL; AY049275; AAK83617.1; -; mRNA.
DR   EMBL; BT020416; AAV97807.1; -; mRNA.
DR   PIR; S38197; S38197.
DR   RefSeq; NP_177333.1; NM_105846.4.
DR   AlphaFoldDB; Q39232; -.
DR   BioGRID; 28739; 6.
DR   STRING; 3702.AT1G71880.1; -.
DR   TCDB; 2.A.2.4.1; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR   iPTMnet; Q39232; -.
DR   PaxDb; Q39232; -.
DR   PRIDE; Q39232; -.
DR   ProteomicsDB; 245227; -.
DR   EnsemblPlants; AT1G71880.1; AT1G71880.1; AT1G71880.
DR   GeneID; 843519; -.
DR   Gramene; AT1G71880.1; AT1G71880.1; AT1G71880.
DR   KEGG; ath:AT1G71880; -.
DR   Araport; AT1G71880; -.
DR   TAIR; locus:2016069; AT1G71880.
DR   eggNOG; KOG0637; Eukaryota.
DR   HOGENOM; CLU_025234_3_0_1; -.
DR   InParanoid; Q39232; -.
DR   OMA; GIAWAGM; -.
DR   OrthoDB; 1230185at2759; -.
DR   PhylomeDB; Q39232; -.
DR   BioCyc; MetaCyc:AT1G71880-MON; -.
DR   SABIO-RK; Q39232; -.
DR   UniPathway; UPA00238; -.
DR   PRO; PR:Q39232; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q39232; baseline and differential.
DR   Genevisible; Q39232; 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:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0008506; F:sucrose:proton symporter activity; IDA:TAIR.
DR   GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR   GO; GO:0009624; P:response to nematode; HEP:TAIR.
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   Membrane; Phosphoprotein; Reference proteome; Sugar transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..513
FT                   /note="Sucrose transport protein SUC1"
FT                   /id="PRO_0000122522"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..67
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..224
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..334
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..474
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        496..513
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17586839"
FT   MUTAGEN         65
FT                   /note="H->C: No sucrose transport activity, high
FT                   instability."
FT                   /evidence="ECO:0000269|PubMed:9671798"
FT   MUTAGEN         65
FT                   /note="H->D,G,L,Y: Reduced sucrose transport activity."
FT                   /evidence="ECO:0000269|PubMed:9671798"
FT   MUTAGEN         65
FT                   /note="H->K: Enhanced sucrose transport activity."
FT                   /evidence="ECO:0000269|PubMed:9671798"
FT   MUTAGEN         65
FT                   /note="H->Q: Reduced sensitivity to DEPC."
FT                   /evidence="ECO:0000269|PubMed:9671798"
FT   MUTAGEN         65
FT                   /note="H->R: Enhanced sucrose transport activity, reduced
FT                   sensitivity to DEPC."
FT                   /evidence="ECO:0000269|PubMed:9671798"
FT   MUTAGEN         65
FT                   /note="H->S: Reduced sucrose transport activity, reduced
FT                   sensitivity to DEPC."
FT                   /evidence="ECO:0000269|PubMed:9671798"
SQ   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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