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NHAS3_SYNY3
ID   NHAS3_SYNY3             Reviewed;         461 AA.
AC   Q55190;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=High-affinity Na(+)/H(+) antiporter NhaS3;
DE   AltName: Full=Sodium/proton antiporter NhaS3;
GN   Name=nhaS3; OrderedLocusNames=sll0689;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND GENE NAME.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=11157951; DOI=10.1128/jb.183.4.1376-1384.2001;
RA   Inaba M., Sakamoto A., Murata N.;
RT   "Functional expression in Escherichia coli of low-affinity and high-
RT   affinity Na(+)(Li(+))/H(+) antiporters of Synechocystis.";
RL   J. Bacteriol. 183:1376-1384(2001).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=11996656; DOI=10.1023/a:1015281906254;
RA   Elanskaya I.V., Karandashova I.V., Bogachev A.V., Hagemann M.;
RT   "Functional analysis of the Na+/H+ antiporter encoding genes of the
RT   cyanobacterium Synechocystis PCC 6803.";
RL   Biochemistry (Mosc.) 67:432-440(2002).
RN   [4]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION,
RP   AND MUTAGENESIS OF ASP-99; GLU-114; GLU-121; ASP-217; ASP-218; GLU-359 AND
RP   GLU-402.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=19372598; DOI=10.1074/jbc.m109.001875;
RA   Tsunekawa K., Shijuku T., Hayashimoto M., Kojima Y., Onai K., Morishita M.,
RA   Ishiura M., Kuroda T., Nakamura T., Kobayashi H., Sato M., Toyooka K.,
RA   Matsuoka K., Omata T., Uozumi N.;
RT   "Identification and characterization of the Na+/H+ antiporter Nhas3 from
RT   the thylakoid membrane of Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 284:16513-16521(2009).
CC   -!- FUNCTION: Na(+)/H(+) antiporter that transports sodium from the
CC       cytoplasm into the thylakoid lumen in exchange for protons. Contributes
CC       to sodium homeostasis and tolerance. Has also Li(+)/H(+) antiport
CC       activity under K(+)-free conditions, but not under K(+)-rich
CC       conditions. {ECO:0000269|PubMed:11157951, ECO:0000269|PubMed:11996656,
CC       ECO:0000269|PubMed:19372598}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.7 mM for Na(+) (under K(+)-free conditions)
CC         {ECO:0000269|PubMed:11157951, ECO:0000269|PubMed:19372598};
CC         KM=0.01 mM for Li(+) (under K(+)-free conditions)
CC         {ECO:0000269|PubMed:11157951, ECO:0000269|PubMed:19372598};
CC       pH dependence:
CC         Activity is pH-independent. {ECO:0000269|PubMed:11157951,
CC         ECO:0000269|PubMed:19372598};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000269|PubMed:19372598}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19372598}.
CC   -!- INDUCTION: Induced in response to increased CO(2) concentrations.
CC       Expression is under circadian control. {ECO:0000269|PubMed:19372598}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA10332.1; -; Genomic_DNA.
DR   PIR; S74414; S74414.
DR   AlphaFoldDB; Q55190; -.
DR   SMR; Q55190; -.
DR   IntAct; Q55190; 1.
DR   STRING; 1148.1001188; -.
DR   TCDB; 2.A.37.2.4; the monovalent cation:proton antiporter-2 (cpa2) family.
DR   PaxDb; Q55190; -.
DR   EnsemblBacteria; BAA10332; BAA10332; BAA10332.
DR   KEGG; syn:sll0689; -.
DR   eggNOG; COG0475; Bacteria.
DR   InParanoid; Q55190; -.
DR   OMA; CAWATTA; -.
DR   PhylomeDB; Q55190; -.
DR   SABIO-RK; Q55190; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
PE   1: Evidence at protein level;
KW   Antiport; Ion transport; Membrane; Reference proteome; Sodium;
KW   Sodium transport; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..461
FT                   /note="High-affinity Na(+)/H(+) antiporter NhaS3"
FT                   /id="PRO_0000423929"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         99
FT                   /note="D->A: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         114
FT                   /note="E->A: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         121
FT                   /note="E->Q: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         217
FT                   /note="D->A,N: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         218
FT                   /note="D->A,N: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         359
FT                   /note="E->Q: Strong decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
FT   MUTAGEN         402
FT                   /note="E->A,Q: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:19372598"
SQ   SEQUENCE   461 AA;  47872 MW;  832E3E7BC17622F6 CRC64;
     MFMNPLLPPL WPMIATAVET ETEIAPLVLA GVLLSLVVIY FASKLGGEVC LRLNLPPVLG
     ELVGGVLVGV SALKLLLFPE GGLAPEDSLV IQLLMGSADL SPEAAQSVFS AQSEVISVIS
     ELGVIILLFE IGLESNLKEL IRVGPQAAIV AVVGVVTPFS LGTIGLMTIF GVAAIPAIFA
     GAALTATSIG ITAKVLAEIN RLSSNEGQII IGAAVLDDIL GIIVLAVVGS LVKTGEIQIS
     NIIYLILSAT GFVVGSILIG RLLSPFYVSL VNRMKTRGQL LLVSICVAFV LSYIAQIVQL
     EAILGSFAAG LILAETEKRE DLEEQILPLA DFFVPVFFVC VGAKTDVSVL NPAVPANREG
     LIIAAFLILV AIVGKVVTGF TLFGKSELNK LAIGVGMIPR GEVGLVFAGV GAASGALDPA
     TDAAIIVMVI VTTFVAPPWL RAVFEGAKKE EAPEKPVPTP D
 
 
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