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CHX14_ARATH
ID   CHX14_ARATH             Reviewed;         829 AA.
AC   Q9LMJ1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cation/H(+) antiporter 14;
DE   AltName: Full=Protein CATION/H+ EXCHANGER 14;
DE            Short=AtCHX14;
GN   Name=CHX14; OrderedLocusNames=At1g06970; ORFNames=F10K1.31;
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].
RX   PubMed=18676662; DOI=10.1104/pp.108.124248;
RA   Zhao J., Cheng N.-H., Motes C.M., Blancaflor E.B., Moore M., Gonzales N.,
RA   Padmanaban S., Sze H., Ward J.M., Hirschi K.D.;
RT   "AtCHX13 is a plasma membrane K+ transporter.";
RL   Plant Physiol. 148:796-807(2008).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA   Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA   Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA   Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT   "Phylogenetic relationships within cation transporter families of
RT   Arabidopsis.";
RL   Plant Physiol. 126:1646-1667(2001).
RN   [6]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15347787; DOI=10.1104/pp.104.046003;
RA   Sze H., Padmanaban S., Cellier F., Honys D., Cheng N.-H., Bock K.W.,
RA   Conejero G., Li X., Twell D., Ward J.M., Hirschi K.D.;
RT   "Expression patterns of a novel AtCHX gene family highlight potential roles
RT   in osmotic adjustment and K+ homeostasis in pollen development.";
RL   Plant Physiol. 136:2532-2547(2004).
CC   -!- FUNCTION: May operate as a cation/H(+) antiporter. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in pollen but also
CC       detected in vegetative tissues like leaf trichomes and root vascular
CC       tissues. {ECO:0000269|PubMed:15347787}.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC       transporter (TC 2.A.37) family. CHX (TC 2.A.37.4) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; EF571900; ABS19937.1; -; mRNA.
DR   EMBL; AC067971; AAF82222.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28061.1; -; Genomic_DNA.
DR   EMBL; DQ446234; ABE65605.1; -; mRNA.
DR   PIR; D86204; D86204.
DR   RefSeq; NP_172178.1; NM_100570.2.
DR   AlphaFoldDB; Q9LMJ1; -.
DR   SMR; Q9LMJ1; -.
DR   STRING; 3702.AT1G06970.1; -.
DR   iPTMnet; Q9LMJ1; -.
DR   PaxDb; Q9LMJ1; -.
DR   PRIDE; Q9LMJ1; -.
DR   ProteomicsDB; 246839; -.
DR   EnsemblPlants; AT1G06970.1; AT1G06970.1; AT1G06970.
DR   GeneID; 837207; -.
DR   Gramene; AT1G06970.1; AT1G06970.1; AT1G06970.
DR   KEGG; ath:AT1G06970; -.
DR   Araport; AT1G06970; -.
DR   TAIR; locus:2007392; AT1G06970.
DR   eggNOG; KOG1650; Eukaryota.
DR   HOGENOM; CLU_005126_6_1_1; -.
DR   InParanoid; Q9LMJ1; -.
DR   OMA; FKMGVQI; -.
DR   OrthoDB; 336706at2759; -.
DR   PhylomeDB; Q9LMJ1; -.
DR   PRO; PR:Q9LMJ1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMJ1; baseline and differential.
DR   Genevisible; Q9LMJ1; AT.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006885; P:regulation of pH; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Antiport; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..829
FT                   /note="Cation/H(+) antiporter 14"
FT                   /id="PRO_0000394984"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         827
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SUQ7"
SQ   SEQUENCE   829 AA;  92160 MW;  2DB677679A6CB5EE CRC64;
     MSKLDLEEVN SMQRGKVHGP FLVENMVCQK NHMLTSKGVF LGSDPLKYAM PLMLLQMSVI
     IITSRLLYRL LKPLKQGMIS AQVLAGIILG PSLFGQSSAY MQMFLPISGK ITLQTLSNLG
     FFIHLFLLGL RIDASIIRKA GSKAILIGTA SYALPFSLGN LTVLFLKNTY NLPPDVVHCI
     STVISLNAMT SFPVTTTVLA ELNILNSDLG RLATNCSIVC EAFSWIVALV FRMFLRDGTL
     ASVWSFVWVT ALILVIFFVC RPAIIWLTER RSISIDKAGE IPFFPIIMVL LTISLTSEVL
     GVHAAFGAFW LGVSLPDGPP LGTGLTTKLE MFATSLMLPC FISISGLQTN FFIIGESHVK
     IIEAVILITY GCKFLGTAAA SAYCNIQIGD AFSLALLMCC QGVIEIYTCV MWKDEKVLNT
     ECFNLLIITL LLVTGISRFL VVCLYDPSKR YRSKSKRTIL DTRQRNLQFR LLLCVYNVEN
     VPSMVNLLEA SYPSRFSPIS VFTLHLVELK GRAHAVLVPH HQMNKLDPNT VQSTHIVNGF
     QRFEQQNQGT LMAQHFTAAA PFSSINDDIC TLALDKKATL IVIPFHKQYA IDGTVDHVNP
     SIRNINLNVL EKAPCSVGIF IDRGETEGRR SVLMSYTWRN VAVIFIEGRD DAEALAFSMR
     IAEHPEVSVT MIHFRHKSSL QQNHVVDVES ELAESYLIND FKNFAMSKPK ISYREEIVRD
     GVETTQVISS LGDSFDLVVV GRDHDLESSV LYGLTDWSEC PELGVIGDMF ASSDFHFSVL
     VIHQQEGDSL AMDNSYKLPA SPHRVGDPRV HPRFSVEEGF TSVDLHSNR
 
 
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