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NAKR1_ARATH
ID   NAKR1_ARATH             Reviewed;         319 AA.
AC   Q8LDS4; Q9LZ42;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Protein SODIUM POTASSIUM ROOT DEFECTIVE 1 {ECO:0000303|PubMed:21193571};
DE            Short=NaKR1 {ECO:0000303|PubMed:21193571};
DE   AltName: Full=Heavy metal-associated plant protein 2 {ECO:0000303|PubMed:23368984};
DE            Short=AtHPP02 {ECO:0000303|PubMed:23368984};
DE   AltName: Full=Nuclear-enriched phloem companion cell gene 6 {ECO:0000303|PubMed:18354040};
DE            Short=NPCC6 {ECO:0000303|PubMed:18354040};
GN   Name=NAKR1 {ECO:0000303|PubMed:21193571};
GN   Synonyms=HPP02 {ECO:0000303|PubMed:23368984},
GN   NPCC6 {ECO:0000303|PubMed:18354040};
GN   OrderedLocusNames=At5g02600 {ECO:0000312|Araport:AT5G02600};
GN   ORFNames=T22P11_190 {ECO:0000312|EMBL:CAB85997.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=18354040; DOI=10.1104/pp.107.115246;
RA   Zhang C., Barthelson R.A., Lambert G.M., Galbraith D.W.;
RT   "Global characterization of cell-specific gene expression through
RT   fluorescence-activated sorting of nuclei.";
RL   Plant Physiol. 147:30-40(2008).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF CYS-260 AND CYS-263, GENE FAMILY, NOMENCLATURE,
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND METAL
RP   BINDING.
RX   PubMed=21193571; DOI=10.1105/tpc.110.080010;
RA   Tian H., Baxter I.R., Lahner B., Reinders A., Salt D.E., Ward J.M.;
RT   "Arabidopsis NPCC6/NaKR1 is a phloem mobile metal binding protein necessary
RT   for phloem function and root meristem maintenance.";
RL   Plant Cell 22:3963-3979(2010).
RN   [9]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=23368984; DOI=10.1111/febs.12159;
RA   de Abreu-Neto J.B., Turchetto-Zolet A.C., de Oliveira L.F., Zanettini M.H.,
RA   Margis-Pinheiro M.;
RT   "Heavy metal-associated isoprenylated plant protein (HIPP):
RT   characterization of a family of proteins exclusive to plants.";
RL   FEBS J. 280:1604-1616(2013).
RN   [10]
RP   FUNCTION, INDUCTION, INTERACTION WITH FT, LACK OF INTERACTION WITH TSF,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=27255839; DOI=10.1038/nplants.2016.75;
RA   Zhu Y., Liu L., Shen L., Yu H.;
RT   "NaKR1 regulates long-distance movement of FLOWERING LOCUS T in
RT   Arabidopsis.";
RL   Nat. Plants 2:16075-16075(2016).
CC   -!- FUNCTION: Required for root meristem maintenance after germination
CC       (PubMed:21193571). Involved in phloem translocation, starch
CC       accumulation and flowering (PubMed:21193571). Promotes flowering in the
CC       photoperiod pathway (PubMed:27255839). Regulates long-distance movement
CC       of FT from leaves to the shoot apex through the phloem stream
CC       (PubMed:27255839). {ECO:0000269|PubMed:21193571,
CC       ECO:0000269|PubMed:27255839}.
CC   -!- SUBUNIT: Interacts with FT, but not with TSF (TWIN SISTER OF FT).
CC       {ECO:0000269|PubMed:27255839}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21193571}. Nucleus
CC       {ECO:0000269|PubMed:21193571, ECO:0000269|PubMed:27255839}. Endoplasmic
CC       reticulum {ECO:0000269|PubMed:27255839}. Note=Mobile through
CC       plasmodesmata. {ECO:0000269|PubMed:21193571}.
CC   -!- TISSUE SPECIFICITY: Expressed in vascular tissues of cotyledons,
CC       rosette leaves and roots in developing seedlings before and during the
CC       floral transition (PubMed:27255839). Expressed specifically in the
CC       phloem companion cells (PubMed:18354040, PubMed:21193571). Not detected
CC       in embryos or seeds (PubMed:21193571). Not detected in the vegetative
CC       shoot apex (PubMed:27255839). {ECO:0000269|PubMed:18354040,
CC       ECO:0000269|PubMed:21193571, ECO:0000269|PubMed:27255839}.
CC   -!- DEVELOPMENTAL STAGE: Start to be expressed 1 day after germination
CC       (DAG) in the vascular tissue at the root-hypocotyl junction.
CC       {ECO:0000269|PubMed:21193571}.
CC   -!- INDUCTION: Circadian-regulation (PubMed:27255839). Up-regulated by CO
CC       in leaves in response to long days (PubMed:27255839).
CC       {ECO:0000269|PubMed:27255839}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB85997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL162971; CAB85997.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002688; AED90495.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90496.1; -; Genomic_DNA.
DR   EMBL; AK117227; BAC41903.1; -; mRNA.
DR   EMBL; BT008344; AAP37703.1; -; mRNA.
DR   EMBL; AK221722; BAD93718.1; -; mRNA.
DR   EMBL; AY085833; AAM63048.1; -; mRNA.
DR   PIR; T48281; T48281.
DR   RefSeq; NP_568105.1; NM_120338.4.
DR   RefSeq; NP_974723.1; NM_202994.3.
DR   AlphaFoldDB; Q8LDS4; -.
DR   SMR; Q8LDS4; -.
DR   STRING; 3702.AT5G02600.1; -.
DR   iPTMnet; Q8LDS4; -.
DR   PaxDb; Q8LDS4; -.
DR   PRIDE; Q8LDS4; -.
DR   ProteomicsDB; 251083; -.
DR   EnsemblPlants; AT5G02600.1; AT5G02600.1; AT5G02600.
DR   EnsemblPlants; AT5G02600.2; AT5G02600.2; AT5G02600.
DR   GeneID; 831874; -.
DR   Gramene; AT5G02600.1; AT5G02600.1; AT5G02600.
DR   Gramene; AT5G02600.2; AT5G02600.2; AT5G02600.
DR   KEGG; ath:AT5G02600; -.
DR   Araport; AT5G02600; -.
DR   TAIR; locus:2181718; AT5G02600.
DR   eggNOG; KOG1603; Eukaryota.
DR   HOGENOM; CLU_071922_0_0_1; -.
DR   InParanoid; Q8LDS4; -.
DR   OrthoDB; 1564517at2759; -.
DR   PhylomeDB; Q8LDS4; -.
DR   PRO; PR:Q8LDS4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LDS4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0010233; P:phloem transport; IMP:TAIR.
DR   GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR   GO; GO:0055078; P:sodium ion homeostasis; IMP:TAIR.
DR   CDD; cd00371; HMA; 1.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR044526; NAKR1/2/3.
DR   PANTHER; PTHR46119; PTHR46119; 1.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Metal-binding; Nucleus;
KW   Reference proteome; Zinc.
FT   CHAIN           1..319
FT                   /note="Protein SODIUM POTASSIUM ROOT DEFECTIVE 1"
FT                   /id="PRO_0000437273"
FT   DOMAIN          249..315
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..241
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT                   ECO:0000305|PubMed:21193571"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT                   ECO:0000305|PubMed:21193571"
FT   MUTAGEN         260
FT                   /note="C->G: Loss of metal binding; when associated with G-
FT                   263."
FT                   /evidence="ECO:0000269|PubMed:21193571"
FT   MUTAGEN         263
FT                   /note="C->G: Loss of metal binding; when associated with G-
FT                   260."
FT                   /evidence="ECO:0000269|PubMed:21193571"
SQ   SEQUENCE   319 AA;  34509 MW;  529F386C7DDE9AFC CRC64;
     MLCASQASTT TLCSTMDQTS QPSSSSSATI RLGGRAIDRH NPIIRDGRRL TPPPSPNLNP
     SSSSSSTYHT PLMTRLGLES SEQKRLAKRK SKKGDSDVGK SPVSCFSSDT PQGSSRYLLS
     NPVFFDGFVD SDPIPIPIDE PEITKADDLN NFHEDRLIIN ASKYLSTSAS FLEKKQPDFF
     EGFLDYEPVL SPDNPFSEPT KASPTASLSS LEDKDVSSPD FKFSPPPPPP PSPPQSSPPS
     PPEKNSSSDQ VVVLRVSLHC KGCAGKVKKH LSKLKGVTSY NIDFAAKKVT VTGDVTPLTV
     LASISKVKNA QFWPEIIQK
 
 
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