CXIP4_ARATH
ID CXIP4_ARATH Reviewed; 332 AA.
AC Q84Y18; Q8L8W3; Q9ZV23;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=CAX-interacting protein 4;
GN Name=CXIP4; OrderedLocusNames=At2g28910; ORFNames=F8N16.20;
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], AND INTERACTION WITH CAX1.
RX PubMed=12480930; DOI=10.1074/jbc.m210883200;
RA Cheng N.-H., Hirschi K.D.;
RT "Cloning and characterization of CXIP1 A novel PICOT domain-containing
RT Arabidopsis protein that associates with CAX1.";
RL J. Biol. Chem. 278:6503-6509(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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], AND INTERACTION WITH CAX1.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14960315; DOI=10.1016/s0014-5793(04)00036-5;
RA Cheng N.-H., Liu J.-Z., Nelson R.S., Hirschi K.D.;
RT "Characterization of CXIP4, a novel Arabidopsis protein that activates the
RT H+/Ca2+ antiporter, CAX1.";
RL FEBS Lett. 559:99-106(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: May regulate CAX1 cation transporter.
CC {ECO:0000269|PubMed:14960315}.
CC -!- SUBUNIT: Interacts with CAX1. {ECO:0000269|PubMed:12480930,
CC ECO:0000269|Ref.5}.
CC -!- INTERACTION:
CC Q84Y18; P46639: KNAT1; NbExp=3; IntAct=EBI-25522794, EBI-530486;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14960315}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots, and at lower
CC levels in flowers. {ECO:0000269|PubMed:14960315}.
CC -!- INDUCTION: Slightly induced by Ca(2+). {ECO:0000269|PubMed:14960315}.
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DR EMBL; AY163162; AAO17572.1; -; mRNA.
DR EMBL; AC005727; AAC79595.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08187.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61431.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61432.1; -; Genomic_DNA.
DR EMBL; AF428457; AAL16226.1; -; mRNA.
DR EMBL; AY142061; AAM98325.1; -; mRNA.
DR EMBL; AY088773; AAM67086.1; -; mRNA.
DR PIR; D84690; D84690.
DR RefSeq; NP_001323648.1; NM_001336192.1.
DR RefSeq; NP_001323649.1; NM_001336191.1.
DR RefSeq; NP_565678.1; NM_128450.2.
DR AlphaFoldDB; Q84Y18; -.
DR BioGRID; 2790; 3.
DR IntAct; Q84Y18; 1.
DR STRING; 3702.AT2G28910.1; -.
DR iPTMnet; Q84Y18; -.
DR PaxDb; Q84Y18; -.
DR PRIDE; Q84Y18; -.
DR ProteomicsDB; 220432; -.
DR EnsemblPlants; AT2G28910.1; AT2G28910.1; AT2G28910.
DR EnsemblPlants; AT2G28910.2; AT2G28910.2; AT2G28910.
DR EnsemblPlants; AT2G28910.3; AT2G28910.3; AT2G28910.
DR GeneID; 817440; -.
DR Gramene; AT2G28910.1; AT2G28910.1; AT2G28910.
DR Gramene; AT2G28910.2; AT2G28910.2; AT2G28910.
DR Gramene; AT2G28910.3; AT2G28910.3; AT2G28910.
DR KEGG; ath:AT2G28910; -.
DR Araport; AT2G28910; -.
DR TAIR; locus:2053210; AT2G28910.
DR eggNOG; KOG2985; Eukaryota.
DR HOGENOM; CLU_062939_0_0_1; -.
DR InParanoid; Q84Y18; -.
DR OMA; RTHAIWK; -.
DR OrthoDB; 1584699at2759; -.
DR PRO; PR:Q84Y18; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84Y18; baseline and differential.
DR Genevisible; Q84Y18; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR001878; Znf_CCHC.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..332
FT /note="CAX-interacting protein 4"
FT /id="PRO_0000270156"
FT ZN_FING 81..98
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 33..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3
FT /note="A -> R (in Ref. 1; AAO17572)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="R -> L (in Ref. 5; AAM67086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 37832 MW; 1996B0AE578C918B CRC64;
MPATAGRVRM PANNRVHSSA ALQTHGIWQS AIGYDPYAPT SKEEPKTTQQ KTEDPENSYA
SFQGLLALAR ITGSNNDEAR GSCKKCGRVG HLTFQCRNFL STKEDKEKDP GAIEAAVLSG
LEKIRRGVGK GEVEEVSSEE EEESESSDSD VDSEMERIIA ERFGKKKGGS SVKKTSSVRK
KKKRVSDESD SDSDSGDRKR RRRSMKKRSS HKRRSLSESE DEEEGRSKRR KERRGRKRDE
DDSDESEDED DRRVKRKSRK EKRRRRSRRN HSDDSDSESS EDDRRQKRRN KVAASSDSEA
NVSGDDVSRV GRGSSKRSEK KSRKRHHRKE RE
