KIN17_ARATH
ID KIN17_ARATH Reviewed; 411 AA.
AC Q9ZVU5;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=KIN17-like protein {ECO:0000305};
GN Name=KIN17 {ECO:0000303|PubMed:24335506};
GN OrderedLocusNames=At1g55460 {ECO:0000312|Araport:AT1G55460};
GN ORFNames=T5A14.13 {ECO:0000312|EMBL:AAD10649.1};
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=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 [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=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 [4]
RP FUNCTION, INTERACTION WITH SPL7, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24335506; DOI=10.1104/pp.113.228239;
RA Garcia-Molina A., Xing S., Huijser P.;
RT "A conserved KIN17 curved DNA-binding domain protein assembles with
RT SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to adapt Arabidopsis growth and
RT development to limiting copper availability.";
RL Plant Physiol. 164:828-840(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24713636; DOI=10.4161/psb.28634;
RA Garcia-Molina A., Xing S., Huijser P.;
RT "The Arabidopsis KIN17 and its homolog KLP mediate different aspects of
RT plant growth and development.";
RL Plant Signal. Behav. 9:E28634-E28634(2014).
CC -!- FUNCTION: Promotes the copper deficiency response by direct interaction
CC with SPL7. Acts with SPL7 in a common pathway to promote copper-
CC responsive genes and alleviate oxidative stress during copper-limiting
CC periods. May promote SPL7 function when copper is limiting
CC (PubMed:24335506). Participates in the control of general plant growth
CC and development, and in the response to counteract the negative effects
CC of UV radiation (PubMed:24713636). {ECO:0000269|PubMed:24335506,
CC ECO:0000269|PubMed:24713636}.
CC -!- SUBUNIT: Interacts with SPL7. {ECO:0000269|PubMed:24335506}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24335506}.
CC Note=Nuclear localization with a speckled distribution pattern.
CC {ECO:0000269|PubMed:24335506}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, lateral roots,
CC cotyledons, rosette leaves, cauline leaves, stems, sepals, style of
CC pistils, mature pollen grains and siliques.
CC {ECO:0000269|PubMed:24335506}.
CC -!- MISCELLANEOUS: Plants silencing KIN17 show aberrant growth and reduced
CC fertility. {ECO:0000269|PubMed:24713636}.
CC -!- SIMILARITY: Belongs to the KIN17 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005223; AAD10649.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33248.1; -; Genomic_DNA.
DR EMBL; AF360132; AAK25842.1; -; mRNA.
DR EMBL; AY051011; AAK93688.1; -; mRNA.
DR PIR; H96596; H96596.
DR RefSeq; NP_564690.1; NM_104422.2.
DR AlphaFoldDB; Q9ZVU5; -.
DR SMR; Q9ZVU5; -.
DR IntAct; Q9ZVU5; 1.
DR STRING; 3702.AT1G55460.1; -.
DR iPTMnet; Q9ZVU5; -.
DR PaxDb; Q9ZVU5; -.
DR PRIDE; Q9ZVU5; -.
DR ProteomicsDB; 238214; -.
DR EnsemblPlants; AT1G55460.1; AT1G55460.1; AT1G55460.
DR GeneID; 841993; -.
DR Gramene; AT1G55460.1; AT1G55460.1; AT1G55460.
DR KEGG; ath:AT1G55460; -.
DR Araport; AT1G55460; -.
DR TAIR; locus:2193859; AT1G55460.
DR eggNOG; KOG2837; Eukaryota.
DR HOGENOM; CLU_030065_1_0_1; -.
DR InParanoid; Q9ZVU5; -.
DR OMA; DKGHVHM; -.
DR OrthoDB; 1420569at2759; -.
DR PhylomeDB; Q9ZVU5; -.
DR PRO; PR:Q9ZVU5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVU5; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:UniProtKB.
DR CDD; cd13155; KOW_KIN17; 1.
DR Gene3D; 1.10.10.2030; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR019447; DNA/RNA-bd_Kin17_WH-like_dom.
DR InterPro; IPR037321; KIN17-like.
DR InterPro; IPR038254; KIN17_WH-like_sf.
DR InterPro; IPR041330; KN17_SH3.
DR InterPro; IPR041995; KOW_KIN17.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR12805; PTHR12805; 1.
DR Pfam; PF10357; Kin17_mid; 1.
DR Pfam; PF18131; KN17_SH3; 1.
DR SMART; SM01253; Kin17_mid; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Stress response;
KW Zinc; Zinc-finger.
FT CHAIN 1..411
FT /note="KIN17-like protein"
FT /id="PRO_0000438804"
FT ZN_FING 28..50
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT REGION 51..160
FT /note="Winged helix-turn-helix (wHTH)"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..352
FT /note="C-terminal subdomain A"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT REGION 358..409
FT /note="C-terminal subdomain B"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT COILED 147..183
FT /evidence="ECO:0000255"
FT COILED 265..294
FT /evidence="ECO:0000255"
FT MOTIF 259..262
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000305|PubMed:24713636"
FT COMPBIAS 241..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 47288 MW; 9DA6F8648002065D CRC64;
MGKNDFLTPK AIANRIKAKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH QRQMQVFGQN
PTRVVDGYSE EFEQTFLDLM RRSHRFSRIA ATVVYNEYIN DRHHVHMNST EWATLTEFIK
HLGKTGKCKV EETPKGWFIT YIDRDSETLF KERLKNKRVK SDLAEEEKQE REIQRQIERA
AEKLNGGGGE GETSGNDEVV DDGDDERKKD EDLRLKSGVK VGFALGGGVK QVATGKERGE
SSKLLFGDEE NDKVERGEKR KRSGDSGRSE KERRSALDEL MKEEEKKKER MNRKDYWLFE
GIIVKVMSKA LAEKGYYKQK GVVKKVIDNY VGEIKMLDSK HVLRVDQKEL ETVLPQIGGM
VKIVNGAYRG SNARLLGVDT EKFCAKVQIE KGVYDGRVIK SIEYEDICKL A
