TIK_ARATH
ID TIK_ARATH Reviewed; 255 AA.
AC Q0WSX8; Q9FLA6;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=TIR domain-containing protein {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=AtTIK {ECO:0000303|PubMed:25217773};
DE AltName: Full=TIR-KASH protein {ECO:0000303|PubMed:25217773};
GN Name=TIK {ECO:0000303|PubMed:25217773};
GN OrderedLocusNames=At5g44920 {ECO:0000312|Araport:AT5G44920};
GN ORFNames=K21C13.10 {ECO:0000312|EMBL:BAB10874.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH SUN1; SUN2; SUN3;
RP SUN4 AND SUN5, AND DISRUPTION PHENOTYPE.
RX PubMed=25217773; DOI=10.1093/jxb/eru368;
RA Graumann K., Vanrobays E., Tutois S., Probst A.V., Evans D.E., Tatout C.;
RT "Characterization of two distinct subfamilies of SUN-domain proteins in
RT Arabidopsis and their interactions with the novel KASH-domain protein
RT AtTIK.";
RL J. Exp. Bot. 65:6499-6512(2014).
RN [5]
RP REVIEW.
RX PubMed=25740919; DOI=10.1093/jxb/erv082;
RA Zhou X., Graumann K., Meier I.;
RT "The plant nuclear envelope as a multifunctional platform LINCed by SUN and
RT KASH.";
RL J. Exp. Bot. 66:1649-1659(2015).
CC -!- FUNCTION: Could play a role in nuclear morphology, specifically nuclear
CC size. {ECO:0000269|PubMed:25217773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: Forms homomers. Interacts with SUN1, SUN2, SUN3, SUN4 and
CC SUN5. {ECO:0000269|PubMed:25217773}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:25217773};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to the SUN proteins. {ECO:0000305|PubMed:25217773}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- DISRUPTION PHENOTYPE: Shorter roots. {ECO:0000269|PubMed:25217773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10874.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010693; BAB10874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95174.1; -; Genomic_DNA.
DR EMBL; AK227788; BAE99770.1; -; mRNA.
DR RefSeq; NP_851131.1; NM_180800.2.
DR AlphaFoldDB; Q0WSX8; -.
DR SMR; Q0WSX8; -.
DR STRING; 3702.AT5G44920.1; -.
DR iPTMnet; Q0WSX8; -.
DR SwissPalm; Q0WSX8; -.
DR PaxDb; Q0WSX8; -.
DR PRIDE; Q0WSX8; -.
DR EnsemblPlants; AT5G44920.1; AT5G44920.1; AT5G44920.
DR GeneID; 834522; -.
DR Gramene; AT5G44920.1; AT5G44920.1; AT5G44920.
DR KEGG; ath:AT5G44920; -.
DR Araport; AT5G44920; -.
DR TAIR; locus:2155382; AT5G44920.
DR InParanoid; Q0WSX8; -.
DR OMA; NSWDGWY; -.
DR PhylomeDB; Q0WSX8; -.
DR PRO; PR:Q0WSX8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WSX8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; NAD; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..255
FT /note="TIR domain-containing protein"
FT /id="PRO_0000441685"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..185
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 201..255
FT /note="KASH"
FT /evidence="ECO:0000305|PubMed:25217773"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 255 AA; 29699 MW; 10AFF7F0DC9FAE76 CRC64;
MDEQVQEPLS DQVFINFRGD ELREIFVNHL ELQLRNAGIN VFIDTKEQKG RRLQYLFTRI
KKSKIALAIF SKRYCESKWC LDELVTMNEQ MKEKKLVVIP IFYNVRSDDV KRAANPDGEG
NLDGEFSLPF KQLKQNHAGE PERVEGWERA LRSVTKRIGF SRSNSKYKHD TDFVLDIVKE
VKKQLNIPTD NSWSAIGVAF LAITINLIFS FFIAPKYLPD QKFFQTPEWF IGTLAVVLAS
WFWYKNNQNK APPPS
