TBKB1_RAT
ID TBKB1_RAT Reviewed; 613 AA.
AC Q6DG50; Q8K1Q5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=TANK-binding kinase 1-binding protein 1;
DE Short=TBK1-binding protein 1;
DE AltName: Full=Protein ProSAPiP2;
GN Name=Tbkbp1 {ECO:0000312|RGD:631328};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:CAC82181.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boeckers T.M.;
RT "Cloning of ProSAPiP2.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH76503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH76503.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE
CC playing a role in antiviral innate immunity. Essential for the
CC efficient induction of IRF-dependent transcription following infection
CC with Sendai virus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). May form a heterodimer with NAP1.
CC Interacts with TKB1 and IKBKE (By similarity). Weakly interacts with
CC DDX3X (By similarity). {ECO:0000250|UniProtKB:A2A9T0,
CC ECO:0000250|UniProtKB:A7MCY6}.
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DR EMBL; AJ278800; CAC82181.1; -; mRNA.
DR EMBL; BC076503; AAH76503.1; -; mRNA.
DR RefSeq; NP_742018.2; NM_172021.2.
DR AlphaFoldDB; Q6DG50; -.
DR SMR; Q6DG50; -.
DR STRING; 10116.ENSRNOP00000012461; -.
DR iPTMnet; Q6DG50; -.
DR PhosphoSitePlus; Q6DG50; -.
DR PaxDb; Q6DG50; -.
DR PRIDE; Q6DG50; -.
DR Ensembl; ENSRNOT00000012462; ENSRNOP00000012461; ENSRNOG00000009370.
DR GeneID; 266764; -.
DR KEGG; rno:266764; -.
DR UCSC; RGD:631328; rat.
DR CTD; 9755; -.
DR RGD; 631328; Tbkbp1.
DR eggNOG; ENOG502QVP4; Eukaryota.
DR GeneTree; ENSGT00940000153704; -.
DR HOGENOM; CLU_029090_0_0_1; -.
DR InParanoid; Q6DG50; -.
DR OMA; QRHSPIQ; -.
DR OrthoDB; 621943at2759; -.
DR PhylomeDB; Q6DG50; -.
DR TreeFam; TF331289; -.
DR PRO; PR:Q6DG50; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000009370; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q6DG50; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR024581; TBD.
DR Pfam; PF12845; TBD; 1.
DR PROSITE; PS51905; ZF_UBZ1; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Immunity; Innate immunity; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..613
FT /note="TANK-binding kinase 1-binding protein 1"
FT /id="PRO_0000324656"
FT ZN_FING 581..607
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 1..280
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 281..330
FT /note="Interaction with TBK1 and IKBKE"
FT /evidence="ECO:0000250"
FT REGION 328..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..162
FT /evidence="ECO:0000255"
FT COILED 218..277
FT /evidence="ECO:0000255"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A7MCY6"
FT CONFLICT 26
FT /note="G -> S (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..223
FT /note="Missing (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="P -> R (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> F (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="P -> L (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="R -> G (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="P -> PHP (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> V (in Ref. 1; CAC82181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67155 MW; 7990F0E5949D1DBA CRC64;
MESMFEDDIS ILTQEALGPS EVWLDGPGDP SLGGDMCSAS HFALITAYGD IKERLGGLER
ENATLRRRLK VYEIKYPLIT DFGEEHGFPL YEIKDGSLLE VEKVSLQQRL NQFQHELQKN
KEQEEQLGEM IQAYEKLCVE KSDLETELGE MRALVETHLR QICGLEKQLQ QQQGLRDAAF
SSLSPPAVPA TACPDLDLHY LALRGGPALG HAGWPGPTSV SVSELERRRL EEALEAAQGE
ARGAQLREEQ LQAECERLQG ELKQLQETRA QDLASNQSEC GMAWVKRVGD DQVNLALAYT
ELTEELGRLR ELSSLQGRIL RTLLQEQARN AGQRHSPLSQ RHSPAPACPS PSPPARPPPC
APCQSPAAQR RSPVPPCPSP QQRRSPASPS CPSPVPQRRS PVPPSCQSPS PQRRSPVPPS
CPAPQPRPPP PPGERTLAER AYAKPPSHHA KAGFQGRRSY SELAEGAAYA AASPAWLQAE
AATLPKPRAY GGELYGPGRP LSPRRAFEGI RLRFEKQPSE EEEWAMPASP PSPEASTIRC
ASFCAGFPIP ESPAATAYAH AEHAQSWPSI NLLMETVGSD IRSCPLCQLG FPVGYPDDAL
IKHIDSHLEN SKI
