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Database: UniProt
Entry: H0VDG7_CAVPO
LinkDB: H0VDG7_CAVPO
Original site: H0VDG7_CAVPO 
ID   H0VDG7_CAVPO            Unreviewed;       716 AA.
AC   H0VDG7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Inhibitor of nuclear factor kappa B kinase subunit epsilon {ECO:0000313|Ensembl:ENSCPOP00000008017.3};
GN   Name=IKBKE {ECO:0000313|Ensembl:ENSCPOP00000008017.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000008017.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000008017.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000008017.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAKN02017887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013013484.1; XM_013158030.1.
DR   RefSeq; XP_013013486.1; XM_013158032.1.
DR   AlphaFoldDB; H0VDG7; -.
DR   STRING; 10141.ENSCPOP00000008017; -.
DR   Ensembl; ENSCPOT00000009004.3; ENSCPOP00000008017.3; ENSCPOG00000008923.4.
DR   GeneID; 100716187; -.
DR   KEGG; cpoc:100716187; -.
DR   CTD; 9641; -.
DR   VEuPathDB; HostDB:ENSCPOG00000008923; -.
DR   eggNOG; KOG4250; Eukaryota.
DR   GeneTree; ENSGT00950000182937; -.
DR   HOGENOM; CLU_000288_101_1_1; -.
DR   InParanoid; H0VDG7; -.
DR   OMA; AEQAKCW; -.
DR   OrthoDB; 2957757at2759; -.
DR   TreeFam; TF324269; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000008923; Expressed in zone of skin and 10 other cell types or tissues.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008384; F:IkappaB kinase activity; IEA:Ensembl.
DR   GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0043254; P:regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0035456; P:response to interferon-beta; IEA:Ensembl.
DR   GO; GO:0034340; P:response to type I interferon; IEA:Ensembl.
DR   Gene3D; 1.20.1270.420; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR041309; TBK1_CCD1.
DR   InterPro; IPR041087; TBK1_ULD.
DR   PANTHER; PTHR22969; IKB KINASE; 1.
DR   PANTHER; PTHR22969:SF10; INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT EPSILON; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18394; TBK1_CCD1; 1.
DR   Pfam; PF18396; TBK1_ULD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..315
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   716 AA;  80615 MW;  EBA3C0676A0FF866 CRC64;
     MQSTANYLWY TDDLLGQGAT ASVYKARNKK SGELVAVKVF NTVSYLRPRE VQVREFEVLR
     KLNHQNIVKL FAVEETGAGR QKVLVMEYCS SGSLLSVLES PENAFGLPEE EFLVVLRCVV
     SGMNHLRENG IVHRDIKPGN IMRLVGEEGQ SIYKLTDFGA ARELDDEEKF ISVYGTEEYL
     HPDIYERAVL HKPQQKAFGV SVDLWSIGVT LYHAATGSLP FVPFGGPRRN KEIMYRITTE
     KPAGAIAGAQ RRENGPLEWS YSLPVTCQLS MGLQSQLVPI LANILEVEEA KCWGFDQFFA
     ETSNILQRVV VHVFCLSQSV LHHIYIHAHN TIAIFLEAVY EQTNVAPQHQ EYLFEGHLCV
     FKPSLSAQHI SHTTASSPLT LFSMASDTPR GLTFRDPAVD IPKFVPKVDL QADYSTAKGV
     LGAGHQALRL ARALLNGQEL MLRGLHWVVQ VLQATCRQTL EVTRTSLLFL GSSLATERSS
     SAARMPEMPE IQKLKRATEL RSKLQTLAAV LSRCSQDMAE TQVSLDHLSS ELAKNRDQVH
     EDRSTQQIQS CLDKMYLIYK QFKKSRMRPG LGYNEEQIHK LDKVNFSHLA KRLLQVFQEE
     CVQKYQASLV THGKWMREVQ KTRNQLRLAS WSVSTCNTEA QGAQENLNKI LDQLLQDRSG
     AEASPPTMAP HPSAAPKDLV VHMQELYEEM KLLAFDLQDN NRVIERLSRV SSPPDA
//
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