VRK3_BOVIN
ID VRK3_BOVIN Reviewed; 451 AA.
AC Q2YDN8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Inactive serine/threonine-protein kinase VRK3;
DE AltName: Full=Serine/threonine-protein pseudokinase VRK3;
DE AltName: Full=Vaccinia-related kinase 3;
GN Name=VRK3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inactive kinase that suppresses ERK activity by promoting
CC phosphatase activity of DUSP3 which specifically dephosphorylates and
CC inactivates ERK in the nucleus. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DUSP3. Interacts with RAN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000305}.
CC -!- CAUTION: Inactive as a kinase due to its inability to bind ATP.
CC {ECO:0000305}.
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DR EMBL; BC110135; AAI10136.1; -; mRNA.
DR RefSeq; NP_001039716.1; NM_001046251.2.
DR RefSeq; XP_005219336.1; XM_005219279.3.
DR RefSeq; XP_005219337.1; XM_005219280.3.
DR RefSeq; XP_005219338.1; XM_005219281.3.
DR RefSeq; XP_010813351.1; XM_010815049.2.
DR RefSeq; XP_015313652.1; XM_015458166.1.
DR AlphaFoldDB; Q2YDN8; -.
DR SMR; Q2YDN8; -.
DR STRING; 9913.ENSBTAP00000007054; -.
DR PaxDb; Q2YDN8; -.
DR Ensembl; ENSBTAT00000007054; ENSBTAP00000007054; ENSBTAG00000005367.
DR GeneID; 520302; -.
DR KEGG; bta:520302; -.
DR CTD; 51231; -.
DR VEuPathDB; HostDB:ENSBTAG00000005367; -.
DR VGNC; VGNC:36836; VRK3.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000158111; -.
DR HOGENOM; CLU_019279_4_4_1; -.
DR InParanoid; Q2YDN8; -.
DR OMA; YCMLRWH; -.
DR OrthoDB; 866200at2759; -.
DR TreeFam; TF106473; -.
DR Reactome; R-BTA-202670; ERKs are inactivated.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000005367; Expressed in semen and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR026870; Zinc_ribbon_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13240; zinc_ribbon_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Inactive serine/threonine-protein kinase VRK3"
FT /id="PRO_0000296678"
FT DOMAIN 123..434
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 47..62
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 34..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV63"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV63"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV63"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV63"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IV63"
SQ SEQUENCE 451 AA; 50549 MW; 055A7E9C724EA90D CRC64;
MICPDCGKGI EATFKFCPYC GKPLPAEKHE GSQSFVKPFT SSSQGSRRKT NTSSETSSKK
VKWCSYAASP SLPLPSEGKS SGSEDTLSTS GKPKGHLSRS PTPRSSPQTT RQSPQTLKRS
RMTASLEALP VGTVLTDKSG QHWKLRCLQT RDDQGILYEA ESDSTTGSES SPQKQRFSLK
LDAKDGRLFN EQNFFQRAAK PLQVNKWKKL YSIPQLAIPT CIGFGVHQDK YRFLVFPTLG
RSLQSILDDF PKHVMSVRSV FQMACRLLDA LEFLHENEYV HGNVTAENIF VNPENLCQVT
LAGYGFTFRY SPGGRHVAYT EGSRSPHEGH LEFISMDLHK GCGPSRRSDL QTLGYCLLKW
LYGTLPWTNC LPNTEEIVKL KQKFLDNPEG LVGQCSRWIT PSETLQEYLK VVMALQYEEK
PPYSTLRNEL EALLQDLRAS AYDPLDLQVV P
