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Database: UniProt
Entry: E1BM51_BOVIN
LinkDB: E1BM51_BOVIN
Original site: E1BM51_BOVIN 
ID   E1BM51_BOVIN            Unreviewed;      1246 AA.
AC   E1BM51;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 3.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=WNK4 {ECO:0000313|Ensembl:ENSBTAP00000026519.6,
GN   ECO:0000313|VGNC:VGNC:36952};
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 {ECO:0000313|Ensembl:ENSBTAP00000026519.6, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000026519.6, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000026519.6,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000026519.6}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000026519.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   AlphaFoldDB; E1BM51; -.
DR   SMR; E1BM51; -.
DR   STRING; 9913.ENSBTAP00000026519; -.
DR   PaxDb; 9913-ENSBTAP00000026519; -.
DR   Ensembl; ENSBTAT00000026519.6; ENSBTAP00000026519.6; ENSBTAG00000019907.6.
DR   VEuPathDB; HostDB:ENSBTAG00000019907; -.
DR   VGNC; VGNC:36952; WNK4.
DR   eggNOG; KOG0584; Eukaryota.
DR   GeneTree; ENSGT00940000159871; -.
DR   HOGENOM; CLU_000550_2_1_1; -.
DR   InParanoid; E1BM51; -.
DR   OMA; XYLRRFR; -.
DR   TreeFam; TF315363; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000019907; Expressed in adult mammalian kidney and 101 other cell types or tissues.
DR   ExpressionAtlas; E1BM51; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0050801; P:monoatomic ion homeostasis; IBA:GO_Central.
DR   GO; GO:0010766; P:negative regulation of sodium ion transport; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IBA:GO_Central.
DR   CDD; cd14033; STKc_WNK4; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR   PANTHER; PTHR13902:SF114; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          174..432
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..101
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..557
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..962
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1246 AA;  135343 MW;  AE9DE6960BF11E18 CRC64;
     MLAPPAPETE VPMSQAEADL PLRPPPTLAA AGPPRLGPPS RRVRRFSGKA EPRPRSSRLS
     RRSSVDLGLL SSWSQPASPV PEPPDPPDSA GSGPAMSPPP SSEEPLEGMW TTGAPVKPAD
     SERLEPAGST GGSGSREQPR ITEAAAARER RREQEEKEDT ETQAVATSPD GRYLKFDIEI
     GRGSFKTVYR GLDTDTTVEV AWCELQTRKL SRAERQRFSE EVEMLKGLQH PNIVRFYDSW
     KSVLRGQVCI VLVTELMTSG TLKTYLRRFR EMKPRVLQRW SRQILRGLHF LHSRVPPILH
     RDLKCDNVFI TGPSGSVKIG DLGLATLKRA SFAKSVIGTP EFMAPEMYEE KYDEAVDVYA
     FGMCMLEMAT SEYPYSECQN AAQIYRKVTS GTKPNSFYKV KMPEVKEIIE GCIRTDKNER
     FTIHDLLAHA FFREERGVHV ELAEEDDGEK PDLKLWLRME DARRGGRPRD NQAIEFLFQL
     GRDAAEEVAQ EMVALGLVCE ADYQPVARAV RERVAAIQRK REKLRKAREL EALPPAPRPP
     PAAVPMTPGP SSAFPPEPEE PEADQHQPFL FRHASYSSTT SDCETDGYLS SSGFLDASDP
     ALQPPSGVPS SPAESHLRLP AAFALSIPRS GPGNDFSPGE SYASEAASGL SDVGEGMERM
     RRPPGKNLRR RPRSRLRVTS VSDQNDRVVE CQLQTHNSKM VTFRFDLDGD SPEEIAAAMV
     YNEFILPSER AGFLNRIREI IQRVETLLKR DTGPVEAAED PLSPQEESAP LPALPGSPPD
     PSRELQSSTS LEQRCWAAFS TSTSSPGTPL SPGSSFSPGT PVFPSPILPI TSPPCHLNPS
     SFSPISPQAS SNLSPHPQSC PLPLSPRAPQ FPVPSAQFPQ SSLFPDCFQG TPAPSFPLCP
     SACPLPSTTA APLLSLASAF SLAVMTVAQS LLSPSPGLLS QSPPAPPGPL PSLPPPTPCT
     PCGQEWPSSL TAEVESEASP NLGQPLPGEA RLAPISKEGK PQLVGRFQVT SSKEPAEPLP
     LQLASPTPSG SLKPPTPQLT SESSDTEDSA GARPEAREAL AESDRAAEGL GAGAEEEGDD
     GQEPQVGGSP PPLSHPSPVW MSYSYSSLCL SSEESESSGE DEEFWAELQN LRQKHLSEVE
     ALQTLQKQEI EDLYSRLGKQ PPPGIVAPAA MLSSRQRRLS KGSFPTSRRN SLQRSEPLGP
     GIMRRNSLSG SSTGSQEQRA SKGVTFAGDV GRMVRAGSRE GEPREW
//
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