ID A0A3Q1MEB9_BOVIN Unreviewed; 2580 AA.
AC A0A3Q1MEB9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=WNK1 {ECO:0000313|Ensembl:ENSBTAP00000072507.1,
GN ECO:0000313|VGNC:VGNC:36949};
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:ENSBTAP00000072507.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000072507.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072507.1,
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:ENSBTAP00000072507.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072507.1};
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 Ensembl; ENSBTAT00000080260.1; ENSBTAP00000072507.1; ENSBTAG00000005221.6.
DR VEuPathDB; HostDB:ENSBTAG00000005221; -.
DR VGNC; VGNC:36949; WNK1.
DR GeneTree; ENSGT00940000155474; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000005221; Expressed in prefrontal cortex and 107 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MEB9; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14030; STKc_WNK1; 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:SF46; SERINE_THREONINE-PROTEIN KINASE WNK1; 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 226..484
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2033..2230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2527..2550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2048..2071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2150..2164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2191..2223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2528..2550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2580 AA; 271127 MW; 3119513E8FD4FBD3 CRC64;
MSGGAADQQS SAQGSLFLSP PAPAPKNGSS SDSSVGEKLG AAAADAAAGR TEEYRRRRHT
MDKDSRGAAA TTTTEHRFFR RSVICDSNAT ALELPGLPLP LPQPGAAAVV PQRSPPEPPR
EETLIPAAAA QVAQQPPAAA AAAAAAAPEE PVAASPATSS APSSAGRDRQ AVQPGPAGSR
EEPPTSRSGS GGGSAKEPQE ERSQQQDDIE ELETKAVGMS NDGRFLKFDI EIGRGSFKTV
YKGLDTETTV EVAWCELQDR KLTKSERQRF KEEAEMLKGL QHPNIVRFYD SWESTVKGKK
CIVLVTELMT SGTLKTYLKR FKVMKIKVLR SWCRQILKGL QFLHTRTPPI IHRDLKCDNI
FITGPTGSVK IGDLGLATLK RASFAKSVIG TPEFMAPEMY EEKYDESVDV YAFGMCMLEM
ATSEYPYSEC QNAAQIYRRV TSGVKPASFD KVAIPEVKEI IEGCIRQNKD ERYSIKDLLN
HAFFQEETGV RVELAEEDDG EKIAIKLWLR IEDIKKLKGK YKDNEAIEFS FDLEKDVPED
VAQEMVDSGY VCEGDHKTMA KAIKDRVSLI KRKREQRQLV REEQEKRKQE ESSFKQQVEQ
QPSTAQAGVQ QPPATSTGGP AASAASASVS TQVEPEEPEA DQHQQLQYQQ PGVSVISDGT
VDSGQGSSVF TESRVSSQQT VSYGSQHEQA PSTGALPGHT ASVVQTQAQP HAVYPPSSLP
QSMAHPRGGT PTYPESQIFF PTIHERPVSF SPPPTCPPKV AIAQRRKSTS FLEAQTHQFQ
PLLRTVGQSL LPPGGSPPNW TPETVVMWGT AASRVAGELC EVQAHPVFEP APVYSDYRAG
LMLPEEAHYF LPPEAVYLAG VHYQAQVAEQ FEGFPYSSPV LSSPMKQTPE QKPVHGGPTS
SSVFEFPSGQ AFLVGHLQNV RLDSGLSPGS PQSSVSAPIS TDATRLKFHP VFVPHSAPAV
LTHNNESRSS CVFEFHVHTP SSSSGEGGGG VLPQRIYRNR QVAVDSNQEE PPLQPAGLHS
RLQPVTEEQQ MPQAPELTIS VVEPTGQTWP IGSPEYSSDS SQVTSSDPSE FQSPPPTGGA
AAPFGSDVSL PFIRVPQTVL QESPLFFCFP QGATSPQVLS ASFSSGGSAL HPQAQGQSQG
QPSSSSLTGV PSSQPMQHSQ QQQGVQPTAP SQQAVQYPLP QTSAPSEATI AQPVSQPPPP
QALPHVSAGK QSTQVVSQVA PPEPAPGAQP QPAQPAAVVS SIDSAHSDVA SGLSDGNENV
PSSSGRHEGR TTKRLHRKSI RSRSRHEKPS RPKLRILNVS NKGDRVVECQ LETHNRKMVT
FKFDLDGDNP EEIATIMVNN DFILALERDA FVEQVREIIE KADEMLSEDV SVEPEGDQSL
ESLHGKDDYG FSGTQKLEGE FKQPIPASSL PQQIAGIPAS SLTQVVHSAG RRFIVSPVPE
SRLRESKLFT EISDTVAAST SAGPGMNLSH SASSLSLQQA FSELRHARMA EGPSTAPPHF
GQTGPVFPAV PPTLSSAPGA PAAAAAASVS APAPSHPLSD VTTSVIQTEV TVAPGTGVMP
PSGLPVPPVS ESLAPSSVAP SVTIPAVLSA LPAPQAAQAP TPGSGASSAG TFPSAPASLT
PASAVGSAVA SAAQLPPVPS QPAVGSSTGV ATLTAVPAAA LGPSLTALPS LALSSSTSAP
ALAETVLVSA HALDKTAHSS TTGLALSLPA TSSSPAPGAG VSSAVSQPTA AAHPLVLPSV
VTSTPVLSQA GPMSAPLLPQ VPGIPPLVQP VVSVPAVQQT LVHSQPQPAP LPNQPHTHCP
EIDADTQPKA PGIDDIKTLE EKLRSLFSEH SSSGAQHAPV SLETSLTVET AVTAGLPTTA
VAPSKPLTST ASTCLPPTSL PLGAAGLSVI PMVTPGQVST PVSSAPGVKL ETAPAKPPLT
KPPVLPMGTE LPAGTPPSEQ LPPFPGPSLT QPPQPLGDLD AQLRRTLSPE SGMLTSAVGP
VSVVAPTAVV ETEAQLPKDV LSVSQVTEAP VLAPTSTAGV LKMGRFQVSV AMDDPQKEGK
SKSEDAKSVH FASSTSESSV LSSSSPESTV VKAEPNGLAV RGASADMPDS AHQPPASEAG
QPSKVGRFQV TTTASRVGRF SVSRTEDKMA EVKGEEPVVS PFMDSEHDIP PTVTPKKEKP
ELSEPSHLNG PSSDLEAAFL SRDVDAGSGS PHSPPQLSSK SLPAQSLSQS LSNSFNSSYM
SSDNESDIED EDLKLELRRL REKHLKEIQD LQSRQKHEIE SLYTKLGKVP PAVIIPPAAP
LAGRRRRPTK SKGSKSSRSS SLGNKSPGPG TLSGQSAASV LHPQQTLPAP GSVPETGPNQ
LLQPVKPSPS SDNLYSAFTS DGAISVPSLS APGQGCAKFN CASEQVTFKA GGRRTRFLRK
MVKKVCPCNQ LCRTSSTNAV GGAVSSQAAP APPPAVTSSR KGMFTDDLHK LVDNWARDAM
SLSGRRGSKG HVSYEGPGMA RKFSAPGQLC VSMTSNLGGS APGSAASATS LGHFPKSMCP
PQQYGFPTPP FGTQWSGTGG PAPQPLSQFQ PVGTASLQNF NISNLQKSIS NPPGSNLRTT
//