ID A0A2K5NRD3_CERAT Unreviewed; 2385 AA.
AC A0A2K5NRD3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSCATP00000039945.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000039945.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000039945.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011909459.1; XM_012054069.1.
DR Ensembl; ENSCATT00000064259.1; ENSCATP00000039945.1; ENSCATG00000042502.1.
DR GeneID; 105582948; -.
DR CTD; 65125; -.
DR GeneTree; ENSGT00940000155474; -.
DR OMA; PEPNGMT; -.
DR OrthoDB; 5478852at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000042502; Expressed in adult mammalian kidney and 12 other cell types or tissues.
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:0042592; P:homeostatic process; IEA:UniProt.
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:UP000233060};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 222..480
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1732..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2024..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2335..2354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
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 101..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1117
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2136..2199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2385 AA; 250765 MW; 128641928365C9CA CRC64;
MSGGAAEKQS GTPGSLFLSP PAPVPKNGSS SDSSVGEKLG AAAADAGTGR TEEYRRRRHT
MDKDSRGAAA ATTTTEHRFF RRSVICDSNA TALELPGLPL SLPQPGIPAV VPQSAPPEPH
REETVAAAAA SQVAQQPAAA AAPGEEAVAG PAPSTVPSST SKDRPVSQPS LAGSKEEPPP
ARSGSGGGGS AKEPQEERSQ QQDDIEELET KAVGMSNDGR FLKFDIEIGR GSFKTVYKGL
DTETTVEVAW CELQDRKLTK SERQRFKEEA EMLKGLQHPN IVRFYDSWES TVKGKKCIVL
VTELMTSGTL KTYLKRFKVM KIKVLRSWCR QILKGLQFLH TRTPPIIHRD LKCDNIFITG
PTGSVKIGDL GLATLKRASF AKSVIGTPEF MAPEMYEEKY DESVDVYAFG MCMLEMATSE
YPYSECQNAA QIYRRVTSGV KPASFDKVAI PEVKEIIEGC IRQNKDERYS IKDLLNHAFF
QEETGVRVEL AEEDDGEKIA IKLWLRIEDI KKLKGKYKDN EAIEFSFDLE RDVPEDVAQE
MVESGYVCEG DHKTMAKAIK DRVSLIKRKR EQRQLVREEQ EKKKQEESSL KQQVEQSNAS
QTGIKQLPSA STGIPTASTT SASVSTQVEP EEPEADQHQQ LQYQQPSISV LSDGTVDSGQ
GSSVFTESRV SSQQTVSYGS QHEQAHSAGT VPGHVPSAVQ AQSQPHGVYP PSSVAQGQSQ
GQPSSSSLTG VSSSQPIQHP QQQQGIQQTA PPQQTVQYSL SQTSTSSEAT TAQPASQPQA
PQVLPQVSAG KQLPVSQPVP TIQGEPQIPV ATQPSAVPVH SGAHFLPVGQ PLPTSLLPQY
PVSQIPISAP HVSTAQTGFS SLPITMAAGI TQPLLTLASS ATTAAIPGVS TVVPSQLPTL
LQPVTQLPSQ VHPQLLQPAV QSMGVPANLG QAAEVPLSSG DVLYQGFPPR LPPQYPGDSN
IAPSSNVASV CIHSTVLSPP MPTEVLATPG YFPTVVQPYV ESNLLVPMGG VGGQVQVSQP
GVSLAQAPTT SSQQAVLEST QGVSQVAPPE PVPVAQPQPT QPATLASSID SAHSDVASGM
SDGNENVPSS SGRHEGRTTK RHYRKSVRSR SRHEKTSRPK LRILNVSNKG DRVVECQLET
HNRKMVTFKF DLDGDNPEEI ATIMVNNDFI LAIERESFVD QVREIIEKAD EMLSEDVSVE
PEGDQGLESL QGKDDYGFSG SQKLEGEFKQ PIPVSSMPQQ IGIPTSSLTQ VVHSAGRRFI
VSPVPESRLR ESKLFTSEIT DTVAASTSQS PGMNLSHSAS SLSLQQAFSE LRHAQMTEGP
NTAPPNFSHT APTFPVVPPF LSSIAGVPTT AAATVPVPAT SSPPNDMSTS VIQSEVTVPT
EEGIAGVATS TGVATAGGLH IPPVSESPVL SSVVSSTTIP AVVSISTTSP SLQVPTSTSE
NIVSSTALYP SVTVSAISAS TGGSTVTPGP KPPAVVSPQA AGSTTVGVAL TSVSATTSLP
STASQLSIQL SSSTSAPTLA ETVVVSAHSL DKTSHSITTG LALSLSAPSS SSSPGTGVSS
SISQPGGLHP LVIPSVIAST PILPQAAGPT STPLLPQVPS IPPLVQPVAN VPAVQQTLIH
SQPQPALLPN QPHTHCPEID SDTQPKAPGI DDIKTLEEKL RSLFSEHSSS GAQHAPVSLE
TSLVVESTVT PGIPTTAVAP SKLLTSTTST CLPPTNLPLG TVALPVTPVV TPGQVSTPVS
TATSGVKPGT APSKPPLTKP PVLPVGTELP AGALPSEQLP PFPGPSLTQS QQPLEDLDAQ
LRRTLSPEII TTVTSAVGPV SVVAPAAVTE AGAQPQKDVS QVTEKGPVLA TSSGAGVFKM
GRFQVSVAAD DTQKEGKSKS EDAKSVHFES STSESSVLSS SSPESTLVKP EPSGITIPGI
SSDVPESAHK TTASEAKSDT GQPTKVGRFQ VTTTANKVGR FSVSKTEDKI TDTKKEGPVA
SPPFMDLEQA VLPAVIPKKE KPELSEPSHL NGPSSDLEAA FLSRDVDDGS GSPHSPHQLS
SKSLPIQNLS QSLSNSFNSS YMSSDNESDI EDEDLKLELR RLRDKHLKEI QDLQSRQKHE
IESLYTKLGK VPPAVIIPPA APLSGRRRRP TKSKGSKSSR SSSLGNKSPQ LSGNLSGQSA
ASVLHPQQTL HPPGNIPESG QNQLLQPLKP SPSSDNLYSA FTSDGAISVP SLSAPGQGTS
STNTVGATVN SQAAQAQPPA MTSSRKGTFT DDLHKLVDNW ARDAMILSGR RGSKGHMNYE
GPGMARKFSA PGQLCISMTS NLGGSAPISA ASATSLGHFT KSMCPPQQYG FPATPFGAQW
SGTGGPAPQP IGQFQPVGTA SLQNFNISNL QKSISNPPGS NLRTT
//