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Database: UniProt
Entry: A0A2K5NRD3_CERAT
LinkDB: A0A2K5NRD3_CERAT
Original site: A0A2K5NRD3_CERAT 
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
//
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