ID A0A1S3A839_ERIEU Unreviewed; 1745 AA.
AC A0A1S3A839;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=WNK3 {ECO:0000313|RefSeq:XP_007530898.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007530898.1};
RN [1] {ECO:0000313|RefSeq:XP_007530898.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007530898.1; XM_007530836.2.
DR CTD; 65267; -.
DR OrthoDB; 5478852at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; cd14031; STKc_WNK3; 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:SF47; SERINE_THREONINE-PROTEIN KINASE WNK3; 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, ECO:0000313|RefSeq:XP_007530898.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 147..405
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 192230 MW; DF203CAFDE4B6276 CRC64;
MATDSGEPAS TEDSEKPDGV SLENQIPQVA ATLTVEPKVK EKTSTISASG EKIERKRFFR
KSVEMMEDDK VGESSFKDER IKTATNITKI EKVPTNVLRG GQEVKYEQCS KATSEPSKDC
VKEKNEKEME EEAEMKAVAT SPSGRFLKFD IELGRGAFKT VYKGLDTETW VEVAWCELQD
RKLTKAEQQR FKEEAEMLKG LQHPNIVRFY DSWESILKGK KCIVLVTELM TSGTLKTYLK
RFKVMKPKVL RSWCRQILKG LQFLHTRTPP IIHRDLKCDN IFITGPTGSV KIGDLGLATL
MRTSFAKSVI GTPEFMAPEM YEEHYDESVD VYAFGMCMLE MATSEYPYSE CQNAAQIYRK
VTSGIKPASF NKVTDPEVKE IIEGCIRQNK SARLSIRDLL NHTFFAEDTG LRVELAEEGD
CSNSSLALRL WVEDPKKLKG KHKDNEAIEF SFNLETDTPE EVACEMVKSG FFHESDSKAV
AKSIRDRVTL IIKTREKKPT GCPEERRNSQ CKPIGNVLPQ HQNITLSSAP PQQTGAECEE
TEVDQYVQQQ LQKKTHHCSS VTGDNLAEVG AGSVLQSDTS NQPNTGYSLD QIMDSQMVSN
IPQTEVNVSG QIYPSQPLVG HYQQISGLQK QQPNLTQPPI LPLVQGQSTV LPVHAVGSPV
VPQSQVSPIT VQKFSQVMPV SKPIGGEQQS TVPKPELGRS LNHDITTVKE NTNVTDNPNG
NGKQDRIKQR RTSCPRPEKG TKFQLTVLQV STSGDNMVEC QLETHNNKMV TFKFDVDGDA
PEDIVDYMVE DNFVLESEKE KFVEELKTIV GQAQEILHIH STAERPIGID SISVESSSNQ
TGSSEQGQIY CASTQTSNES VTQSSPVGRW RFCINQTIRS RESQSPPPHQ QSMTLVPGLH
PLSSARKTSN KEIAQDPLLN LENAPCQQTV FTSKSEQKDV VDGKISDYAG KETKQPALLY
QMEDDRQIMS SAACSSSYTA TSIHVVPVEC EGLSNQAGIF LPMYPCHQTA SQADIPMASP
GESTQIASNS ITTVAFMSDQ KPQSLSVKHT TMDAEFISQE GETTVDNEVS SPKTVTSIKT
PCLESTTLLP STILESDGER PPKVEFTDNR IKTLDEKLRN LLYQEHSVSS IFPESHKDIQ
SIDSPFSSST EETLSFPVPD VLAVSHCGIQ DSPAQSPNFQ QTGSQILSGV AVSQPANVSV
FKRDLNMITS VPSELCLHEM STDASLPGDP EAYHAAVSSH GAIHLQTGVE TEDIRLAVAP
DPIPLTGQST TDNRALSGCK SMSGSFQQGR FQVITVPQQQ SMKATSIGIE HVPEFNEMAS
HSSEEVLGFT ETAKSQLVEM EPAAHSPQIL FSSQMIQALH KTFNEDKRIP KKGDSLPFST
VCGTSASSIT PEKEPEEKSA TRNMQSGSEL FLKEKEKLNI GKQHGSDSKF SATFSVRGKS
VAKTHQENDQ CLPPGKEQGC AQTQSSLFYS PSSPMSSDDE SEIEDEDLKV ELHRLREKHI
QEVVNLQTQQ NKELQELYER LRALKDNKTL SSEIPLPPAS PRRPRSFKSK LRSRPQSLTH
VDNSTAATDP VHVESNAASC QQSPASKKGM FTDDLHKLVD DWTKETVGSS LVKPSLNQLK
QSQHKVETDN WNKVHENSPS TMGYTSPWIS SLTQIRGAVQ TSLPQGLPHP SFPGPLSSYG
IPHVCQYNAV GAPGYPVQWA GISGTPQPSV VIPTQSGGPF QPGMNLQAFP ASPVQNPSTI
PPGPK
//
