ID A0A3B1K0Z6_ASTMX Unreviewed; 2670 AA.
AC A0A3B1K0Z6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=WNK2 {ECO:0000313|Ensembl:ENSAMXP00000047760.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000047760.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000047760.1}
RP IDENTIFICATION.
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 STRING; 7994.ENSAMXP00000047760; -.
DR Ensembl; ENSAMXT00000037599.1; ENSAMXP00000047760.1; ENSAMXG00000003641.2.
DR GeneTree; ENSGT00940000157161; -.
DR InParanoid; A0A3B1K0Z6; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000003641; Expressed in camera-type eye and 11 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13983; STKc_WNK; 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:SF10; SERINE_THREONINE-PROTEIN KINASE WNK2; 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:UP000018467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 272..530
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 59..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1870..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..1970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2166..2194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2208..2253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2292..2314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2331..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2445..2484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1913..1958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2102..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2208..2223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2447..2469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2670 AA; 283865 MW; EE9788C46DC57D07 CRC64;
MFTAGGGTWE CEIQPALPHV DDPHLLQLHR GELGHGAAAS SSLSSAPPTL AAGAQPAFLK
RPGMEDGPAS ATSVASPASK CPSVPGSRCD LLHASTPEAR DGDGDSSSPS EGSVVRGGSD
PSASNYRRGA GARQQRFIRR SLWFADSDDQ QGCEPTENEC ATVTASVSLR NLVVDRSRRA
ARTSLREGSS TESQGQGGHK DSATESASAD EERGRVDGAA AVVVPASPAA ATELNGDTTD
GTRGNATKCA SEENEEEAEM KAVATSPGGR FLKFDIELGR GSFKTVYKGL DTETWVEVAW
CELQDRKLTK VERQRFKEEA EMLKGLQHPN IVRFYDFWES LLKGKKCIVL VTELMTSGTL
KTYLKRFKVM KPKVLRSWCR QILKGLHFLH TRTPPIIHRD LKCDNIFITG PTGSVKIGDL
GLATLKRASF AKSVIGTPEF MAPEMYEEHY DESVDVYAFG MCMLEMATSE YPYSECQNAA
QIYRKVTSGV KPASFNKVMD PEVKEIIGEC ICQNKEDRYS IKDLLNHAFF AEDTGVRVEL
AEENDGRKAS IALRLWVEDP RKLKGKYKDG GVIEFTFDLE KEVPEGVAQE MVESGLFHES
DAKIVGKSIR DRVALIKWRR ERTVPSEAQS STTQAAPVQL AAGTVPALCE PSGPVDLEES
EADQHSHLGN LSASTTSTTS DSGIGSTVYS DSHSSSQHSV LYQSLQETVS TATQQHHPSG
LFLTSRDRVL EVLGSSQGAG CKAGACAQGS CLTDSLKHHM HIQSVFRPVS PDPMHVLPAL
SDRREEDGES CFFSQRLLLS PLTFEPRRHS DSSMGLLSET EGEHMVVSEA RARRSSLSYA
PLSHACPSLL LLRTRAEKSA GAVLPPLYMC SCQRRSPVPS PTGLLPGTGG HKGSHNESSD
ISDLNKSLQS ITGHKHTPNA SFLRVPPILA ETGPHRPARS HGHEKQMESL GGEPTPKPTA
PRRASMCVGD HSLNHRSGVS GAALQLHTHL LQPSQSYAAA PAAAAALVAP TQPGYPPPGQ
PLQPQSYSSV PSTVQQQATF TQHVPVQQPV PAQSMNIQSY PATGHTGLPS VQANLHQTVG
YVPVPPVQAL APVQALAPVQ ALAPVQALAL PNQAPPTVQQ TLGTTTQIYP LLQQGTAVVN
NQNLTASQSS VLPVPAHVPM QQASAMQNFP DAATLQLSIQ TLQTGASSLQ HGSVAPSLLQ
SRPEAVQHQQ AIAHQGLHPP GGIVSGKTEL AESALHSPSQ LQSVASAGTP AFSSHTALES
QKILQSSSVP SQMFSAQPSL AHCTAAQQQQ PHQTSSKTPS HLAQLTSLNP VSSVGVLLSG
QDSCSSSFSS SVQSSLTPLY LSTGQPAPSL PSLSPVPCSQ MEEAVSAQHP LLLPSTSPLP
TQSPQKPFTA PAFTTAAPTI NAYQHSYPVA QQNSANSITT PSLLTICQTT PPVHQNLPPS
PNPASLSIGA LPTSQVPLPQ GASTSNNQAP AVLPVPKPAQ MCSTQSGVFI STSSVPVHCS
QTAVTTAPIA TAVPACPAQT ATAAQLPQPA LQAALTSQSP SLGTAVPDLG STAAPLDLNQ
EPQVFAASSS MSQQKQSSAR GSGVGQPPTD VFAEESILDK QTTVAGSAYD SVNSDATSGK
EMSDGNEGTH GGRSESRVRK HLRKSSRTRS RQEKTGKPKL SMLNVCNTGD KMVECQLETH
NHKMVTFKFD LDGDAPEEIA TYMVENDFIL LLEKEMFIEQ LKDIVEKAED ILSEDAEGER
GSDPSSRPGH SLISRTSGSE VLTPQLMQSN QLVYQQNVLH TGKRLFIICP VAEVPTYKGE
DKDSEGLPAA QIPDASVGEA VAPQKPSSLS KPYVTSPESS QSVEDHQASH SVAAAVSMVA
DIPCCPITPP VPQDASSEKL HAALHQPASR DVSPVTDTPL NQAQTVVLQQ PFSTPIAPPT
VSTAQSQPQS PAHQTQQAPS SASSTSGLAS SQAQPGTGPG ESDGEGPPRL EFADRTIKTL
DEKLRNLLYQ EYNPSQTTSS ASDPPGSPPM SDSQGSDGAL RKGEMLPQIP ERSDSLGTLS
DSAVAPLNRM LIRNDSTESS SGQSSCKSRF KIVPTPPDVL RCLEHSRTSS AGAAQRDGEA
AETTNAEVSF TPNNGDQAKT HSNRYSAPPD FYQDVHSSSR EIIPSIPHAQ TSLSIDVATQ
HGLNLSSDSC EEDNSFSAAH KPSPHAHALS EHSGTDLMKR AVAFFRRSGR SSSVQSSDSP
SRPPLLNGHA PCVSNHAHST YVSSDNDSEF EDADMKKELQ RLREKHMKEI SELQAHQRGE
IEQLYSRLGR SVPPSVGFLH AAPPTGRRRR ASKHKLKAGK LLNPMVQQLK SNRAETCSSA
STSPAKSSVL NTSAGSSMAT LQSPVSEPLQ PVQTQQPCSL KVSLSSDNIY GSPTHTPPGQ
GWTVYHQTSE RVTYKSSSKP RTRFLSGPVS LSIWSTLKRL CLGKERSSRS SHSAGATPVT
TASNQQSTPP PVVTPVPPPR PMTALAQAQT NNSNNKTGTF TDDLHKLVDD WAKETLAVAP
QPRPSLNQIK QQQRHQDFKP TSIRMSGASN QIKPPVPPSS LPFQLPLTCP LSSSMGPAMP
PTLSTTPSPV LQPASYLLPT APFGGVMPTP GYQTQWPGIP CPAGTMGPGN LLGTAGMVPF
PALANPALQA FPMALNGSDN PVCPGSARTV
//
