ID W5NVJ8_SHEEP Unreviewed; 1601 AA.
AC W5NVJ8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=MAST2 {ECO:0000313|Ensembl:ENSOARP00000002194.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000002194.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000002194.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000002194.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000002194.1}
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; AMGL01001240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; W5NVJ8; -.
DR STRING; 9940.ENSOARP00000002194; -.
DR PaxDb; 9940-ENSOARP00000002194; -.
DR Ensembl; ENSOART00000002245.1; ENSOARP00000002194.1; ENSOARG00000002081.1.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_000288_9_2_1; -.
DR OMA; PHNIPPG; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000002081; Expressed in tricuspid valve and 52 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF136; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 317..590
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 591..659
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 909..997
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 174783 MW; F48B0A6665B6ED07 CRC64;
TGNSPLDSPR NFSPNAPAHF SFVPARRTDG RRWSLASLPS SGYGTNTPSS TVSSSCSSQE
KLHQLPFQPT ADELHFLTKH FSTESVPDEE GRQSPALRPR PAASVSPGRS PVSFDSEIIM
MNHVYKERFP KATAQMEERL AEFISSNTPD NVLPLADGTL SFIHHQVIEM ARDCLDKSRS
GLITSHYFYE LQENLEKLLQ DAHERSESSE VAFVMQLVKK LMIVIARPAR LLECLEFDPE
EFYHLLEAAE GHAKEGQGIK CDIPRYIVSQ LGLTRDPLEE MAQLSSYDSP DTPETDDSVE
GRGASLTSKK TPSEEDFETI KLISNGAYGA VFLVRHKSTR QRFAMKKINK QNLILRNQIQ
QAFVERDILT FAENPFVVSM FCSFETKRHL CMVMEYVEGG DCATLLKNIG ALPVDMVRLY
FAETVLALEY LHNYGIVHRD LKPDNLLITS MGHIKLTDFG LSKIGLMSLT TNLYEGHIEK
DAREFLDKQV CGTPEYIAPE VILRQGYGKP VDWWAMGIIL YEFLVGCVPF FGDTPEELFG
QVISDEIVWP EGDDALPPDA QDLTSKLLHQ NPLERLGTGS AYEVKQHPFF TGLDWTGLLR
QKAEFIPQLE SEDDTSYFDT RSERYHHVDS EDEEEVSEDG CLEIRQFSSC SPRFNKVYSS
MERLSLLEER RTPPPTKRSL SEEKEDRTDG LAGLRGRERS WVIGSPEILR KRLSVSESSH
TESDSSPPLT VRRHCSGLLD VPRFPEGTEE AVGAPRRQQQ EGAWLLTPSG EGASGPAVER
PAERRLKLDE EPAGQSSAPS PAMETRGGRG TPQLAEGATA KAISDLAVRR ARQRLLSGDS
IEKRTARPIN KVIKSASATA LSLLIPAEHH SCSPLASPMS PHSQSSNPSS RDSSPSRDFL
PALSSSRPPI VIHRAGKKYG FTLRAIRVYM GDSDVYTVHH MVWHVEDGGP ASEAGLRQGD
LITHVNGEPV HGLVHTEVVE LILKSGNKVS ISTTPLENTS IKVGPARKGS YKAKMARRSK
RSRGKDGQES RKRSSLFRKI TKQASLLHTS RSLSSLNRSL SSGESGPGSP THSHSLSPRS
PTQGYRVTPE AVHSVGGNSS QSSSPSSSVP SSPAGSGHTR PSSLHGLAPK LQRQYRSPRR
KSAGSIPLSP LAHTPSPPPA ASPQRSPSPL SGHGAQAFPT KLHLSPPLGR QLSRPKSAEP
PRSPLLKRVQ SAEKLAAALA ASEKKLATSR KQSLDLPHPE LKKELPPREV SPLEVVGPRS
VLSGKGALPG KGVLQAAPSR ALGTLRQDRA ERRESLQKQE AIREVDSSED DTDEGPENSQ
GVQEPSLVPH RERGQDPPLR GAGEGEEEDA FLPRDPRGQG PAVPGLLTGV TLGSPRMEGP
GISQKKLGIL QAFEEGSSSS SSAPNLGKAG PTDPIPAECC WKAQHLHTQA LTALCPSSSG
LIPASCSTAS TPGELGPWSW KFLFKGPDRA SPAGKAAMED RPANSQDLET TTPGHPTNLS
PRQEGKSWPP SAPGLAHPPC EVPSQSWLWE SECAQREKEE PALVITKVPD ASGDRRQDVP
CKSCPFTPEP GPSLLQKGQD PGGPQKHQDL ALASDELLKQ T
//
