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Database: UniProt
Entry: W5QHW4_SHEEP
LinkDB: W5QHW4_SHEEP
Original site: W5QHW4_SHEEP 
ID   W5QHW4_SHEEP            Unreviewed;      1297 AA.
AC   W5QHW4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=TNIK {ECO:0000313|Ensembl:ENSOARP00000022314.1};
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:ENSOARP00000022314.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000022314.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000022314.1,
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:ENSOARP00000022314.1}
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; AMGL01009833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01009840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSOART00000022619.1; ENSOARP00000022314.1; ENSOARG00000020761.1.
DR   Proteomes; UP000002356; Chromosome 1.
DR   Bgee; ENSOARG00000020761; Expressed in gastric lymph node and 55 other cell types or tissues.
DR   ExpressionAtlas; W5QHW4; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          1..234
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          984..1271
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          229..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..281
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..735
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..768
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..787
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1297 AA;  148061 MW;  CA7F6FDFA3A6E119 CRC64;
     MDVTGDEEEE IKQEINMLKK YSHHRNIATY YGAFIKKNPP GMDDQLWLVM EFCGAGSVTD
     LIKNTKGNTL KEEWIAYICR EILRGLSHLH QHKVIHRDIK GQNVLLTENA EVKLVDFGVS
     AQLDRTVGRR NTFIGTPYWM APEVIACDEN PDATYDFKSD LWSLGITAIE MAEGAPPLCD
     MHPMRALFLI PRNPAPRLKS KKWSKKFQSF IESCLVKNHS QRPATEQLMK HPFIRDQPNE
     RQVRIQLKDH IDRTKKKRGE KDETEYEYSG SEEEEEENDS GEPSSILNLP GESTLRRDFL
     RLQLANKERS EALRRQQLEQ QQRENEEHKR QLLAERQKRI EEQKEQRRRL EEQQRREKEL
     RKQQEREQRR HYEEQMRREE ERRRAEHEQE YIRRQLEEEQ RQLEILQQQL LHEQALLLEY
     KRKQLEEQRQ AERLQRQLKQ ERDYLVSLQH QRQEQRPVEK KPLYHYKEGM SPSEKPAWAK
     EVEERSRLNR QSSPAMPHKV ANRISDPNLP PRSESFSISG VQPARTPPML RSVDPQIPHL
     VAVKSQGPAL TASQSVHEQP TKGLSGFQEA LNVSSHRVEM PRQNSDPTSE NPPLPTRIEK
     FDRSSWLRQE EDIPPKVPQR TTSISPALAR KNSPGNGSAL GPRLGSQPIR ASNPDLRRTE
     PVLESSLQRT SSGSSSSSST PSSQPSSQGG SQPGSQAGSS ERTRVRANSK SEGSPVLPHE
     PSKVKPEESR EITRPSRPAD LTALAKELRE LRIEETNRPL KKVTDYSSSS EESESSDEEE
     EDGESETQDG TVAVSDIPRL IPTGAPGSAE QYNVGMVGTH GLETSHADTF GSSISREGTL
     MIREPSGEKK RPGHSDSNGF AGHINLPDLV QQSHSPAGTP TEGLGRVSTH PQEMDAGTEY
     GLGSSTKASF TPFVDPRVYQ TSPTDEDEED EESSAAALFT SELLRQEQAK LNEARKISVV
     NVNPTNIRPH SDTPEIRKYK KRFNSEILCA ALWGVNLLVG TENGLMLLDR SGQGKVYNLI
     NRRRFQQMDV LEGLNVLVTI SGKKNKLRVY YLSWLRNRIL HNDPEVEKKQ GWITVGDLEG
     CIHYKVVKYE RIKFLVIALK NAVEIYAWAP KPYHKFMAFK SFADLQHKPL LVDLTVEEGQ
     RLKVIFGSHT GFHVIDVDSG NSYDIYIPSH IQGNITPHAI VILPKTDGME MLVCYEDEGV
     YVNTYGRITK DVVLQWGEMP TSVAYIHSNQ IMGWGEKAIE IRSVETGHLD GVFMHKRAQR
     LKFLCERNDK VFFASVRSGG SSQVFFMTLN RNSMMNW
//
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