ID A0A2Y9IVR1_ENHLU Unreviewed; 1648 AA.
AC A0A2Y9IVR1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=LOC111143196 {ECO:0000313|RefSeq:XP_022352446.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022352446.1};
RN [1] {ECO:0000313|RefSeq:XP_022352446.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022352446.1};
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};
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 RefSeq; XP_022352446.1; XM_022496738.1.
DR Proteomes; UP000248482; Unplaced.
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, ECO:0000313|RefSeq:XP_022352446.1};
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:UP000248482};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 516..789
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 790..858
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1144..1232
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1648 AA; 180837 MW; 7F4A25A2F1B690A5 CRC64;
MKRSRCRDRP QPAPPPAGRR EDGAQRAVEL PQPQPLPPRR RAPPGRQLLE ERTGLSGPEV
REQDVIAGLS PLLFRKLSNP DIFSSTGKAK LQRQLSQDDC KLRRGSLASS LSGKQLLPLS
SSVHSSVGQV TWQSSGEASN LVRMRNQSLG QSAPSLTAGL KELSLPRRGS FCRTSNRKSL
IVTSNTSPTL PRPHSPLHGH TGNSPLDSPR NFSPNAPAHF SFVPARRTDG RRWSLASLPS
SGYGTNTPSS TVSSSCSSQE KLHQLPFQPT ADELHFLTKH FSTESVPDEE GRQSPAMRPR
SRSLSPGRSP VSFDSEIIMM NHVYKERFPK ATAQMEERLA EFISSNTPDS VLPLADGTLS
FIQHQVIEMA RDCLDKSRNR LITSHYFYEL QENLEKLLQD AHERSESSEV AFVMQLVKKL
MIVIARPARL LECLEFDPEE FYHLLEAAEG HAKEGQGIKC DIPRYIVSQL GLTRDPLEEM
AQLSSYDSPD TPETDDSVEG RGASLTSKKT PSEEDFETIK LISNGAYGAV FLVRHKSTRQ
RFAMKKVNKQ NLILRNQIQQ AFVERDILTF AENPFVVSMF CSFETKRHLC MVMEYVEGGD
CATLLKNIGA LPVDMVRLYF AETVLALEYL HNYGIVHRDL KPDNLLITSM GHIKLTDFGL
SKIGLMSLTT NLYEGHIEKD AREFLDKQVC GTPEYIAPEV ILRQGYGKPV DWWAMGIILY
EFLVGCVPFF GDTPEELFGQ VISDEIVWPE GDDALPPDAQ DLTSKLLHQN PLERLGTGSA
AEVKQHSFFT GLDWTGLLRQ KAEFIPQLES EDDTSYFDTR SERYHHVDSE DEEEVSEDGC
LEIRQFSSCS PRFSKVYSSM ERLSLLEERR APPPTKRSLS EEKDDRSDGL AGLKGRDRGW
VIGSPEIFRK RLSVSESSHT ESDSSPPLTV RRRCSGLLDA PRFPEGPEEA SPTPRRQQQE
GTWLLTPPSG EGVSGPVPER PVERRLKLDE EPFGQSCGSS PGVAQQAAQG PGLEAAAGRQ
GGEAPQHCRS HCSLGPTAVE TAGGRGTPQL TEGATAKAIS DLAVRRARHR LLSGDSVEKR
TTRPINKVIK SASATTLSLL IPAEHTSSPL ASPMSPHSQS SNPSSRDSSP SRDFLPALSS
SRPPIIIHRA GKKYGFTLRA IRVYMGDSDV YTVHHMVWHV EDGGPASEAG LRQGDLITHV
NGEPVHGLVH TEVVELILKS GNKVSISTTP LENTSIKVGP ARKGSYKAKM ARRSKRSRGK
DGQESRKKSS LFRKITKQAS LLHTSRSLSS LNRSLSSGES GPGSPTHSHS LSPRSPTQGY
RVTPDAVHSG TLRQDRAERR ESLQKQEAIR EVDSSEDDTE EGPENSQGVR EPNLAPTPEV
GRAAPLTGAG EGEEEDAFLS RDPKSQGLVV SGLLTEVTLK PPRMEGPSVP QRELGIPQVF
EEASSSSGAP SLGEAGPTDP IPPEGCWKAQ HFHTQALTAL CPSSSGPVPT SRSAASSTSG
EPGPWSWKFL IEGPDRASPS RKATMEGGMA SSQDLETVTP AHPENLSPRQ EGKSWPPGAP
GLVHPPCEFP HQSRLWEPEC AEREKEEPAL GITKVPDASG DRRQDVPCRS CPLTQEPGPS
LLQRGRDPGG PQKHQDLALV PDELLKQT
//
