ID A0A383YPE4_BALAS Unreviewed; 1729 AA.
AC A0A383YPE4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=MAST2 {ECO:0000313|RefSeq:XP_007164596.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007164596.1};
RN [1] {ECO:0000313|RefSeq:XP_007164596.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007164596.1};
RG RefSeq;
RL Submitted (JAN-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_007164596.1; XM_007164534.1.
DR CTD; 23139; -.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000261681; 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_007164596.1};
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:UP000261681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 445..718
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 719..787
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1038..1126
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 103..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1729 AA; 189005 MW; 93865A28A7489599 CRC64;
MRNQSLGQSA PSLTAGLKEL SLPRRGSLIS ALCRGSEVNR LILSPTSAPT LSLTKVPFSA
DCPLATSPLA FFLNTQAHSS PGSPSSSRSL QWSCRTSNRK SLIVTSSTSP TLPRPHSPLH
GHTGNSPLDS PRNFSPNAPA HFSFVPARSH GHRADRTDGR RWSLASLPSS GYGTNTPSST
VSSSCSSQEK LHQLPFQPTA DELHFLTKHF STESVPDEEG RQSPALRPRS RSLSPGRSPV
SFDSEIIMMN HVYKERFPKA TAQMEEHLAE FISSNTPDNV LPLADGTLSF IHHQVIEMAR
DCLDKSRSGL ITSHYFYELQ ENLEKLLQDA HERSESSEVA FVMQLVKKLM IVIARPARLL
ECLEFDPEEF YHLLEAAEGH AKEGQGIKCD IPRYIVSQLG LTRDPLEEMA QLSSYDSPDT
PETDDSVEGR GASLTSKKTP SEEDFETIKL ISNGAYGAVF LVRHKSTRQR FAVKKINKQN
LILRNQIQQA FVERDILTFA ENPFVVSMFC SFETKRHLCM VMEYVEGGDC ATLLKNIGAL
PVDMVRLYFA ETVLALEYLH NYGIVHRDLK PDNLLITSMG HIKLTDFGLS KIGLMSLTTN
LYEGHIEKDT REFLDKQVCG TPEYIAPEVI LRQGYGKPVD WWAMGIILYE FLVGCVPFFG
DTPEELFGQV ISDEIVWPEG DDALPPDAQD LTSKLLHQNP LERLGTGSAY EVKQHPFFIG
LDWTGLLRQK AEFIPQLESE DDTSYFDTRS ERYHHIDSED EEEVSEDGYL EIRQFSSCSP
RFSKVYSSME RLSLLEERRM PPPTKRSLSE EKEDRSDSLA GLRSRERSWV IGSPEILRKR
LSVSESSHTE SDSSPPLTVR RHCSGLLDVP RFPEGTEEAG GPPRRQQQEG AWLLTPPSGE
WVSGPAPERP AERRLKLDEE PLGQSSASSP AAETRGGRGT PQLAEGATAK AISDLAVRRA
RHRLLSGDSI EKRTARPINK VIKSASATAL SLLIPTEHHT CSPLASPMSP HSQSSNPSSR
DSSPSRDFLP ALSSSRPPII IHRAGKKYGF TLRAIRVYMG DSDVYTVHHM VWHVEDGGPA
SEAGLRQGDL ITHVNGEPVH GLVHTEVVEL ILKSGNKVSI STTPLENTSI KVGPARKDSY
KAKMARRSKR SRGKDGQESR KRSSLFRKIT KQASLLHTSL CLSXXXXXXX XXXXXXTHSH
SLSPRSPTQG YRVTPEAVHS VGGNSSQSSS PSSSVPSSPA GSGHTRPSSL HGLAPKLQRQ
YRSPRRKSAG SIPLSPLAHT PSPPPAASPQ RSPSPLSGHG AQAFPTKLHL SPPLGRQLSR
PKSAEPPRSP LLKRVQSAEK LAAALAASEK KLATSRKHSL DLPHPELKKE LPPREVSPLE
VVGTRSVLSG KGALPGKGVL QAAPSRALGT LRQDRAERRE SLQKQEAIRE VDSSEDDTDE
GPENSQGVQE PSLVPNPEVG QDPLLRGAGA GEGEEEDAFL PRDPRSQGPV VPGLLTGVTL
GSPRMEGPSV PQKRLGILQA FEKAASSSSS APNLGRAGPT DPIPPEGCWK AQHLHTQALT
ALCPSSSGLI PTSCSTASTS GELGPWSWKF IVEGPDRASP TRKATMLDGL ASSQDLETTT
PVHPANLSPR QEGKSWPPSA PGLAHLPCEV PSQSWLWEPE CTQREEEEPA LGITKVPDAS
GDRRQDIPCK SCPLTQEPGP SLLQKGRDPG GPQKHQDLAL APDELLKQT
//
