ID A0A2U3XC76_LEPWE Unreviewed; 1647 AA.
AC A0A2U3XC76;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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_006729079.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006729079.1};
RN [1] {ECO:0000313|RefSeq:XP_006729079.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006729079.1};
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_006729079.1; XM_006729016.2.
DR STRING; 9713.A0A2U3XC76; -.
DR GeneID; 102727274; -.
DR KEGG; lww:102727274; -.
DR CTD; 23139; -.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000245341; 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_006729079.1};
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:UP000245341};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 373..646
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 647..715
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 960..1048
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1647
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 26..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 179767 MW; FE417DAA8609DAD2 CRC64;
MRNQSLGQSA PSLTAGLKEL SLPRRGSFCR TSNRKSLIVT SSTSPTLPRP HSPLHGHTGN
SPLDSPRNFS PNAPAHFSFV PARRTDGRRW SLASLPSSGY GTNTPSSTVS SSCSSQEKLH
QLPFQPTADE LHFLTKHFST ESVPDEEGRQ SPAMRPRSRS LSPGRSPVSF DSEIIMMNHV
YKERFPKATA QMEEHLAEFI SSNMPDSVLP LADGTLSFIH HQVIEIARDC LDKSQNRLIT
SHYFYELQEN LEKLLQDAHE RSQSSEVAFV MQLVKKLMIV IARPARLLEC LEFDPEEFYH
LLEAAEGHAK EGQGIKCDIP RYIVSQLGLT RDPLEEMAQL SSYDSPDTPE TDDSVEGRGA
SLTSKKTPSE EDFETIKLIS NGAYGAVFLV RHKSTRQRFA MKKVNKQNLI LRNQIQQAFV
ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT LLKNIGALPV DMVRLYFAET
VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI GLMSLTTNLY EGHIEKDARE
FLDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGIILYEFL VGCVPFFGDT PEELFGQVIS
DEIVWPEGDD ALPPDAQDLT SKLLHQNPLE RLGTGSASEV KQHSFFTGLD WTGLLRQKAE
FIPQLESEDD TSYFDTRSER YHHVDSEDEE EVSEDGCLEI RQFSSCSPRF SKVYSSMERL
SLLEERRAPP PTKRSLSEEK DDRSDGLAGL KGRDRSWVIG SPEILRKRLS VSESSHTESD
SSPPLTVRRR CSGLLDAPRF PEGPDEASST PRRQQQEDTW LLTAPSGEGL SGPVERRLKL
DEEPLGQSCG PSPAVETRGG RGTPQLTEGA TAKAISDLAV RRARHRLLSG DSVEKRTTRP
ISKVIKSASA TTLSLLIPAE HTCSPLASPM SPHSQSSNPS SRDSSPSRDF LPALSSSRPP
IIIHRAGKKY GFTLRAIRVY MGDSDVYTVH HMVWHVEDGG PASEAGLRQG DLITHVNGEP
VHGLVHTEVV ELILKSGNKV SISTTPLENT SIKVGPARKG SYKAKMARRS KRSRGKDGQE
SRKRSSLFRK ITKQASLLHT SRSLSSLNRS LSSGESGPGS PTHSHSLSPR SPTQGYRVTP
DAVHSVGGTS SQSSSPSSSV PSSPAGSGHT RPSSLHGLAP KLQRQYRSPR RKSAGSIPLS
PLAHTPSPPP AASPQRSPSP LSGHGAQALP AKLHLSPPLG RQLSRPKSAE PPRSPLLKRV
QSAEKLAAAL AASEKKLGTA RKHSLDLPHP ELKKEPPPRE VSPLEAVGTR SVLSGKGVLQ
PSPSWALGTL RQDRAERRES LQKQEAIREV DSSEDDAEEG PENGQGVQEP SLAPSPAVGR
VPPLAGAGEG EEEDAFSSRG PQSQGPVVPG LLTEVTLKPP RMEGPSVPQR KLGIPQAFEE
AASSSSAAPS LRKAGRTDPI PPEGCWKAQP FHTQALTALC PSSSGLIPTS RSAASSTSGE
PGPWSWKFLI KGADGASPSR KAAMEGGMAS SQDLETITPA HPENLSPRQE GKSWPPGAPG
LVHPPREFPH QSWLWEPAGA QREKEEPALG ITEVPDASGD TRQDVPCRSC PLTQEPGPSL
LQRGREPGAP QKHQDLALVP DELLKQT
//
