ID A0A3Q0GFG6_ALLSI Unreviewed; 2034 AA.
AC A0A3Q0GFG6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Microtubule-associated serine/threonine-protein kinase 4 isoform X3 {ECO:0000313|RefSeq:XP_025057175.1};
GN Name=MAST4 {ECO:0000313|RefSeq:XP_025057175.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025057175.1};
RN [1] {ECO:0000313|RefSeq:XP_025057175.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025057175.1; XM_025201390.1.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; 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:SF224; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_025057175.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..246
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 247..319
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 549..622
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 320..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1818..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1946..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1955..1988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2034 AA; 222750 MW; CEBE742E83A68042 CRC64;
MKKINRQNLI LRNQIQQAFV ERDILTFAEN PFVVSMYCSF ETRRHLCMVM EYVEGGDCAT
LMKNMGPLPV DMARMYFAET VLALEYLHNY GIVHRDLKPD NLLVTSMGHI KLTDFGLSKV
GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGIILYEFL
VGCVPFFGDT PEELFGQVIS DEINWPEKDE APPPDAQDLI TLLLRQNPLE RLGTGGAYEV
KQHQFFRSLD WNSLLRQKAE FIPQLESEDD TSYFDTRSEK YHHMETEEED DTNDEDFNLE
IRQFSSCSHR FSKVFSSIDR ASQNQNEEKE DTGEKTKNAT LPCVESLSWS SEYSETQQLS
TSNSSDTEST RQQHGSGFLP KLAISAEADQ DETTCLGESR EEQEKATFAN EEHGQDELEV
TTPASTISSS TLSVGSFSEH LDQINARIES VDSTDNSSKP SSETASHMAR QRLESTEKKK
ISGKVTKSLS ASALSLMIPG GRSSVPDVFG ISPLGSPMSP HSLSSDPSSS RDSSPSRESS
IAAASPHQPI VIHSSGKKYG FTIRAIRVYV GDSDIYTVHH IVWNVEEGSP AYQAGLKAGD
LITHINGEPV HGLVHTEVIE LLLKSPVTKR DSILITIYFW QSGNKVSITT TPFENTSIKT
GPARRNSYRS RMVRRSKKTK KKESLERRRS LFKKLAKQPS PLLHTSRSFS CLNRSLSSGE
SLPGSPTHSL SPRSPTPSYR STPDFPSGTN SSQSSSPSSS APNSPAGSGH IRPSTLHGLG
PKLGGQRYRS GRRKSAGSIP LSPLARTPSP TPQPTSPQRS PSPLLGHSIG NSKIAQAFPS
KMHSPPTIVR HIVRPKSAEP PRSPLLKRVQ SEEKLAPSYG SDKKHICSRK HSLEVTQEEV
NKELSQREVT LQSLEENVCD VPSLTRVRPA EQGCLKRPVS RKLGRQESID ELDREKLKVK
IVMKKQDLSE KANTIPEPSG ELEHPATLRL EERDKKTFQK ALERSNQFET KITSLETHSG
GSILKDMLHK NANMRSNDCT ALDKQMPCHG PPLNELGHIS YDFKRISPPC TLQDVLPHST
DRMLNGKGEN ADKNVPTKDL IKFERLDGKL ANIDYLRKKM SFEEKDDSLC PVLKTKLTSN
VHECLQLNTV RPINIQQDST TAADSRAFIS SAHAAQISSV SFVPLKALNG RVETGVEKSS
LITTESPVRK SPSEYKLEGR SVSCLKPIEG TLDIALLSGP QTSKTDLPVC ALPEGPSTSS
SVGYSMPQAS QGSGINRDMP CQKELLLSCS ESNKSNLLEP QLLQSRKGSP NSPVIPVTTE
VEREKRISHP SAKCSFSVNE VNQKREDSYS KQADHAAEAK SQAVQHQCAK PVPTSSKAST
AQDFPEKAVG KQRQTQRELP IKYPLAQRNS ESLPAKAEVN RDLPVKLSVG DVFTSESKII
QRISADFAVP LQTNATKLQT PGLKAEPKDG KGSPKQVAKD GANPAGVSVE KNVNKQKVIT
DSKNETSLSK RSVQPSTNTD PKSEKSLLGS SIQKDNSKDW GKKELKQSSN TQLQTAERLV
LNQATGQQLS YSGSSSVRES VNRNRVDAHV GVQEQVKPGT PSMETSNNKS RQVPDTSSSK
SKPFDKVTLS QKQCTANIKE KEVLVQPSAS SRKDGKPASK SMQDPPCFVS SSERRLTNEY
VQVDRPVVLE RASVSAIQSD RSTSESKSKP SCIGHVSAIP ENIKPSQRPE PAGFSELADQ
KQLYTSEKQS MPPKFSTVKD SLSLSKQADK SPSSHIISAD KRPEGKKFTE ALYVQNDNGK
LEPSISLVNC DARGKGAEKA TLGSKGSQDS KGKGQVNQKQ LTDASKQIAT KHPSSATVQS
SCCAAATPAK QLICPPSFPE CKQEASVFSS ANNDASSTKV QGSLPEVPVA SSKELKKPTS
CSTGDGKMVM TKSISLVTLP SAALPPEALH PASNLGGKSG NQERSLSSNN TVDVKGKDTS
QAQPPSTRKL NVGKDIPRSV TTPDRPHALS SDKDSARQRR GKDAARSSPH KKSS
//
