ID A0A3P8RF91_ASTCA Unreviewed; 1821 AA.
AC A0A3P8RF91;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Microtubule associated serine/threonine kinase family member 4 {ECO:0000313|Ensembl:ENSACLP00000039626.1};
GN Name=MAST4 {ECO:0000313|Ensembl:ENSACLP00000039626.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000039626.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000039626.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000039626.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 8154.ENSACLP00000039626; -.
DR Ensembl; ENSACLT00000040565.1; ENSACLP00000039626.1; ENSACLG00000026723.1.
DR GeneTree; ENSGT00940000156399; -.
DR OMA; SAPCAYD; -.
DR Proteomes; UP000265100; Chromosome 7.
DR Bgee; ENSACLG00000026723; Expressed in muscle tissue and 8 other cell types or tissues.
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 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; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..140
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 141..212
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 427..515
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 217..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1821 AA; 196296 MW; 1D05CC665CF49D9D CRC64;
MGHIKLTDFG LSKVGLMNMT TNLYEGHIEK DAREFSDKQV CGTPEYIAPE VILRQGYGKP
VDWWAMGIIL YEFLVGCVPF FGDTPEELFG QVISDEINWP DGDEAPPPDA QELITLLLRQ
NPLERLGTGG AAEVKQHQFF HNLDWNGLLR QKAEFIPQLE SEDDTSYFDT RSERYHHLET
EEEDTNDEDF NVDLRQFSSC SHRFSKVYSS LDLSRGHLEE KGETEEKKTE SPLTVDSLSW
TPDFAEAPSL SHSTDTDSMN QGPRPSLLPK FAISAESEGD ETSGIGDPSK ASFSIGEFPQ
DEPEAATPGS THSGATLSGS FSEHLDQLTP RGEGVESPDS TSHTSADHGP PSTSLRPESA
VEKSGAVPKV PKSVSTGALS LMIPGDIFGA SPLASPLSPY SLSSDPSSRD SSPSRDSSLC
PSNPRQPVVI HSSGKKFGFT LRAIRVYACD SDIYTVYHMV WNVEDGGPAH KAGLKAGDLI
THVNGEPVHG LVHTEVVELL LKSGSKVAIS TTPFENTSIK TGPARRNSYR SKMVRCGKKP
KKEKTPERRR SLFRRFAMQP SPLLHTSRSF SSLNHSLSSG ESLPGSPTHS LSPRSPTAAF
RPAPDFTQSG GNSSQSSSPS SSAPNSPAGS GHIRPSTLHG LGPKLPGQRL RQGRRKSAGS
IPLSPLARTP SPTPQPTSPQ RSPPPLLSGH SVAISKTTQG FPAKIHSPPT IVRHIVRPKS
AEPPRSPLLK RVQSEEKLSP SYTGEKKHLC PRKRSLEVTQ EEVQDEDVRT GERDFTGLQS
VDEAACEPLT ITRLRPVEQG CLKRPISRKM GRQESIEELD KEKLKSKMVV KRQEWSERRE
SLQKQDALHE SDSSAPCAYD GDEGFLVRSQ NKVQSSPESG TLEAKAASST LKDVLYKKLS
TRVSEGIAEP SGGSSESDGA LRSALCSGHP EWQHSRQGKD GMKPDRLDFK APSIEFTRKR
LSFEEREDCM CRLTSTLHEN LHFGSTRSKS LQLDTAMPHD HMKAGLGSVH SSPEGLAPKL
FSGRGESAVE KLHLISSAES PLRKTSSEYK LEGRHVSSLK PLEGTLDIGL LSGPRVSKTE
TCLSKMAENT SDTVSVNPPI RLQSPTERQI TIPQTKTTDK MKSPLTCSLS PETVSSVNSI
VVSKEQSNNS ATEMKVNASG EKTQDRQGES LKASNSKADP STFSVKQEGR TGMKASHEHR
GPRHSSHFSS CGKTPSIREV SNEDQEDEVE QQEEIPDTTS QNTDSSKTAV SLVDLKTSPP
FTTLEARAVS KPLTGPLKQS ADSVLDTGQL QSCEKRKTAA QSSDTTSRPA SEANVQTNSA
SVHVPANVPN ICSSNTEPGV SVSASAFGAL PDSKSEHSET SVSSSVKLVG DAGSSGSKTE
NSASSTAAKV EQKKEVCTIN KATSLNIITD ATLNKKHNTV SAAAVQDSGM SLQKKDVNVS
PKTKNTAAVK DSEQPSQMCP TEKAQHRSSD AQLCTSVVSV KENTVVPSAK LKSSGSTATS
ETVSSPKSKS RPDPQPTLPT SVKREKEAKT QESAAPPVPA VKGSPSSKEK DLPKESAPST
SHVQATHDAK RKEASPVSAG DGAKSEDSVQ AKPLPTHADT RQREIQPKCS AAVKDVPNSK
LKSLPPKTSS ALKPAAAPAI KQTLDSKPKD TSPKNHPTVI KDPRDPKTKE CALPLTTSQQ
LRKEPLPPSD VSSQPDPPAV LPKLPAKTEP PSSADTSGKG FSCEPAVKIS KDAPKSEVVK
PDSHKPPDTR TTTPDKPASS LRKEQGERKK KETAQEVTPA QKNTKRDTSR ASPSAAKDSL
DRDTSRCKQL KESPRSSSNK K
//
