MAST1_RAT
ID MAST1_RAT Reviewed; 1570 AA.
AC Q810W7; Q810W8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Syntrophin-associated serine/threonine-protein kinase;
GN Name=Mast1 {ECO:0000312|RGD:631372};
GN Synonyms=Sast {ECO:0000303|PubMed:12614677};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO72536.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAO72536.1};
RX PubMed=12614677; DOI=10.1016/s0306-4522(02)00785-6;
RA Yano R., Yap C.C., Yamazaki Y., Muto Y., Kishida H., Okada D.,
RA Hashikawa T.;
RT "Sast124, a novel splice variant of syntrophin-associated serine/threonine
RT kinase (SAST), is specifically localized in the restricted brain regions.";
RL Neuroscience 117:373-381(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; SER-346; THR-351;
RP SER-689; SER-954 AND SER-1414, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Microtubule-associated protein essential for correct brain
CC development (By similarity). Appears to link the dystrophin/utrophin
CC network with microtubule filaments via the syntrophins. Phosphorylation
CC of DMD or UTRN may modulate their affinities for associated proteins.
CC Isoform 2 may play a role in neuronal transcriptional regulation.
CC {ECO:0000250|UniProtKB:Q9R1L5, ECO:0000269|PubMed:12614677,
CC ECO:0000303|PubMed:12614677}.
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:0000250|UniProtKB:Q9BXM7};
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:0000250|UniProtKB:Q9BXM7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BXM7};
CC -!- SUBUNIT: Interacts with the microtubules. Part of a low affinity
CC complex that associates with, but is distinct from, the postsynaptic
CC density. Interacts with SNTB2. {ECO:0000250|UniProtKB:Q9R1L5}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:Q9R1L5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9R1L5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9R1L5}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9R1L5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9R1L5}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9R1L5}. Note=Also localized in the soma of
CC neurons. Observed as punctate clusters in the processes of interneurons
CC and along the cell body periphery. Colocalizes with syntrophins at the
CC cell membrane. {ECO:0000250|UniProtKB:Q9R1L5}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12614677}; Synonyms=Sast170
CC {ECO:0000303|PubMed:12614677};
CC IsoId=Q810W7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12614677}; Synonyms=Sast124
CC {ECO:0000303|PubMed:12614677};
CC IsoId=Q810W7-2; Sequence=VSP_051684;
CC -!- TISSUE SPECIFICITY: Both isoform 1 and isoform 2 appear to be
CC restricted to the brain. Isoform 2 is strongly expressed in the neurons
CC of the subventricular zone and granule cells of the olfactory bulb,
CC Islands of Calleja, hippocampal dentate gyrus and cerebellum.
CC {ECO:0000269|PubMed:12614677}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AY227206; AAO72535.1; -; mRNA.
DR EMBL; AY227207; AAO72536.1; -; mRNA.
DR RefSeq; NP_851603.1; NM_181089.1. [Q810W7-1]
DR AlphaFoldDB; Q810W7; -.
DR SMR; Q810W7; -.
DR BioGRID; 261861; 1.
DR IntAct; Q810W7; 1.
DR STRING; 10116.ENSRNOP00000004646; -.
DR iPTMnet; Q810W7; -.
DR PhosphoSitePlus; Q810W7; -.
DR jPOST; Q810W7; -.
DR PaxDb; Q810W7; -.
DR PRIDE; Q810W7; -.
DR Ensembl; ENSRNOT00000004646; ENSRNOP00000004646; ENSRNOG00000003469. [Q810W7-1]
DR GeneID; 353118; -.
DR KEGG; rno:353118; -.
DR CTD; 22983; -.
DR RGD; 631372; MAST1.
DR eggNOG; KOG0605; Eukaryota.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000157700; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR InParanoid; Q810W7; -.
DR OMA; GMREKSW; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; Q810W7; -.
DR TreeFam; TF313149; -.
DR PRO; PR:Q810W7; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000003469; Expressed in cerebellum and 3 other tissues.
DR Genevisible; Q810W7; RN.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 1.20.1480.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR028777; MAST1.
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:SF150; PTHR24356:SF150; 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; SSF140482; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1570
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000086311"
FT DOMAIN 376..649
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 650..721
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 969..1057
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 23..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 499
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 382..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1090..1117
FT /note="SKKRSSLFRKITKQSNLLHTSRSLSSLN -> RGHEFKSQQPHGGSQPSVTR
FT SNTLFWCV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12614677"
FT /id="VSP_051684"
SQ SEQUENCE 1570 AA; 171028 MW; 3BFFCA50771BACB9 CRC64;
MSDSLWTALS NFSMPSFPGG SMFRRTKSCR TSNRKSLILT STSPTLPRPH SPLPGHLGSS
PLDSPRNFSP NTPAHFSFAS SRRADGRRWS LASLPSSGYG TNTPSSTVSS SCSSQERLHQ
LPYQPTVDEL HFLSKHFGST ESITDEDGGR RSPAVRPRSR SLSPGRSPSS YDNEIVMMNH
VYKERFPKAT AQMEEKLRDF ARAYEPDSVL PLADGVLSFI HHQIIELARD CLTKSRDGLI
TTVYFYELQE NLEKLLQDAY ERSESLEVAF VTQLVKKLLI IISRPARLLE CLEFNPEEFY
HLLEAAEGHA KEGHLVKTDI PRYIIRQLGL TRDPFPDVVR LEEQDSGGSN TPEQDDTSEG
RSSTSKAKKP PGESDFDTIK LISNGAYGAV YLVRHRDTRQ RFAMKKINKQ NLILRNQIQQ
AFVERDILTF AENPFVVGMF CSFETRRHLC MVMEYVEGGD CATLLKNIGA LPVEMARMYF
AETVLALEYL HNYGIVHRDL KPDNLLITSM GHIKLTDFGL SKMGLMSLTT NLYEGHIEKD
AREFLDKQVC GTPEYIAPEV ILRQGYGKPV DWWAMGIILY EFLVGCVPFF GDTPEELFGQ
VISDDILWPE GDEALPTDAQ LLISSLLQTN PLVRLGAGGA FEVKQHSFFR DLDWTGLLRQ
KAEFIPHLES EDDTSYFDTR SDRYHHVNSY DEDDTTEEEP VEIRQFSSCS PRFSKVYSSM
EQLSQHEPKT PVSASGASKR DPNAKGPEEK VAGKREGLGG LTLREKTWRG GSPEIKRFSA
SEASFLEGEA SPPLGARRRF SALLEPSRFT APQEDEDEAR LRRPPRPSSD PPSSLDTRVP
KEAAQGEGTS TPGEPEATER SHPGDFCPPS KDGDPSGPRA TNDLVLRRAR HQQLSGDLSV
EKRPSRTGGK VIKSASATAL SVMIPAVDPH GGSPLASPMS PRSLSSNPSS RDSSPSRDYS
PAVSGLRSPI TIQRSGKKYG FTLRAIRVYM GDSDVYSVHH IVWHVEEGGP AQEAGLCAGD
LITHVNGEPV HGMVHPEVVE LILKSGNKVA VTTTPFENTS IRIGPARRSS YKAKMARRNK
RPSAKDGQES KKRSSLFRKI TKQSNLLHTS RSLSSLNRSL SSSDSLPGSP THGLPARSPT
HSYRSTPDSA YLGASSQSSS PASSTPNSPA SSASHHIRPS TLHGLSPKLH RQYRSARCKS
AGNIPLSPLA HTPSPTQASP PPLPGHTVGS SHTTQSFPAK LHSSPPIVRP RPKSAEPPRS
PLLKRVQSAE KLGASLGADK KGALRKHSLE VGHPDFRKDF HGELALHSLA ESDGETPPIE
GPGATRQVAM RRLGRQESPL SLGADPLLPD GVQRPMASGK EDSAGGTEAC TPPRATTPGS
RTLERDLGCT RHQSVQTEDG PGGVARALAK AALSPVQEHE TGRRSSSGEA GTPPVPIVVE
PARPGVKTQT PQPLGTDSKG LKEPVAQIPL VPDAPRVRER WVLEEVEERT TLSGPRSKPA
SPKLSPDPQT PTVAPTKNVP RSAAPPVPPA SLMVPGTKPE AGSNSRCPAE GVASAGLTKT
GAPSPASLGP
