MATK_MOUSE
ID MATK_MOUSE Reviewed; 505 AA.
AC P41242; Q6LE90;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Megakaryocyte-associated tyrosine-protein kinase;
DE EC=2.7.10.2;
DE AltName: Full=Protein kinase NTK;
DE AltName: Full=Tyrosine-protein kinase CTK;
GN Name=Matk; Synonyms=Ctk, Ntk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=7511815; DOI=10.1073/pnas.91.7.2597;
RA Klages S., Adam D., Class K., Fargnoli J., Bolen J.B., Penhallow R.C.;
RT "Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2597-2601(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=8197166; DOI=10.1073/pnas.91.11.4975;
RA Chow L.M.L., Jarvis C.D., Hu Q., Nye S.H., Gervais F.G., Veillette A.,
RA Matis L.A.;
RT "Ntk: a Csk-related protein-tyrosine kinase expressed in brain and T
RT lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4975-4979(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=DDY/STD;
RX PubMed=7898936;
RA Kaneko Y., Nonoguchi K., Fukuyama H., Takano S., Higashitsuji H.,
RA Nishiyama H., Takenawa J., Nakayama H., Fujita J.;
RT "Presence of alternative 5' untranslated sequences and identification of
RT cells expressing ctk transcripts in the brain and testis.";
RL Oncogene 10:945-952(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43 (ISOFORM 1), ALTERNATIVE
RP SPLICING, AND SUBCELLULAR LOCATION.
RC STRAIN=129/Sv; TISSUE=Kidney;
RX PubMed=7970703;
RA Chow L.M., Davidson D., Fournel M., Gosselin P., Lemieux S., Lyu M.S.,
RA Kozak C.A., Matis L.A., Veillette A.;
RT "Two distinct protein isoforms are encoded by ntk, a csk-related tyrosine
RT protein kinase gene.";
RL Oncogene 9:3437-3448(1994).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Could play a significant role in the signal transduction of
CC hematopoietic cells. May regulate tyrosine kinase activity of SRC-
CC family members in brain by specifically phosphorylating their C-
CC terminal regulatory tyrosine residue which acts as a negative
CC regulatory site. It may play an inhibitory role in the control of T-
CC cell proliferation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts with KIT. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7970703}. Membrane
CC {ECO:0000250}. Note=In platelets, 90% of MATK localizes to the membrane
CC fraction, and translocates to the cytoskeleton upon thrombin
CC stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P41242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41242-2; Sequence=VSP_004966;
CC Name=3;
CC IsoId=P41242-3; Sequence=VSP_011565;
CC -!- TISSUE SPECIFICITY: Most abundant in brain, and to a lesser extent in
CC the spleen, the thymus and the liver. Also found in the T-cell lineage.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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 EMBL; U05210; AAA18829.1; -; mRNA.
DR EMBL; L27738; AAB59677.1; -; mRNA.
DR EMBL; D45243; BAA08199.1; -; mRNA.
DR EMBL; L33339; AAA64431.1; -; Genomic_DNA.
DR CCDS; CCDS24048.1; -. [P41242-1]
DR CCDS; CCDS70078.1; -. [P41242-3]
DR PIR; I48926; I48926.
DR PIR; I59296; I59296.
DR RefSeq; NP_001272783.1; NM_001285854.1.
DR RefSeq; NP_001272784.1; NM_001285855.1.
DR RefSeq; NP_034898.1; NM_010768.2.
DR RefSeq; XP_006513358.1; XM_006513295.3.
DR RefSeq; XP_006513362.1; XM_006513299.2.
DR AlphaFoldDB; P41242; -.
DR BMRB; P41242; -.
DR SMR; P41242; -.
DR BioGRID; 201319; 11.
DR STRING; 10090.ENSMUSP00000113221; -.
DR iPTMnet; P41242; -.
DR PhosphoSitePlus; P41242; -.
DR EPD; P41242; -.
DR MaxQB; P41242; -.
DR PaxDb; P41242; -.
DR PRIDE; P41242; -.
DR ProteomicsDB; 292092; -. [P41242-1]
DR ProteomicsDB; 292093; -. [P41242-2]
DR ProteomicsDB; 292094; -. [P41242-3]
DR DNASU; 17179; -.
DR GeneID; 17179; -.
DR KEGG; mmu:17179; -.
DR UCSC; uc007ggv.2; mouse. [P41242-1]
DR CTD; 4145; -.
DR MGI; MGI:99259; Matk.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; P41242; -.
DR OrthoDB; 491765at2759; -.
DR PhylomeDB; P41242; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR BioGRID-ORCS; 17179; 1 hit in 74 CRISPR screens.
DR PRO; PR:P41242; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P41242; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR CDD; cd09937; SH2_csk_like; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035027; Csk-like_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..505
FT /note="Megakaryocyte-associated tyrosine-protein kinase"
FT /id="PRO_0000088074"
FT DOMAIN 46..108
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 120..209
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 233..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 483..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 239..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7511815,
FT ECO:0000303|PubMed:7898936"
FT /id="VSP_011565"
FT VAR_SEQ 43
FT /note="T -> TQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004966"
FT CONFLICT 105..106
FT /note="HG -> QR (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56056 MW; 0A1661C1FBFD6A53 CRC64;
MARRSSRVSW LAFEGWESRD LPRVSPRLFG AWHPAPAAAR MPTRWAPGTQ CMTKCENSRP
KPGELAFRKG DMVTILEACE DKSWYRAKHH GSGQEGLLAA AALRHGEALS TDPKLSLMPW
FHGKISGQEA IQQLQPPEDG LFLVRESARH PGDYVLCVSF GRDVIHYRVL HRDGHLTIDE
AVCFCNLMDM VEHYTKDKGA ICTKLVKPRR KQGAKSAEEE LAKAGWLLDL QHLTLGAQIG
EGEFGAVLQG EYLGQKVAVK NIKCDVTAQA FLDETAVMTK LQHRNLVRLL GVILHHGLYI
VMEHVSKGNL VNFLRTRGRA LVSTSQLLQF ALHVAEGMEY LESKKLVHRD LAARNILVSE
DLVAKVSDFG LAKAERKGLD SSRLPVKWTA PEALKNGRFS SKSDVWSFGV LLWEVFSYGR
APYPKMSLKE VSEAVEKGYR MEPPDGCPGS VHTLMGSCWE AEPARRPPFR KIVEKLGREL
RSVGVSAPAG GQEAEGSAPT RSQDP
