ID MATK_RAT Reviewed; 467 AA. AC P41243; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 24-JAN-2024, entry version 173. DE RecName: Full=Megakaryocyte-associated tyrosine-protein kinase; DE EC=2.7.10.2; DE AltName: Full=Protein kinase BATK; DE AltName: Full=Tyrosine-protein kinase CTK; GN Name=Matk; Synonyms=Batk, Ctk; 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] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RX PubMed=7807586; DOI=10.1002/jnr.490380613; RA Kuo S.S., Moran P., Gripp J., Armanini M., Phillips H.S., Goddard A., RA Caras I.W.; RT "Identification and characterization of Batk, a predominantly brain- RT specific non-receptor protein tyrosine kinase related to Csk."; RL J. Neurosci. Res. 38:705-715(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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. 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:0000250}. Membrane {ECO:0000250}. CC Note=In platelets, 90% of MATK localizes to the membrane fraction, and CC translocates to the cytoskeleton upon thrombin stimulation. CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Enriched in lymphoid tissues. 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; L34542; AAA64524.1; -; Genomic_DNA. DR EMBL; BC087726; AAH87726.1; -; mRNA. DR PIR; I56579; I56579. DR RefSeq; NP_068631.1; NM_021859.2. DR RefSeq; XP_006241051.1; XM_006240989.3. DR RefSeq; XP_006241052.1; XM_006240990.3. DR RefSeq; XP_008763350.1; XM_008765128.2. DR AlphaFoldDB; P41243; -. DR BMRB; P41243; -. DR SMR; P41243; -. DR BioGRID; 248843; 2. DR IntAct; P41243; 1. DR STRING; 10116.ENSRNOP00000027730; -. DR iPTMnet; P41243; -. DR PhosphoSitePlus; P41243; -. DR PaxDb; 10116-ENSRNOP00000027730; -. DR Ensembl; ENSRNOT00000027730.5; ENSRNOP00000027730.4; ENSRNOG00000020431.6. DR Ensembl; ENSRNOT00055057237; ENSRNOP00055047191; ENSRNOG00055033114. DR Ensembl; ENSRNOT00060054831; ENSRNOP00060045335; ENSRNOG00060031639. DR Ensembl; ENSRNOT00065037356; ENSRNOP00065030159; ENSRNOG00065021931. DR GeneID; 60450; -. DR KEGG; rno:60450; -. DR UCSC; RGD:69058; rat. DR AGR; RGD:69058; -. DR CTD; 4145; -. DR RGD; 69058; Matk. DR eggNOG; KOG0197; Eukaryota. DR GeneTree; ENSGT00940000160775; -. DR HOGENOM; CLU_000288_7_2_1; -. DR InParanoid; P41243; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P41243; -. DR BRENDA; 2.7.10.2; 5301. DR Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling. DR PRO; PR:P41243; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000020431; Expressed in frontal cortex and 20 other cell types or tissues. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd09937; SH2_csk_like; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24418:SF399; MEGAKARYOCYTE-ASSOCIATED TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. 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; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; P41243; RN. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding; KW Reference proteome; SH2 domain; SH3 domain; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1..467 FT /note="Megakaryocyte-associated tyrosine-protein kinase" FT /id="PRO_0000088075" FT DOMAIN 7..69 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 81..170 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 194..443 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 445..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 311 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 200..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 221 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 467 AA; 51897 MW; 283FF9348BB5FA8F CRC64; MPTQRWAPGT QCMTKCENSR PKPGELAFRK GDMVTILEAC EDKSWYRAKH HSSGQEGLLA AAALRQREAL STDPKLSLMP WFHGKISGQE AIQQLQPPED GLFLVRESAR HPGDYVLCVS FGRDVIHYRV LHRDGHLTID EAVCFCNLMD MVEHYTRDKG AICTKLVKPK RKQGAKSAEE ELAKAGWLLD LQHLTLGAQI GEGEFGAVLQ GEYLGQKVAV KNIKCDVTAQ AFLDETAVMT KLQHRNLVRL LGVILHHGLY IVMEHVSKGN LVNFLRTRGR ALVSTSQLLQ FALHVAEGME YLESKKLVHR DLAARNILVS EDLVAKVSDF GLAKAELRKG LDSSRLPVKW TAPEALKNGR FSSKSDVWSF GVLLWEVFSY GRAPYPKMSL KEVSEAVEKG YRMEPPDSCP GPVHTLMGSC WEAEPSRRPP FRKIVEKLGR ELRSVGVAAP AGGQEAEGSA PTRSQDP //