MATK_RAT
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 03-AUG-2022, entry version 166.
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; P41243; -.
DR PRIDE; P41243; -.
DR Ensembl; ENSRNOT00000027730; ENSRNOP00000027730; ENSRNOG00000020431.
DR GeneID; 60450; -.
DR KEGG; rno:60450; -.
DR UCSC; RGD:69058; rat.
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 OMA; IMKLCWE; -.
DR OrthoDB; 491765at2759; -.
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 tissues.
DR Genevisible; P41243; RN.
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 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
