SRMS_MOUSE
ID SRMS_MOUSE Reviewed; 496 AA.
AC Q62270; Q62360; Q923M5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tyrosine-protein kinase Srms;
DE EC=2.7.10.2 {ECO:0000250|UniProtKB:Q9H3Y6};
DE AltName: Full=PTK70;
GN Name=Srms; Synonyms=Srm;
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=9226137; DOI=10.1111/j.1600-0625.1997.tb00161.x;
RA Kawachi Y., Nakauchi H., Otsuka F.;
RT "Isolation of a cDNA encoding a tyrosine kinase expressed in murine skin.";
RL Exp. Dermatol. 6:140-146(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Lung;
RX PubMed=7935409; DOI=10.1128/mcb.14.10.6915-6925.1994;
RA Kohmura N., Yagi T., Tomooka Y., Oyanagi M., Kominami R., Takeda N.,
RA Chiba J., Ikawa Y., Aizawa S.;
RT "A novel nonreceptor tyrosine kinase, Srm: cloning and targeted
RT disruption.";
RL Mol. Cell. Biol. 14:6915-6925(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase which phosphorylates
CC DOK1 on tyrosine residues. Also phosphorylates KHDRBS1/SAM68 and VIM on
CC tyrosine residues. Phosphorylation of KHDRBS1 is EGF-dependent.
CC {ECO:0000250|UniProtKB:Q9H3Y6}.
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 (via the SH2 and SH3 domains) with DOK1. Interacts
CC with KHDRBS1/SAM68 and VIM. {ECO:0000250|UniProtKB:Q9H3Y6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H3Y6}.
CC Note=Localizes to punctate cytoplasmic structures.
CC {ECO:0000250|UniProtKB:Q9H3Y6}.
CC -!- TISSUE SPECIFICITY: Higher expression in liver, lung, thymus and skin
CC than in brain, kidney, heart and spleen (PubMed:9226137). In skin,
CC highly expressed in keratinocytes (PubMed:9226137). Abundant in lung,
CC liver, spleen, kidney and testis and is also detected in the cerebrum
CC (PubMed:7935409). {ECO:0000269|PubMed:7935409,
CC ECO:0000269|PubMed:9226137}.
CC -!- DEVELOPMENTAL STAGE: In the brain, expression is low at 11 dpc with
CC higher levels detected in 15 dpc and postnatal brain. Expressed at low
CC levels in adult brain. {ECO:0000269|PubMed:7935409}.
CC -!- DOMAIN: The N-terminal region regulates its kinase activity.
CC {ECO:0000250|UniProtKB:Q9H3Y6}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:7935409}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D49427; BAA08406.1; -; mRNA.
DR EMBL; D26186; BAA05331.1; -; mRNA.
DR EMBL; AL450341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A56040; A56040.
DR AlphaFoldDB; Q62270; -.
DR SMR; Q62270; -.
DR STRING; 10090.ENSMUSP00000016498; -.
DR iPTMnet; Q62270; -.
DR PhosphoSitePlus; Q62270; -.
DR MaxQB; Q62270; -.
DR PaxDb; Q62270; -.
DR PRIDE; Q62270; -.
DR ProteomicsDB; 254560; -.
DR MGI; MGI:101865; Srms.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; Q62270; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-8849472; PTK6 Down-Regulation.
DR ChiTaRS; Srm; mouse.
DR PRO; PR:Q62270; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62270; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
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; PF14604; SH3_9; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
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; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..496
FT /note="Tyrosine-protein kinase Srms"
FT /id="PRO_0000088161"
FT DOMAIN 55..116
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 124..216
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 234..495
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 240..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 384
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Y6"
FT CONFLICT 78
FT /note="R -> G (in Ref. 2; BAA05331)"
FT /evidence="ECO:0000305"
FT CONFLICT 236..237
FT /note="LR -> FG (in Ref. 2; BAA05331)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> K (in Ref. 1; BAA08406)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="I -> N (in Ref. 1; BAA08406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55758 MW; 7FE39C9912219BAF CRC64;
MEPFLRKRLT FLSFFWDKIW PADESEEDIP RIQGHDDNPV PEQAAAVEPC SFPAPRARLF
RALYDFTARC AEELSVSRGD RLYALKEEGD YIFAQRLSGP PSTGLVPVTY LAKATPEPPS
DQPWYFSGIS RAQAQQLLLS PANAPGAFLI RPSESSIGGY SLSVRAQAKV CHYRICMAPS
GSLYLQEGQL FPSLDALLAY YKTNWKLIQN PLLQPCIPQI PLVQDEWERP RSEFVLRRKL
GEGFFGEVWE GLWLGSIPVA VKVIKSADMK LADLTKEIEA LKSLRHERLI RLHAICSLGE
PVYIVTELMG KGNLQVYLGS SEGKALSLPH LLGFACQVAE GMSYLEERRV VHRDLAARNV
LVGDDLTCKV ADFGLARLLK DDVYSPSSGS KIPVKWTAPE AANYRVFSQK SDVWSFGILL
YEVFTYGQCP YEGMTNHETL QQISRGYRLP RPAVCPAEVY VLMVECWKGS PEERPTFAIL
REKLNAINRR LHLGLT
