ID   SRK4_SPOLA              Reviewed;         506 AA.
AC   P42690;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-NOV-2023, entry version 117.
DE   RecName: Full=Tyrosine-protein kinase isoform SRK4;
DE            EC=2.7.10.2;
GN   Name=SRK1;
OS   Spongilla lacustris (Freshwater sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Spongillida; Spongillidae; Spongilla.
OX   NCBI_TaxID=6055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1378585;
RA   Ottilie S., Raulf F., Barnekow A., Hannig G., Schartl M.;
RT   "Multiple src-related kinase genes, srk1-4, in the fresh water sponge
RT   Spongilla lacustris.";
RL   Oncogene 7:1625-1630(1992).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=SRK4;
CC         IsoId=P42690-1; Sequence=Displayed;
CC       Name=SRK1;
CC         IsoId=P42686-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X61604; CAA43801.1; -; mRNA.
DR   PIR; S24553; S24553.
DR   AlphaFoldDB; P42690; -.
DR   SMR; P42690; -.
DR   BRENDA; 2.7.10.2; 5838.
DR   GO; GO:0005737; C:cytoplasm; 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; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd09933; SH2_Src_family; 1.
DR   CDD; cd11845; SH3_Src_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; 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; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF447; TYROSINE-PROTEIN KINASE SRC64B; 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; PR00452; SH3DOMAIN.
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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..506
FT                   /note="Tyrosine-protein kinase isoform SRK4"
FT                   /id="PRO_0000088157"
FT   DOMAIN          54..116
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          122..214
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          240..493
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         246..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   506 AA;  57562 MW;  8ABDF4A2546C280B CRC64;
     MGSCCSSQDG DGNGKATAGS TVDSHELSQS VKGKIKQPEP KPKPPPQVPP AQDVKYPIYV
     GKYDYDSRTD DDLSFKKGDL MYIISTDEGD WWFARSKDTA GKEGYIPSNY VAEYKSLDAE
     EWFFGQVKRV DAEKQLMMPF NNLGSFLIRD SDTTPGDFSL SVRDIDRVRH YRIKKLENGT
     YFVTRRLTFQ SIQELVAYYT QQADGLCVNL KGPCMVMEKP QTAGLSKQAN EEWEIEKKQI
     KLLRGLGAGQ FGEVWEGLWN GTTSVAVKTL KPGTMSIEEF LEEASIMKQL RHPKLIQLYA
     VCTKEEPIYI VTELMKHGSL LEYLRGDGRS LKLPDLVDMC SQVASGMSYL EQQNYIHRDL
     AARNILVGEH KICKVADFGL ARVIDEEIYE AKLGAKFPIK WTAPEAAMYS RFTIKSDVWS
     FGIVLYEVIT YGRFPYPGMT NAQVLEQIQQ SYRMPRPMGC PEKLYAIMMD CWREDPASRP
     TFETLSWQLE EFFTTGDDAG YKDMER
//