ID   SRK1_SPOLA              Reviewed;         505 AA.
AC   P42686;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-NOV-2023, entry version 118.
DE   RecName: Full=Tyrosine-protein kinase isoform SRK1;
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=SRK1;
CC         IsoId=P42686-1; Sequence=Displayed;
CC       Name=SRK4;
CC         IsoId=P42690-1; Sequence=External;
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; X61601; CAA43798.1; -; mRNA.
DR   PIR; S24550; S24550.
DR   AlphaFoldDB; P42686; -.
DR   SMR; P42686; -.
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; cd05068; PTKc_Frk_like; 1.
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..505
FT                   /note="Tyrosine-protein kinase isoform SRK1"
FT                   /id="PRO_0000088156"
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   505 AA;  57693 MW;  6399E411C6112F91 CRC64;
     MGSCCSSQDG DGNGKATAGS TVDSHELSQS VKGKIKQPEP KPKPPPQVPP AQDVKYPIYV
     GKYDYDSRTD DDLSFKKGDL MYIISTDEGD WWFARSKDTA GKEGYIPSNY VAEYKSLDAE
     EWFLGKIKRV EAEKMLNQSF NQVGSFLIRD SETTPGDFSL SVKDQDRVRH YRVRRLEDGS
     LFVTRRSTFQ ILHELVDHYK IETDGLCCKL LYPCLQAEKP QTAGLLRQAN EEWEIEKTQI
     KLLRRLGAGQ FGEVWEGLWN GTTSVAVKTL KPGTMSVEEF LQEASIMKRL RHPKLIQLYA
     VCTKEEPIYI VTELMKYGSL LEYLRGEDGV LKIEQLVDVA AQVASGMSYL EQQNYIHRDL
     AARNILVGEH GICKVADFGL ARVIDEEIYE AHTGAKFPIK WTAPEAAMYN RFTIKSDVWS
     FGVVLYEIIT YGRFPYPGMT NPEVLEKIQQ NYRMPCPANC PKQFHDIMLD CWREDPASRP
     TFETLQWQLE EFFNSEGYRD PDAIH
//