SRK1_SPOLA
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 03-AUG-2022, entry version 114.
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 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; 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; 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 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