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Database: UniProt
Entry: B6DS95_STRPU
LinkDB: B6DS95_STRPU
Original site: B6DS95_STRPU 
ID   B6DS95_STRPU            Unreviewed;       521 AA.
AC   B6DS95;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=SFK7 {ECO:0000313|EMBL:ACI14304.1};
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668 {ECO:0000313|EMBL:ACI14304.1};
RN   [1] {ECO:0000313|EMBL:ACI14304.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19150445; DOI=10.1016/j.ydbio.2008.12.032;
RA   Townley I.K., Schuyler E., Parker-Gur M., Foltz K.R.;
RT   "Expression of multiple Src family kinases in sea urchin eggs and their
RT   function in Ca2+ release at fertilization.";
RL   Dev. Biol. 327:465-477(2009).
RN   [2] {ECO:0000313|Proteomes:UP000007110}
RP   NUCLEOTIDE SEQUENCE.
RA   Murali S., Liu Y., Vee V., English A., Wang M., Skinner E., Han Y.,
RA   Muzny D.M., Worley K.C., Gibbs R.A.;
RT   "Genome sequencing for Strongylocentrotus purpuratus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001135851}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC         ECO:0000256|RuleBase:RU362096};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   EMBL; FJ161084; ACI14304.1; -; mRNA.
DR   RefSeq; NP_001135851.1; NM_001142379.1.
DR   AlphaFoldDB; B6DS95; -.
DR   EnsemblMetazoa; NM_001142379; NP_001135851; GeneID_577286.
DR   GeneID; 577286; -.
DR   KEGG; spu:577286; -.
DR   CTD; 577286; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; B6DS95; -.
DR   OMA; XWYFGKL; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd05034; PTKc_Src_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   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007110};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|RuleBase:RU362096}.
FT   DOMAIN          68..129
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          135..233
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          255..506
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   521 AA;  58917 MW;  B49DE2DCB2E4B826 CRC64;
     MGCLHSTTNA PASDHRSKQP DTSFNSPGTG YNNGGSRPDQ PFTNIATPSF DQGPQNAIQP
     SQTHSAKKEV ISFIALYDYE ARSEDDLSFK KGEKLEILNN TDGDWWLARS PLTNKEGYIP
     SNYIARVKSI DAEDWYYGKV GRKDAEKKLL APGLQKGTFI VRDGEANPGT FSLSVRDHDP
     GKGEHIKHYR IRKLDNDSGY YITQRSQFQT LLELVHHYEQ SADGLCCSLS VPCPKENPIT
     AGLGKDMWEI PRESLKLDAK LGSGQFGEVW KGLWNGNTEV AVKTLRPKTM TPAAFLAEAN
     IMKTCRHENL VQLYAVCSDR EPIYIVTELM KHGSLLDYLK DGDGRHLKLP QLVDMGAQVA
     SGMGYLERKN YVHRDLAARN VLVNTGNICK VADFGLARMI QDDEYCARQG AKFPIKWTSP
     EAALYGRFTI KSDVWSFGIL LTELITYGRI PYPGMMNMEV LEQVERGYRM PRPHNCPDSL
     YDMCMMKCWH KDSQQRPTFE FLHSFLDDYF VSTEPNYREA D
//
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