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Database: UniProt
Entry: A0A3Q4BKB8_MOLML
LinkDB: A0A3Q4BKB8_MOLML
Original site: A0A3Q4BKB8_MOLML 
ID   A0A3Q4BKB8_MOLML        Unreviewed;       900 AA.
AC   A0A3Q4BKB8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000020567.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000020567.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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DR   AlphaFoldDB; A0A3Q4BKB8; -.
DR   STRING; 94237.ENSMMOP00000020567; -.
DR   Ensembl; ENSMMOT00000020910.1; ENSMMOP00000020567.1; ENSMMOG00000015649.1.
DR   OMA; EIMSYGQ; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13190; FERM_C_FAK1; 1.
DR   CDD; cd05056; PTKc_FAK; 1.
DR   Gene3D; 1.20.80.10; -; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR041390; FADK_N.
DR   InterPro; IPR049385; FAK1-like_FERM_C.
DR   InterPro; IPR041784; FAK1/PYK2_FERM_C.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR   InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46221; FERM AND PDZ DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR46221:SF7; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR   Pfam; PF21477; FERM_C_FAK1; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF18038; FERM_N_2; 1.
DR   Pfam; PF03623; Focal_AT; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF68993; FAT domain of focal adhesion kinase; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          38..337
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          401..661
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          746..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          693..724
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         433
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   900 AA;  103373 MW;  4D3EE9EF8585811C CRC64;
     MYEVMSGDTL GWKVPSPRQS VVEPSPELHL TGDGGSVKIL KVCFCTNNNL GKNFKLVKCD
     SSWQIRAIIR SILISGRLGP NIEHVGSYGL LLKHLKSEEL HWLHPDLTVG EVEQRYESHH
     VEAEWRYDLR IRYVPVNFLE KFKDDRSTFL YFYQQVRSDY MQDHASKVSD GMALQLGCLE
     LRRFYKDMNA KGLEKKSNFE LLEQLRKLIQ QTFQQYATLK EDDCMVKFFE TLKDFVSYDE
     EVFPCELVQG WSLSVELVIG GRGIRQRTQK NSAPVFLADF KQIKKIQCFS QSAGKALVHL
     DVEGARQRLS INVATVPMAE NMMDLIDGYC RLEKDTDDTV IYRPNKGVFL RMSRCTVKLN
     MQHHTHCSVK TVLSGSDIYC EILDERPKSG LLKYGISRSD IVLGRILGEG FFGEVYDGVY
     KNDNGGRINV AVKTCKDCAP DVMEKFMSEA VIMKNLDHQH IVKLIGIIED DPVWIVMELY
     QYGELGNYLT QNQNKLTNIT LVLFSLQICK ALVYLEGVNM VHRDIAVRNV LVAGPECVKL
     GDFGLSRYIE DEEYYKASVS RLPIKWMAPE SINFRRFTTA SDVWMFAVCM WEIMSYGQQP
     FFWLENRDVI NQLEQGIRLP KPDNCPPALY SLMTRCWSYD PGERPSFTEL VVKISDVHKM
     EKEQEVERER DRALMCLCTF SDTLEANSRE DAQRLWQRER QQMQETLRQQ KEQMMEDKMW
     LEKEERLLVG SRASLTVVDP LSVSLSAPEK PPRLKAQPAP TAELDRSDDK VYQAVMDLVK
     VVVQLKNDIP EVKPEQYISI VQSVGMALRD LIRSVDDILP TLHESIRTEI EGTQKLLNND
     MAELISKMRL AQQNAITSLK EECKKQMLAA AHTLAMDSKN MLDAVDQARV RANLAKPVDL
//
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