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Database: UniProt
Entry: A0A1S3M582_SALSA
LinkDB: A0A1S3M582_SALSA
Original site: A0A1S3M582_SALSA 
ID   A0A1S3M582_SALSA        Unreviewed;      1152 AA.
AC   A0A1S3M582;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN   Name=LOC106570401 {ECO:0000313|RefSeq:XP_013998146.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013998146.1};
RN   [1] {ECO:0000313|RefSeq:XP_013998146.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013998146.1};
RG   RefSeq;
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   RefSeq; XP_013998146.1; XM_014142671.1.
DR   AlphaFoldDB; A0A1S3M582; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa14.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; -; 1.
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; 1.20.5.540; Single helix bin; 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:SF11; 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   Kinase {ECO:0000313|RefSeq:XP_013998146.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          72..392
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          516..774
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          794..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         548
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1152 AA;  130264 MW;  FA66B874BAEA6578 CRC64;
     MYADGYRCLS PHHSRVTCAC WPFLMGEYDR HLAHSKGMAT AYLDPNLNHA LAGGAKSRLS
     TTTERAPGAP DRVLKVFHHF ESNSEHSTWA SNIRHGDATD VRGIIQKILD IHKVKCVACF
     GLRLSHSQSG QVHWLHPDMG VSHVREKYEQ NRSQEEWRYE LRIRYLPKGF LHHFSEDKPT
     LNYFYQQVKN DYMVEIADQV EQDIALKLGC LEIRRFFREM RGNALDKKSN YELLEKDVGL
     RRFFPKSLLD SVKAKTLRKL IQQTFKQFAN MNDDQSILKF LEILAPVYRY DKECFKCALG
     LSWVIQVELA IGPEEGISYL TDKGSTPTHL ANFTQVQTIG YSVMEDKERK GMLQLNVAGA
     AEPLTVTTPS LTTAENMADL IDGYCRLVNG VTQSFIIRPQ KEGERALPSI PKVPNNEKRI
     VEGVVRSAGV RAISVSDSVN SVTPTPPKPA KARRFLLPFV FCAHDSPPKE TDDYAEIIDE
     DDTYTMPSTT SLYPNRPAVS YGVDEARDYE IQRDRIELGR CIGEGQFGDV HQGVYNSPEN
     PTLNVAIKTC KNSTSDSVRE KFLQEALTMR QFDHPHIVKL IGVITENPVW IIMELCTMGE
     LRSFLQVRKY NLDLSTLILF SHQLSTALAY LESKRFVHRD IAARNVLVSS TDCVMLGDFG
     LSRYMEDSSY YKASKGKLPI KWMAPESINF RRFTSASDVW MFGVCMWEIL MYGIKPFQGV
     KNNDVIGRIE NGERLAMPHN CPPTLYSLMT KCWAYDPSKR PRFTELKTQL STILEEEKAQ
     QEERLRMEMR RQVTVSWDSG GSDEAPPKPS RPGYPSPRSS EGFYPSPQHA GQLNHYQVGY
     PGPHGMPAMP SGGYPPQAGV LDPHETWNHH RPGDVPMWSP NMEDGGVLDL RGLGQVLPPH
     LMEERLMMQQ QQMEEDQRWL EQEECFLKPE SRNSRGSIDR EDCSLQGPTG NQHIYQPVGL
     GKPEHVAPPK KPPRPGAPSH LGSLASLNPV DSYNEGVKPW RIQPQEISPP PTANLDRSND
     KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PVLPASTHRE
     IEMAQKLLNS DLAELINKMK LAQQYVLTSL QQDYKKQMLT AAHALAVDAK NLLDVIDQAR
     LKMIHAQSRG SH
//
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