ID A0A2Y9LQD9_DELLE Unreviewed; 1096 AA.
AC A0A2Y9LQD9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Focal adhesion kinase 1 {ECO:0000256|ARBA:ARBA00039644};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE AltName: Full=Protein-tyrosine kinase 2 {ECO:0000256|ARBA:ARBA00042078};
DE AltName: Full=pp125FAK {ECO:0000256|ARBA:ARBA00043012};
GN Name=PTK2 {ECO:0000313|RefSeq:XP_022410931.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410931.1};
RN [1] {ECO:0000313|RefSeq:XP_022410931.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022410931.1};
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}. Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000256|ARBA:ARBA00004120}. 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_022410931.1; XM_022555223.2.
DR AlphaFoldDB; A0A2Y9LQD9; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0051239; P:regulation of multicellular organismal process; 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:SF8; 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_022410931.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 79..399
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 466..724
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 729..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1096 AA; 123798 MW; 02EDF4B040021B2F CRC64;
MLFEVTGRGA LGPTGAVCME KSGCSPFPVC WAKEYDRYLA SSKIMAAAYL DPNLNHTPNS
STKTHLGTGV ERSPGAMERV LKVFHYFESN SEPTTWASII RHGDATDVRG IIQKIVDSHK
VKHVACYGFR LSHLRSEEVH WLHLDMGVSN VREKYELAHP PEEWKYELRI RYLPKGFLNQ
FTEDKPTLNF FYQQVKSDYM LEVADQVDQD IALKLGCLEI RRSYWEMRGN ALEKKSNYEV
LEKDVGLKRF FPRSLLDSVK AKTLRKLIQQ TFRQFANLNR EESILKFFEI LSPVYRFDKE
CFKCALGSSW IISVELAIGP EEGISYLTDK GCNPTHLADF NQVQTIQYSN SEDKDRKGTL
QLKIAGAPEP LTVTAPSLTI AENMADLIDG YCRLVHGATQ SFIIRPQKEG ERALPSIPKL
ANSEKQGVRT HAVSVSETDD YAEIIDEEDT YTMPSTRDYE IQRERIELGR CIGEGQFGDV
HQGAYTSPEN PALAVAIKTC KNCTSDSVRE KFLQEALTMR QFDHPHIVKL IGVITENPVW
IIMELCTLGE LRSFLQVRKY SLDLASLILY AYQLSTALAY LESKRFVHRD IAARNVLVSS
NDCVKLGDFG LSRYMEDSTY YKASKGKLPI KWMAPESINF RRFTSASDVW MFGVCMWEIL
MHGVKPFQGV KNNDVIGRIE NGERLPMPPN CPPTLYSLMT KCWAYDPSRR PRFTELKAQL
STILEEEKVQ QEERMRMESR RQVTVSWDSG GSDEAPPKPS RPGYPSPRSS EGFHPSPQHM
VQTNHYQVSG YPGSHGITAV AGSIYPGQAS LLDQTDSWNH RPQEISMWQP NVEDSATLDL
RGIGQVLPTH LMEERLIRQQ QEMEEDQRWL EKEERFLKPD VRLSRGSIDR EDGGPQGPTG
NQHIYQPVGK PDPAAPPKKP PRPGAPGHLS SLASLGSPGD NYNEGVKLQP QEISPPPTAN
LDRSNDRVYE NVTGLVRAVI EMSSKIQPAP PEEYVPMVKE VGLALRTLLA TVDETIPVLP
ASTHREIEMA QKLLNSDLGE LISKMKLAQQ YVMTSLQQEY KKRMLTAAHA LAVDAKNLLD
VIDQARMKAL GQARPR
//
