ID A0A452EJE2_CAPHI Unreviewed; 1095 AA.
AC A0A452EJE2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
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|Ensembl:ENSCHIP00000012150.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000012150.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000012150.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000012150.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; LWLT01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017914111.1; XM_018058622.1.
DR AlphaFoldDB; A0A452EJE2; -.
DR STRING; 9925.ENSCHIP00000012150; -.
DR Ensembl; ENSCHIT00000019940.1; ENSCHIP00000012150.1; ENSCHIG00000013943.1.
DR GeneID; 102177814; -.
DR CTD; 5747; -.
DR GeneTree; ENSGT00940000155113; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000291000; Chromosome 14.
DR Bgee; ENSCHIG00000013943; Expressed in uterus and 18 other cell types or tissues.
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: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:0000256|ARBA:ARBA00023137};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 78..398
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 465..723
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 728..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1095 AA; 123750 MW; F7D126B7905854F2 CRC64;
MLLEVVGQGA LEPQALSMEK SGCSPFPVCW AKEYDRYLAS SKRMAAAYLD PNLNHTPSSS
TKTHLGTGVE RSPGTMERVL KVFHYFESNS EPTTWASIIR HGDATDVRGI IQKIVDSHKV
KHVACYGFRL SHLRSEEVHW LHLDMGVSNV REKYELAHPP EEWKYELRIR YLPKGFLNQF
TEDKPTLNFF YQQVKSDYML EIADQVDQDI ALKLGCLEIR RSYWEMRGNA LEKKSNYEVL
EKDVGLKRFF PRSLLDSVKA KTLRKLIQQT FRQFANLNRE ESILKFFEIL SPVYRFDKEC
FKCALGSSWI ISVELAIGPE EGISYLTDKG CNPTHLADFN QVQTIQYSNS EDKDRKGTLQ
LKIAGAPEPL TVTAPSLTIA ENMADLIDGY CRLVHGATQS FIIRPQKEGE RALPSIPKLA
NSEKQGVRTH AVSVSETDDY AEIIDEEDTY TMPSTRDYEI QRERIELGRC IGEGQFGDVH
QGTYTSPENP ALAVAIKTCK NCTSDSVREK FLQEALTMRQ FDHPHIVKLI GVITENPVWI
IMELCTLGEL RSFLQVRKYS LDLASLILYA YQLSTALAYL ESKRFVHRDI AARNVLVSSN
DCVKLGDFGL SRYMEDSTYY KASKGKLPIK WMAPESINFR RFTSASDVWM FGVCMWEILM
HGVKPFQGVK NNDVIGRIEN GERLPMPPNC PPTLYSLMTK CWAYDPSRRP RFTELKAQLS
TILEEEKVQQ EERMRMESRR QVTASWDSGG SDEAPPKPSR PGYPSPRSSE GFYPSPQHMV
QTNHYQVSGY PGPHGVTAMA GSIYPGQASL LDQTDSWNHR PQEISMWQPS VEDSAALDLR
GLGQALPTHL MEERLIRQQQ EMEEDQRWLE KEERFLKPDV RLSRGSIDRE DGGPQAPTGN
QHIYQPVGKP DPAAPPKKPP RPGAPGHLGS LASLGSPGDS YNEGVKLQPQ EISPPPTANL
DRSNDRVYEN VTGLVRAVIE MSSKIQPAPP EEYVPMVKEV GLALRTLLAT VDETIPVLPA
STHREIEMAQ KLLNSDLGEL INKMKLAQQY VMTSLQQEYK KQMLTAAHAL AVDAKNLLDV
IDQARLKALG QPRPH
//