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Database: UniProt
Entry: A0A452EJE2_CAPHI
LinkDB: A0A452EJE2_CAPHI
Original site: A0A452EJE2_CAPHI 
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
//
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