ID   FAK1_XENLA              Reviewed;        1068 AA.
AC   Q91738; Q91563;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Focal adhesion kinase 1;
DE            Short=FADK 1;
DE            EC=2.7.10.2;
DE   AltName: Full=Protein-tyrosine kinase 2;
DE   AltName: Full=pp125FAK;
GN   Name=ptk2; Synonyms=fak1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   PubMed=7642098; DOI=10.1016/0378-1119(95)00153-w;
RA   Zhang X., Wright C.V., Hanks S.K.;
RT   "Cloning of a Xenopus laevis cDNA encoding focal adhesion kinase (FAK) and
RT   expression during early development.";
RL   Gene 160:219-222(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Embryo;
RX   PubMed=7649362; DOI=10.1006/dbio.1995.1214;
RA   Hens M.D., DeSimone D.W.;
RT   "Molecular analysis and developmental expression of the focal adhesion
RT   kinase pp125FAK in Xenopus laevis.";
RL   Dev. Biol. 170:274-288(1995).
CC   -!- FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling
CC       pathways involved in cell motility, proliferation and apoptosis.
CC       Activated by tyrosine-phosphorylation in response to either integrin
CC       clustering induced by cell adhesion or antibody cross-linking, or via
CC       G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin
CC       or lysophosphatidic acid, or via LDL receptor occupancy. Microtubule-
CC       induced dephosphorylation at Tyr-397 is crucial for the induction of
CC       focal adhesion disassembly (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton,
CC       cilium basal body {ECO:0000250|UniProtKB:Q05397}. Note=Constituent of
CC       focal adhesions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q91738-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q91738-2; Sequence=VSP_004978, VSP_004979, VSP_004980;
CC   -!- DEVELOPMENTAL STAGE: Present in the fertilized egg and in cleavage and
CC       blastula stage embryos. During gastrulation, expression increases
CC       significantly and is detected in mesoderm, marginal zone ectoderm, and
CC       cells of the blastocoel roof. Later in development, prominently
CC       expressed at intersomitic junctions, in the brain and in several
CC       cranial nerves.
CC   -!- PTM: Phosphorylated on tyrosine residues; phosphorylated kinase is
CC       first detected during gastrulation, suggesting that tyrosine
CC       phosphorylation is developmentally regulated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. FAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; L33920; AAA99456.1; -; mRNA.
DR   EMBL; U11078; AAA80333.1; -; mRNA.
DR   PIR; I51670; I51670.
DR   PIR; JC4200; JC4200.
DR   RefSeq; NP_001084066.1; NM_001090597.1. [Q91738-1]
DR   AlphaFoldDB; Q91738; -.
DR   SMR; Q91738; -.
DR   GeneID; 399286; -.
DR   KEGG; xla:399286; -.
DR   AGR; Xenbase:XB-GENE-952029; -.
DR   CTD; 399286; -.
DR   Xenbase; XB-GENE-952029; ptk2.L.
DR   OrthoDB; 1614410at2759; -.
DR   BRENDA; 2.7.10.2; 6725.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 399286; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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-KW.
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: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; PS00661; FERM_2; 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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell junction; Cell membrane;
KW   Cell projection; Cytoplasm; Cytoskeleton; Developmental protein; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..1068
FT                   /note="Focal adhesion kinase 1"
FT                   /id="PRO_0000088080"
FT   DOMAIN          35..355
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          435..693
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        559
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         441..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         513..515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         403
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         413
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         589
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         590
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         874
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         941
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         393..398
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:7642098"
FT                   /id="VSP_004978"
FT   VAR_SEQ         418..425
FT                   /note="KSYGLDEA -> T (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:7642098"
FT                   /id="VSP_004979"
FT   VAR_SEQ         917..919
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:7642098"
FT                   /id="VSP_004980"
FT   CONFLICT        439
FT                   /note="R -> P (in Ref. 2; AAA99456)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1068 AA;  121156 MW;  EF5BEBD60D2C99DA CRC64;
     MAAAYLDPNL NHNPSTNAKS RLSTGMERSP GAIERVLRVF HYFESNNEPA TWSSNIRHGD
     ATDVRGIIQK IVDSHKVKNV ASYGLRLSHL HSEEVHWLHP DIGVSHIREK YEQSHPPEEW
     KYELRIRYLP KGFVNQFTED KPTLNFFYQQ VKNDYMSEIA DQVDQEIALK LGCLEIRRSY
     GEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
     LKFFEILSPV YRYDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGSNP THLADFTQVQ
     TIQYSSSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VSGASESFII
     RPQKEGERAL PSIPKLANNE KHGVRPHAVS VSDEFSGDET DDYAEIIDEE DTYTMPSKSY
     GLDEAGDYEI QRDRIELGRC IGEGQFGDVH QGVYMSPENP AMAVAIKTCK NCTSDSVREK
     FLQEALTMRQ FDHPHIVKLI GVITENPVWI IMELCTLGEL RSFLQVRKYS LDLASLILYS
     YQLSTALAYL ESKRFVHRDI AARNVLVSSS DCVKLGDFGL SRYMEDSTYY KASKGKLPIK
     WMAPESINFR RFTSASDVWM FGVCMWEILM YGVKPFQGVK NNDVIGRIEN GERLPMPPNC
     PPTLYSLMTK CWAYDPSRRP RFTELKAQLS TILEEEKLQQ EERMRMESRR QVTVSWDSGG
     SDEAPPKPSR PGYPSPRSSE GFFPSPQHMM QPNHYQVSGF SVAHGIPSMS GNMYPGQASV
     LDHMDSWNHR TPDINMWQPS MEDSGPMDMR SLAQVLPTHL MEERLIRQQQ EMEEDQRWLE
     KEERFLKPDV RLSRGSVDHV DGNIQCPAGN QHIYQPVGKP DHVAPPKKPP RPGAPSHLGN
     LPAHNSPVDG YNEGVKPWRI QPQEISPPPT ANLDRTNDKV YENVTGLVKA VIEMSSRIQP
     APPEEYVPMV KGVGLALRTL LATVDETIPV LPASTHREIE MAQKLLNSDL AELINKMKLA
     QQYVMTSLQQ EYKKQMLTAA HALAVDAKNL LDVIDQARLK IISHSRPH
//