FAK1_XENLA
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 03-AUG-2022, entry version 150.
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 PRIDE; Q91738; -.
DR GeneID; 399286; -.
DR KEGG; xla:399286; -.
DR CTD; 399286; -.
DR Xenbase; XB-GENE-952029; ptk2.L.
DR OrthoDB; 43729at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 399286; Expressed in egg cell and 19 other 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: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 Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR041390; FADK_N.
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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF68993; SSF68993; 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
