ID G3WC11_SARHA Unreviewed; 1147 AA.
AC G3WC11;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 82.
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:ENSSHAP00000012966.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000012966.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000012966.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000012966.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; G3WC11; -.
DR STRING; 9305.ENSSHAP00000012966; -.
DR Ensembl; ENSSHAT00000013072.2; ENSSHAP00000012966.2; ENSSHAG00000011092.2.
DR eggNOG; KOG4257; Eukaryota.
DR GeneTree; ENSGT00940000155113; -.
DR HOGENOM; CLU_002646_0_0_1; -.
DR InParanoid; G3WC11; -.
DR TreeFam; TF315363; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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:UP000007648};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 114..434
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 514..772
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 778..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1147 AA; 130526 MW; 206EDFED5CCF2E64 CRC64;
MPREPPAGSG LESEAWEPLT RASGREGFDE LLWNRIKETR RFFNISFLFD HSDPVVTCFY
ISRLYFLKEY DRYLASSKTM AAAYLDPNLN HTPSSSTKTH LSTGMERSPG AMERVLKVFH
YFENSSEPTT WASIIRHGDA TDVRGIIQKI VDSHKVKHVA CYGFRLSHLR SEEVHWLHLD
MGVSNVREKY ELAHPPEEWK YELRIRYLPK GFLNQFTEDK PTLNFFYQQV KNDYMLEIAD
QVDQEIALKL GCLEIRRSYW EMRGNALEKK SNYEVLEKDV GLKRFFPKSL LESVKAKTLR
KLIQQTFRQF ANLNREESIL KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS
YLTDKGSNPT HLADFNQVQT IQYSNSDDKD RKGMLQLKIA GAPEPLTVTA PSLTIAENMA
DLIDGYCRLV NGATQSFIIR PQKEGERALP SIPKLANNEK QGVRTHTVSV SDEISGDETD
DYAEIIDEED TYTMPSKSYG IDEARDYEIQ RERIELGRCI GEGQFGDVHQ GVYMSPENPA
MAVAIKTCKN CTSDSVREKF LQEALTMRQF DHPHIVKLIG VITENPVWII MELCTLGELR
SFLQVRKYSL DLASLILYAY QLSTALAYLE SKRFVHRDIA ARNVLVSSTD CVKLGDFGLS
RYMEDSTYYK ASKGKLPIKW MAPESINFRR FTSASDVWMF GVCMWEILMH GVKPFQGVKN
NDVIGRIENG ERLPMPPNCP PTLYSLMTKC WAYDPSRRPR FTELKAQLST ILEEEKLQQE
ERMRMESRRQ VTVSWDSGGS DEAPPKPSRP GYPSPRSSEG FYPSPQHMVQ ANHYQVSGYT
GSHGITAMAG SIYPGQASLL DQTESWNHRP QEVSMWQPNM EDSASLDMRG LGQVLPAHLM
EERLIRQQQE MEEDQRWLEK EERFLKPDVR LSRGSIDRED GSLQGPTGNQ HIYQPVGKPD
PAAPPKKPPR PGAPSHLGSL ASLNSPVDSY NEGVKPWRLQ PQEISPPPTA NLDRSNDKVY
ENVTGLVKAV IEMSSKIQPA PPEEYVPMVK EVGLALRTLL ATVDETIPLL PASTHREIEM
AQKLLNSDLG ELINKMKLAQ QYVMTSLQQE YKKQMLTAAH ALAVDAKNLL DVIDQARLKM
LGQARPH
//
