ID A0A2K5K7Q8_COLAP Unreviewed; 1018 AA.
AC A0A2K5K7Q8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000037130.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000037130.1}
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 AlphaFoldDB; A0A2K5K7Q8; -.
DR Ensembl; ENSCANT00000060380.1; ENSCANP00000037130.1; ENSCANG00000041792.1.
DR Proteomes; UP000233080; Unplaced.
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:0043066; P:negative regulation of apoptotic process; IEA:UniProt.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:UniProt.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0030155; P:regulation of cell adhesion; 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:0010033; P:response to organic substance; 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; 2.
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 Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
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:UP000233080};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 36..356
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 427..685
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 7..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1018 AA; 115575 MW; 61A133E4DBC303A9 CRC64;
IMAAAYLDPN LNHTPNSSTK THLGTGMERS PGAMERVLKV FHYFESNSEP TTWASIIRHG
DATDVRGIIQ KIVDSHKVKH VACYGFRLSH LRSEEVHWLH VDMGVSSVRE KYELAHPPEE
WKYELRIRYL PKGFLNQFTE DKPTLNFFYQ QVKSDYMLEI ADQVDQEIAL KLGCLEIRRS
YWEMRGNALE KKSNYEVLEK DVGLKRFFPK SLLDSVKAKT LRKLIQQTFR QFANLNREES
ILKFFEILSP VYRFDKECFK CALGSSWIIS VELAIGPEEG ISYLTDKGCN PTHLADFTQV
QTIQYSNSED KDRKGMLQLK IAGAPEPLTV TAPSLTIAEN MADLIDGYCR LVNGASQSFI
IRPQKGEVLF LSIPNYISTK YLVSCLTSFN VSVSFPAETD DYAEIIDEED TYTMPSTRDY
EIQRERIELG RCIGEGQFGD VHQGVYMSPE NPALAVAIKT CKNCTSDSVR EKFLQEALTM
RQFDHPHIVK LIGVITENPV WIIMELCTLG ELRSFLQVRK YSLDLASLIL YAYQLSTALA
YLESKRFVHR DIAARNVLVS SNDCVKLGDF GLSRYMEDST YYKASKGKLP IKWMAPESIN
FRRFTSASDV WMFGVCMWEI LMHGVKPFQG VKNNDVIGRI ENGERLPMPP NCPPTLYSLM
TKCWAYDPSR RPRFTELKAQ LSTILEEEKA QQEERMRMES RRQATVSWDS GGSDEAPPKP
SRPGYPSPRS SEGFYPSPQH MVQTNHYQVS GYPGSHGITA MAGSIYPGQT SLLDQTDSWN
HRPQEIAMWQ PNVEDSTALD LRGIGQVLPT HLMEERLIRQ QQEMEEDQRW LEKEERFLKP
DVRLSRGSID REDGSLQGPV NPAAPPKKPP RPGAPGHLGS LASLSSPADS YNEGVKLQPQ
EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP EEYVPMVKIE MAQKLLNSDL
GELINKMKLA QQYVMTSLQQ EYKKQMLTAA HALAVDAKNL LDVIDQARLK MLGQTRPH
//
