ID A0A0B2V5S5_TOXCA Unreviewed; 790 AA.
AC A0A0B2V5S5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Focal adhesion kinase 1 {ECO:0000313|EMBL:KHN76797.1};
GN Name=ptk2 {ECO:0000313|EMBL:KHN76797.1};
GN ORFNames=Tcan_14083 {ECO:0000313|EMBL:KHN76797.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN76797.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN76797.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN76797.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN76797.1}.
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DR EMBL; JPKZ01002430; KHN76797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V5S5; -.
DR STRING; 6265.A0A0B2V5S5; -.
DR OMA; RIQCEED; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
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:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
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: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; 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; 1.10.510.10; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46221; FERM AND PDZ DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR46221:SF11; 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; 2.
DR SMART; SM00295; B41; 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.
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:0000313|EMBL:KHN76797.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transferase {ECO:0000313|EMBL:KHN76797.1}.
FT DOMAIN 5..321
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 222..526
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 790 AA; 90011 MW; 707B0EFEF104A96B CRC64;
MNETDIIRVY IPNGSVKSVR YDFETKVQRV IHVVLASLGI DKVSYGHFAL RLVQFPTAHT
SNNDCYWLHG SFTMRHIYEK YFSTSASCSQ LRFELRLRFV PKDLQEMYQT QTDAFMFLHD
QVLADYLTQV SWRLPTETAM QLASLQLRKR LCALDKCFNL EELEAEGVLT RYLPETIVVN
TKPKALRKSL LAAVKRNAAL SPTECMFQFL NIVLKVSQFD VEIFRASLGT GWTTPIDIFV
GMRVGISYNT EIRCAPTPVT QLRNIVEISI RKLDETSEKA IVQLRLTGSN QPMSITVPNS
LIAESLAHLL DGYQMLLSQQ GSVWTPKELM CNTLTSEFIT QCDSLKHHLN RENESEESTF
LAKAFSLSSD LRIDRSRVSL EELLGDGQFG NVYRGTHLLE DGSSQAVAVK VCKIDSEPSE
MQNFLEEASS RGKLPIKWMA PESINYRRFN TATDIWMFGV CVWEILMCGI KPWQDVRNHD
VILKLEAEER LAKPENCPQV LYDFLRRMWA FDAKMRPTIG ETNRFLNHLL DQIDCGIPFN
ELRAPCKEEA DTELSDETVL NGNAKPLPIL KLDASTVPTS TLWRTLEQQR IQCEEDEKWL
EEEEEKLLPL PAIATTRTFE HLTSLSGSRP LLDDHGVLPQ GYEFDRTDDN VHRSVFKVVG
AVSNLSKSFV PSMDNAQFVA LVKVITNELK ELFHESSQCL ASLQPAEQRQ VQLVETLLGA
DMRNMAQSMR MALAENATEE DCEQARREVL KTAHQLAFNC KHFLESVDSA RLRSDVAKLK
RKDALLSQRV
//
