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Database: UniProt
Entry: A0A3Q2I072_HORSE
LinkDB: A0A3Q2I072_HORSE
Original site: A0A3Q2I072_HORSE 
ID   A0A3Q2I072_HORSE        Unreviewed;      1106 AA.
AC   A0A3Q2I072;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 26.
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:ENSECAP00000041146.3,
GN   ECO:0000313|VGNC:VGNC:22002};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000041146.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000041146.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000041146.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000041146.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000041146.3};
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   RefSeq; XP_005613368.1; XM_005613311.2.
DR   AlphaFoldDB; A0A3Q2I072; -.
DR   Ensembl; ENSECAT00000062879.3; ENSECAP00000041146.3; ENSECAG00000014150.4.
DR   VGNC; VGNC:22002; PTK2.
DR   GeneTree; ENSGT00940000155113; -.
DR   Proteomes; UP000002281; Chromosome 9.
DR   Bgee; ENSECAG00000014150; Expressed in spinal cord and 23 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q2I072; baseline.
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:UP000002281};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          79..399
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          473..731
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          736..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..931
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         505
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1106 AA;  125305 MW;  13E741A27EDB7AE3 CRC64;
     MLLELAGREA LRPAAAICME KSGCSPFPMC WAKEYDRYLA SSKIMAAAYL DPNLNHTPNS
     STKTHLGTGV ERSPGAMERV LKVFHYFESN SEPTTWASII RHGDATDVRG IIQKIVDSHK
     VKHVACYGFR LSHLRSEEVH WLHLDMGVSN VREKYELAHP PEEWKYELRI RYLPKGFLNQ
     FTEDKPTLNF FYQQVKSDYM LEIADQVDQD IALKLGCLEI RRSYWEMRGN ALEKKSNYEV
     LEKDVGLKRF FPRSLLDSVK AKTLRKLIQQ TFRQFANLNR EESILKFFEI LSPVYRFDKE
     CFKCALGSSW IISVELAIGP EEGISYLTDK GCNPTHLADF NQVQTIQYSN SEDKDRKGML
     QLKIAGAPEP LTVTAPSLTI AENMADLIDG YCRLVNGATQ SFIIRPQKEG ERALPSIPKL
     ANSERQGVRT HAVSVSETDD YAEIIDEEDT YTMPSKSYGI DEARDYEIQR ERIELGRCIG
     EGQFGDVHQG VYLSPENPAL AVAIKTCKNC TSDSVREKFL QEALTMRQFD HPHIVKLIGV
     ITENPVWIIM ELCTLGELRS FLQVRKYNLD LASLILYAYQ LSTALAYLES KRFVHRDIAA
     RNVLVSSNDC VKLGDFGLSR YMEDSTYYKA SKGKLPIKWM APESINFRRF TSASDVWMFG
     VCMWEILMHG VKPFQGVKNN DVIGRIENGE RLPMPPNCPP TLYSLMTKCW AYDPSRRPRF
     TELKAQLSTI LEEEKVQQEE RMRMESRRQV TVSWDSGGSD EAPPKPSRPG YPSPRSSEGF
     YPSPQHMVQT NHYQVSGYPG SHGVTAVAGS IYPAQASLLD QTDSWNHRPQ EISMWQPNVE
     DSAALDLRGI GQVLPAHLME ERLIRQQQEM EEDQRWLEKE ERFLKPDVRL SRGSIDREDG
     SLQGPTGNQH IYQPVGKPDP AAPPKKPPRP GAPGHLGSLA SLSSPGDSYN EGVKPWRLQP
     QEISPPPTAN LDRSNDRVYE NVTGLVKAVI EMSSKIQPAP PEEYVPMVKE VGLALRTLLA
     TVDETIPVLP ASTHREIEMA QKLLNSDLGE LINKMKLAQQ YVMTSLQQEY KKQMLTAAHA
     LAVDAKNLLD VIDQARLRML GQTRPH
//
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