ID A0A026W508_OOCBI Unreviewed; 1712 AA.
AC A0A026W508;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Focal adhesion kinase {ECO:0000313|EMBL:EZA51098.1};
GN ORFNames=X777_10386 {ECO:0000313|EMBL:EZA51098.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA51098.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA51098.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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}. 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 EMBL; KK107419; EZA51098.1; -; Genomic_DNA.
DR STRING; 2015173.A0A026W508; -.
DR OMA; CEWRYEL; -.
DR Proteomes; UP000053097; 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:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
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: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; 1.10.510.10; 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: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; 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:0000313|EMBL:EZA51098.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transferase {ECO:0000313|EMBL:EZA51098.1}.
FT DOMAIN 4..322
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 384..642
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1712 AA; 188000 MW; 3750A5EE8D344A8B CRC64;
MDKATLKVHL PNGGFNVVKF GDAIDVRGII SLVTSRLAVG TRHYRNLYAM RLHHPGSGES
YWLHQDTTMY QVQEKYERKH PHCEWRYELR VRYLPQNLND LYEKDKVTFY YYYDQVRNDY
LLANHAALDQ DVAVQLCCLE IRYFFKDMPQ IALDKKSNLE YLEREVGLHK FLPRSVLNGM
KPKALRKLIQ QHFKKVAALS ELECMFKFFD LLRAHYRFDQ ERFICALGSS WSIPVELVIG
PDLGISYMAH RGGTVPTRMA EFSQIQSIQT LVSDCKEHAK ACIKLRVAGA AETLSITCSS
LDQAESLADL IDGYCRLVTG SNTSLWNRKD AQPPKSRQDG TSSPEKSAGK TGTILSEDYA
EIVDEEGDYS TPATRDYEIV RNQVELGEII GEGQFGNVHK GSYKGRDGQT VAVAVKTCKV
DADLATAEKF LEEAYIMQQF EHPHIIRLIG VCSEAPIWLV MELARLGEMR AYLQSNKHRL
DLATLLLYTF QLSTALSYLE SKKFVHRDIA ARNVLVSSHG CVKLADFGLS RWVEDQSYYT
ASKCKLPIKW MAPESINFRR FTTSSDVWMF GVCMWEILML GVKPFQGVKN NEVIRKLENG
ERLALPNHCP PRLYSLMSQC WSYEPSKRPT FKEIRETLHE ILLEEKHQQQ ETMRRENRRV
QAMSWGADDV PPPKPSRQPQ NTTEQSQLNV SAAPVSTYIV AQSPEVLAQL LKDNQARGVC
PSVYTTPASP FNTLAVQFQD EDQILTTALV PDLPFFDPAL SEPPSITTHD TTQSGGDSTL
SDTNLDSLDS SDNTPLMSSL SISDTAVQTQ SPAANRKQQK VKEMQNLYAV SSKVVGSITG
DLYSPVQKFS ASSAVSLPPA TASVAVAGNT CGEIYGPVAS FTQSSAIVGN LSQSASVGGN
YGENPGNFGP SSLGSSIIMP NCSQAQFATS GPHAQSQPIN YGNFVVSNNT SQVFGGGQST
SQNASSVQSA SGSNGGGGGG GVIYPRNISS ANMISSASSA ECLYGPVLKF RAQNAQLQPA
TAELKPAGTT AGNYGQAGRT NLIAQNLKSQ SLYPQNYPHQ QIYSNIAQPG QQAMYLPQMQ
NVARQNAIPQ AVSYAAIQHT NQQSQLSGAN PIYTAHATSV SVVQAQKVHV PNYTQQAQPG
ISSQPATSQI IGMNQSVGVG ITQASVPSHF IMSSSAIQQN IHPIPSSYMV EQPSSLGPID
HAQCSMHASV DGMMTSTVGA HQQQVTQPQM ASIIAKAVNV PQMATGIAKI TTFVTQKQDE
QLTSSTDGTL SGSLISSAVS DSTMSSSSSM TEEAQQDQRN MHSQLFDNMT DNLNTGIDDE
QKLLEQRLLE QQRQSEEDSR WLAREEKRLS IATSGDESAS PPVPRSVTQS PSHEPHSANT
GSLGSDKGSD KVIVVKKMEP TPTADLDRTN DKVYDCTTSV VRAVMSLSQG VQQSKADQYL
ELVRRVGIEL KALLSSVDIL VEILPISAHR EVEMAHKVLS KDMAELVAAM KLAQNYSATT
LDAEYRKGML SAAHILAMNA KNLLDVIDSI RIRYPYVDSQ ICQKQCDVVN RTRESTPENR
IRSSQSGEQF LRRSQSSERQ GTTFRQSQSG DLLHRMGQSV DRSSPGSQSD VNSSSSLERK
HNMVTNSLER NSTTRRQMAT NSLERKRPSL TCNAGPMNNS VNLPPMVPVS CNLVQTASPV
IHPSQSVTTG VNQQAVFTAN SKTANETPIN DS
//
