ID A0A182N274_9DIPT Unreviewed; 2795 AA.
AC A0A182N274;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Focal adhesion kinase 1 {ECO:0008006|Google:ProtNLM};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR001732-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR001732-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR001732-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 STRING; 7168.A0A182N274; -.
DR EnsemblMetazoa; ADIR001732-RA; ADIR001732-PA; ADIR001732.
DR VEuPathDB; VectorBase:ADIR001732; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000075884; 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:InterPro.
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: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 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; 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; 2.
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; 2.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273}.
FT DOMAIN 873..1277
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1393..1684
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 18..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2117..2136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2532..2573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2363..2378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2795 AA; 303541 MW; BCF73231E14422BD CRC64;
MNDRDTSGTV FSNRMALHHH HQHRNLSSSA TGEPQVVPRI TPPNPSAMGP SFGENDVKRS
APPDAEAGSG GGVVLRNRVI DLDKNRIKCN RNRIWSRPSS FLSFFKQSLG SSNGGTGGGV
ARSSNCGESV PDTAVVGASV TSSNGVPHST TDVIANGDPT LDGVDGKSAG GQRLDLNMIR
KLEEEIYKRG REQRPDAEAK DFHEFYFNNR RYSGGERKTF SNDTSAFNGD NHRAVLLVDP
HALEPILLKR PLSTDEARLT SDEAANDSGR GSLDHSGPTA AASLLHHQTA SGGGNQSIII
VDNSEYYPVL MRYDINADQI DRQQQQQQQY RRKRTEMLKI DTTTHPAAVS SSTGGVAVAP
IKRPSGTDRT TSPAATGGFP MKSDEKLSSF ASSQSSSLSG ATSSSVELPS PPALCEPPGF
EPTGVGLRHR PPLMVSVTQP TAITSTSAPT AESGGSGGRR GKKQLQQRTA NLFQRFLQHR
RSLNLSVRRK RGRPSHECAH FKNTEVAFGG RAHWADVILG SSGSSHSKSS GGGNKVKFEY
LKRMARYDCE AGAANVGHDR HALVRSSRSS VRRRATSEPD LVSRQNWKSD GFVQHLHRHH
RQTLYWSTGD LSGLGRMMEV GKNFENIFES TSDNLSARLS AVVMSSSSSS SVPLSGSGSL
SSSTTASSMG STSSQRILQR RLAAALLKST HYNHHSTGSS NSNNHSKPPL SSCSAGNSAS
SNSSTSLATQ TSGPVGGGNF LRKKSSSFRG VLRRSNTPDV VNTWVYRKSY DGSGNGLGEP
PYHRGHGSPH ASPSRYSYNN TAKSPLQHWR TSSAGASDFK RNSRLRSSAS AAVPGATGHH
QHHHHNMVDL NVPRGHSPHF SPSRQTTQTG DTQTLHVYLP NHGFRMIRFD EASDVRQIIN
LIVGWMSPGH KTNPQSYALR LRHMLTKEVL WMPPDTSMSQ VMAHIFNPSC SNADCPNVDK
STIAKRMQQK TSGAVGHANS VWKAELRVRY IPKNLKELYE RDRTTCHFYF DQIKQDYIQS
NVPNIDPEIA VQLCCLGIRH YYKDTNHTSN DRKQHLDYIE KEMGFGNFIP KSVIDTIKQK
NLKKQIQAGY KKVYSYNEME YMLKFFDLLR TQYTFDQEQF NVQLSSSWNI RVDLIIGPHV
GISYSVNPQA PPTKVTDFES IERITTSILP TSLTKSDHQG ISGRGARGKD QPDLTSSCGS
NSSTGDSDKG KKDGKKGSST GSSGSSSHCA CGDIKTQLRI RVSGNSEDLA ITCDGIKTSE
SIADLVDGYC RLFNNNDNSL WDRSVTPKGG AGTATPPTGG SATNSLEKSH LKKSLTESQT
SCTDRHGSRS SSADRLNGGN GDDLNNSSAG SSQLQQPPKP TLNEDYAELG MCDEEGDYST
PAARDYELDR SQITLNEIIG VGQFGDVHIG SCRLPNKSTL VSKLNQSLTS EFDEYSQMVM
DNGNADAQKT GIIQVAVKTC KPDADTTTSE KFLQEAYIMK KFEHPHIIKL IGISSGPPIW
IVMELARHGE LRAYLKKNGP KLKLGTLLLY SYQLSTALSY LESKKFVHRD IAARNVLVSS
PTCIKLADFG LSRWVEDQSY YTSTKGMLPI KWMAPESINF RRFTTASDVW MFGVCTWEIL
MLGIKPFQGV KNCDVIGKLE NGERLPLPPN CPPRLYSLMS QCWSLEPHKR PNFKSVKETL
YEILMEERHS DCETMRRENR RVAAMSWGAG DDMAPPKPAR GPTMGGEGPL VPGAPQTYIV
ARDPTVLAAL MRENEQRGIN PSSYTTPASV FNTLAVDLDP NAPPNNTDNQ VAKEIAVANL
PLKTVPLPVT ELHKLDPTID EAGAAHATAA AAGATADGGA TESMPPQQQQ QQQQPGGTPP
SGMASQYPQP AFVKSPQQED QPPGGAKSRS LERNVGQNIV SAYAARINSL ERTRQMSMEY
GNSVKAMRSN SLTRQYSGGN QSDLYPGVGH GVRSASLERG AQVGAGGYMT RMGSLERNQQ
QQPQPSSQSI FLNSIKGGSL ERNQSAAIVN DMMNSKIAYK GGSLERNQHI LLTRSGSAVG
SLERNMMPFQ NYRSPVAAAP KEQEPFQEEI YDFGGVNVKS CASIALKKSV EKGMLPPSSL
AVSPGISANT GANYALPPPY SSASKQQQAA ANQQQLQGTP QRAMWCGSNT SIHQQMYVQQ
QAPGVGGPPI IGIASSQQVQ IPMKISHSQP VQPVQQVQPI QQMATAVAQP VPVQQQQAQQ
FDPQQQPPPA QLQETQQLLE EKLRKQQQES EIDSKWLQQE ENNLKKRLSL ITANAASMSL
DQPSTGGPLQ EGGTPPINGG GSSLSGSYHS QQSPHFSPQN TMSGPQSLGD HYPTTPNTSD
SRPHTPNSGG NGGGGGAGAS SGGMIKSKSS SMERCTTPQS GDEKFAVKKV EPTKTMPLDR
TNDMVYNATT SVVKSIMALS QGVDRAQAPE YLNLVRNVGF ELRALLGAVD QLSANFPPQR
YKEVEMAHKV LSKDMYELVT AMRLAQQYSE TTLDAEYRKS MLSAAHVLAM DAKNLLDVVD
SIRVRYTSLF MQQPSDPSSP TQRQHQTPSA AVQHPSNMPQ TFSQQQQQQQ HSFDQSQLLM
MGECYQNLQP KQTMLPHSSP PTSLTHSYET STTGMALGAT AAPSSYQQSG IYDNECIISS
QQQPGEGGKL KKPVIAAKPP SVVAMASVKL KPVASVPLDV PGGADGCGGS GGDMYTNAVL
STSPNGSSAD IKLPDPVSCT IVQENLLAAN NQKVMATTNK LIPDDSDSHE NKATKNLITY
VKQFISLEQQ MMTDGKLNFA GINLTEPIPT HHEHK
//
