ID B4PB85_DROYA Unreviewed; 1200 AA.
AC B4PB85;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDW91498.1};
DE EC=2.7.10.- {ECO:0000313|EMBL:EDW91498.1, ECO:0000313|EMBL:KRJ99875.1};
DE SubName: Full=Uncharacterized protein, isoform D {ECO:0000313|EMBL:KRJ99875.1};
GN Name=Dyak\GE13847 {ECO:0000313|EMBL:EDW91498.1};
GN ORFNames=Dyak_GE13847 {ECO:0000313|EMBL:EDW91498.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW91498.1, ECO:0000313|Proteomes:UP000002282};
RN [1] {ECO:0000313|EMBL:EDW91498.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW91498.1};
RG The Drosophila yakuba Sequencing Consortium;
RT "The Genome of Drosophila yakuba.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDW91498.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW91498.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3] {ECO:0000313|EMBL:EDW91498.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW91498.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
RN [4] {ECO:0000313|EMBL:EDW91498.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW91498.1};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; CM000158; EDW91498.1; -; Genomic_DNA.
DR EMBL; CM000158; KRJ99875.1; -; Genomic_DNA.
DR RefSeq; XP_002091786.1; XM_002091750.2.
DR RefSeq; XP_015052769.1; XM_015197283.1.
DR AlphaFoldDB; B4PB85; -.
DR SMR; B4PB85; -.
DR EnsemblMetazoa; FBtr0260365; FBpp0258857; FBgn0231493.
DR EnsemblMetazoa; FBtr0402255; FBpp0361115; FBgn0231493.
DR GeneID; 6530945; -.
DR eggNOG; KOG4257; Eukaryota.
DR HOGENOM; CLU_002646_0_1_1; -.
DR OMA; IWQRETI; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000002282; Chromosome 2R.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
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:InterPro.
DR GO; GO:0016020; C: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 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; 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; 1.
DR Pfam; PF00373; FERM_M; 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; 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};
KW Transferase {ECO:0000313|EMBL:EDW91498.1}.
FT DOMAIN 22..386
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 457..740
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 400..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 133928 MW; CF2AF44AA8295C17 CRC64;
MNTAGATSQP PPTKNETHSE EYLIHVHMPN KSFKAVRFNV KETVFHVIRR TVEDLGTDGR
TPSIQRYACR MLNMITKEVI WLARSTSMQK VLSHILTPGC SNVDCPNNQA ELDEVLLEHG
RRITDNRVWR VELRVRYVPN NIQELFEEDK ATCFYYFNQV KEDFIQANVT SIDTEVAVQL
CCLGIRHYFK NITVKAPDKK QHIDYIEKEI GFKSFLPQSV IATSKPKNLK KLIQVGYKKV
YNYNDIEYLT RFFDLLKNIY LTNFEQFAVT LSSAWNISGI LHVGPHIGIS YQTHPQASLT
NVAQFKDVVS IKTCTLPKEK LSKSGENTTE PELQNFNCNC QKIKTQIKIS ASNNVEDLVI
TCNGINTAES IADLIDGYCR LLSKDLEFTI WHRETTASNE DSAKALPNDA TLGSNKSTSS
QGKPMLTDDY AEIGLLEGEG DYSTPTVRNY ELDRALITPS AKIGVGQFGD VYVGTYTLPK
LGKGKNAAGN GKNSNSDQRN ADARPDVIQV AIKTCKANDD PEKTENFLAE AYIMQKFDHP
HIIRLIGICS VMPIWIVMEL AKLGELRAYL KTNSERLSHG TLLKYCYQLS TALSYLESKK
FVHRDIAARN VLVSSPTCVK LADFGLSRWV SDQSYYHSTP TVALPIKWMS PESINFRRFT
TASDVWMFGV CIWEILMLGV KPFQGVKNSD VILKLENGER LPLPPNCPPR LYSLMSQCWA
YEPLKRPNFK RIKETLHEIL IEDSINSSET LKREQRKVAS MSWIGSDDID IPPSKPSRVI
HDPDITGLMP ETTGLPQTYI IAQNPAVLAK LMMENQKRGI NPAAYTTPAS GIHNVLGEKL
RQQQKDSNSD SEWLIQEELL RQRSCSIPQG SINDHQAQIF KLDFMSAGPS SLPDCSNSSS
RPMTPNANLS SLKSNHSSAD HLSSLTAAEE QMGPNARNLG SAVSSRPLNR ADDEVYCATT
LVVKSIMALS QGVEKANTEG YLELVKNVGV KLRNLLTSVD KISVIFPAQA LKEVQMAHQV
LSKDMHELVS AMRLAQQYSD TTLDCEYRKS MLSAAHVLAM DAKNLFDVVD SIRQRYQHLF
PPSATKETNC SSSFESTSGS IVTEPVNDLG GYIKTSTSGD LLQNTGIYDN DLHHSFNSQL
QLQNPKASID LSGGGSLQRG MSLGLDTTRS TNEPLRIVEE TLGSPGEHMY CNTSALHGHA
//