ID A0A0B4KI15_DROME Unreviewed; 864 AA. AC A0A0B4KI15; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 24-JUL-2024, entry version 63. DE SubName: Full=Furin 1, isoform H {ECO:0000313|EMBL:AGB96333.1}; DE EC=3.4.21.- {ECO:0000313|EMBL:AGB96333.1}; GN Name=Fur1 {ECO:0000313|EMBL:AGB96333.1, GN ECO:0000313|FlyBase:FBgn0004509}; GN Synonyms=Dfur1 {ECO:0000313|EMBL:AGB96333.1}, dFur1 GN {ECO:0000313|EMBL:AGB96333.1}, dFurin 1 {ECO:0000313|EMBL:AGB96333.1}, GN Dfurin1 {ECO:0000313|EMBL:AGB96333.1}, dKLIP-1 GN {ECO:0000313|EMBL:AGB96333.1}, Dmel\CG10772 GN {ECO:0000313|EMBL:AGB96333.1}, fur-1 {ECO:0000313|EMBL:AGB96333.1}, GN fur1 {ECO:0000313|EMBL:AGB96333.1}, fur[1] GN {ECO:0000313|EMBL:AGB96333.1}, Furin {ECO:0000313|EMBL:AGB96333.1}, GN furin {ECO:0000313|EMBL:AGB96333.1}, Furl GN {ECO:0000313|EMBL:AGB96333.1}, Klip1 {ECO:0000313|EMBL:AGB96333.1}, GN l(3)rL205 {ECO:0000313|EMBL:AGB96333.1}; GN ORFNames=CG10772 {ECO:0000313|EMBL:AGB96333.1, GN ECO:0000313|FlyBase:FBgn0004509}, Dmel_CG10772 GN {ECO:0000313|EMBL:AGB96333.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AGB96333.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily. CC {ECO:0000256|ARBA:ARBA00005325}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014297; AGB96333.1; -; Genomic_DNA. DR RefSeq; NP_001262953.1; NM_001276024.1. DR AlphaFoldDB; A0A0B4KI15; -. DR SMR; A0A0B4KI15; -. DR MEROPS; S08.048; -. DR DNASU; 47220; -. DR EnsemblMetazoa; FBtr0336804; FBpp0307775; FBgn0004509. DR GeneID; 47220; -. DR AGR; FB:FBgn0004509; -. DR CTD; 47220; -. DR FlyBase; FBgn0004509; Fur1. DR VEuPathDB; VectorBase:FBgn0004509; -. DR OrthoDB; 5474719at2759; -. DR BioGRID-ORCS; 47220; 0 hits in 3 CRISPR screens. DR ChiTaRS; Fur1; fly. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0004509; Expressed in oviduct (Drosophila) and 46 other cell types or tissues. DR ExpressionAtlas; A0A0B4KI15; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR034182; Kexin/furin. DR InterPro; IPR002884; P_dom. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf. DR InterPro; IPR023827; Peptidase_S8_Asp-AS. DR InterPro; IPR022398; Peptidase_S8_His-AS. DR InterPro; IPR023828; Peptidase_S8_Ser-AS. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR InterPro; IPR032815; S8_pro-domain. DR InterPro; IPR038466; S8_pro-domain_sf. DR PANTHER; PTHR42884:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_2; 1. DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1. DR Pfam; PF01483; P_proprotein; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR Pfam; PF16470; S8_pro-domain; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1. DR SUPFAM; SSF52743; Subtilisin-like; 1. DR PROSITE; PS51829; P_HOMO_B; 1. DR PROSITE; PS51892; SUBTILASE; 1. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. PE 3: Inferred from homology; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118..141 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 662..791 FT /note="P/Homo B" FT /evidence="ECO:0000259|PROSITE:PS51829" FT REGION 1..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 150..187 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..26 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 40..57 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..181 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 372 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 413 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 587 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" SQ SEQUENCE 864 AA; 94493 MW; 4596A2CF11559C64 CRC64; MKNDVVRWSR QPTSNTTNSS SSSRSDSNST HKHRSKSNKL NARQLGSNAA RSCQQRSSVA TTLEDEQQTI IECDIGNFNF DCNLFKTSFL TQHKQKRSGK SSSKSKSNRS RPLAKTKAVF LLALQFSAVV FLCNINVGFV AGSVATAASS AGGSSPAAPS SAPSSPPTVA VPPPPPPSSA LKVDPNGQSP VLPPYVLDYE TGGKAKLTPN NGKFGQSGSS GSNNNHIVGH YTHTWAVHIP NGDNGMADAV AKDHGFVNLG KIFDDHYHFA HHKVSKRSLS PATHHQTRLD DDDRVHWAKQ QRAKSRSKRD FIRMRPSRTS SRAMSMVDAM SFNDSKWPQM WYLNRGGGLD MNVIPAWKMG ITGKGVVVTI LDDGLESDHP DIQDNYDPKA SYDVNSHDDD PMPHYDMTDS NRHGTRCAGE VAATANNSFC AVGIAYGASV GGVRMLDGDV TDAVEARSLS LNPQHIDIYS ASWGPDDDGK TVDGPGELAS RAFIEGTTKG RGGKGSIFIW ASGNGGREQD NCNCDGYTNS IWTLSISSAT EEGHVPWYSE KCSSTLATTY SSGGQGEKQV VTTDLHHSCT VSHTGTSASA PLAAGIAALV LQSNQNLTWR DLQHIVVRTA KPANLKDPSW SRNGVGRRVS HSFGYGLMDA AEMVRVARNW KAVPEQQRCE INAPHVDKVI PPRTHITLQL TVNHCRSVNY LEHVQAKITL TSQRRGDIQL FLRSPANTSV TLLTPRIHDN SRSGFNQWPF MSVHTWGESP QGNWQLEIHN EGRYMAQITQ WDMIFYGTET PAQPDDVANP SQSNQFNLYG NDMAHNDVEY DSTGQWRNMQ QCLVDALSGS EEIGSEHNPY QNRGIMLRAC MWLA //