FUR1C_DROME
ID FUR1C_DROME Reviewed; 1101 AA.
AC P30430; Q27235; Q9VBR5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Furin-like protease 1, isoform 1-CRR;
DE Short=Furin-1;
DE EC=3.4.21.75;
DE AltName: Full=Kex2-like endoprotease 1;
DE AltName: Full=dKLIP-1;
DE Flags: Precursor;
GN Name=Fur1; ORFNames=CG10772;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=1545235; DOI=10.1523/jneurosci.12-03-00705.1992;
RA Hayflick J.S., Wolfgang W.J., Forte M.A., Thomas G.;
RT "A unique Kex2-like endoprotease from Drosophila melanogaster is expressed
RT in the central nervous system during early embryogenesis.";
RL J. Neurosci. 12:705-717(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R, and Tuebingen; TISSUE=Embryo;
RX PubMed=8491178; DOI=10.1002/j.1460-2075.1993.tb05834.x;
RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T.,
RA Van de Ven W.J.M.;
RT "Generation of structural and functional diversity in furin-like proteins
RT in Drosophila melanogaster by alternative splicing of the DFur1 gene.";
RL EMBO J. 12:1853-1870(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., 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.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
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).
CC -!- FUNCTION: Furin is likely to represent the ubiquitous endoprotease
CC activity within constitutive secretory pathways and capable of cleavage
CC at the RX(K/R)R consensus motif. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of mature proteins from their proproteins by cleavage
CC of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and
CC Yaa is Arg or Lys. Releases albumin, complement component C3 and von
CC Willebrand factor from their respective precursors.; EC=3.4.21.75;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:8491178}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8491178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1-CRR; Synonyms=A;
CC IsoId=P30430-1; Sequence=Displayed;
CC Name=1; Synonyms=F;
CC IsoId=P26016-2; Sequence=External;
CC Name=1-X; Synonyms=E;
CC IsoId=P26016-1; Sequence=External;
CC Name=2; Synonyms=C, D, F;
CC IsoId=P26016-3; Sequence=External;
CC -!- TISSUE SPECIFICITY: In adults, isoform 1-CRR is expressed in CNS, fat
CC body, and female reproductive tissues, and in embryos, in anal pads,
CC hindgut, developing antennomaxillary complex, oenocytes, clipeolabrum,
CC pharynx, trachea, CNS and developing posterior spiracles.
CC {ECO:0000269|PubMed:8491178}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1-CRR is expressed in embryos, larvae,
CC pupae and adults. {ECO:0000269|PubMed:8491178}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; M81431; AAA28467.1; -; mRNA.
DR EMBL; L12370; AAA28545.1; -; Genomic_DNA.
DR EMBL; L12369; AAA28545.1; JOINED; Genomic_DNA.
DR EMBL; L12372; AAA28548.1; -; mRNA.
DR EMBL; AE014297; AAN14051.1; -; Genomic_DNA.
DR RefSeq; NP_733102.1; NM_170654.2. [P30430-1]
DR AlphaFoldDB; P30430; -.
DR SMR; P30430; -.
DR BioGRID; 70692; 5.
DR MEROPS; S08.048; -.
DR DNASU; 47220; -.
DR EnsemblMetazoa; FBtr0089982; FBpp0089025; FBgn0004509. [P30430-1]
DR GeneID; 47220; -.
DR CTD; 47220; -.
DR FlyBase; FBgn0004509; Fur1.
DR VEuPathDB; VectorBase:FBgn0004509; -.
DR BioGRID-ORCS; 47220; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Fur1; fly.
DR GenomeRNAi; 47220; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004509; Expressed in oviduct (Drosophila) and 46 other tissues.
DR ExpressionAtlas; P30430; baseline and differential.
DR Genevisible; P30430; DM.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0097688; P:glutamate receptor clustering; IMP:FlyBase.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR GO; GO:0001941; P:postsynaptic membrane organization; IMP:FlyBase.
DR GO; GO:0097090; P:presynaptic membrane organization; IMP:FlyBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR CDD; cd00064; FU; 1.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_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 Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 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 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..309
FT /evidence="ECO:0000255"
FT /id="PRO_0000027022"
FT CHAIN 310..1101
FT /note="Furin-like protease 1, isoform 1-CRR"
FT /id="PRO_0000027023"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 340..654
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 662..791
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
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 REGION 886..915
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 COMPBIAS 897..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 413
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 587
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 430..579
FT /evidence="ECO:0000250"
FT DISULFID 522..552
FT /evidence="ECO:0000250"
FT DISULFID 669..695
FT /evidence="ECO:0000250"
FT CONFLICT 1014
FT /note="T -> I (in Ref. 1; AAA28467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1101 AA; 120993 MW; 90DC38E2CACB71A0 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 QVGEVGMTRD
HSNTAACLKW SDRKCLECND SAYMFEDQCY DVCPVHTYPL DKFQAEEDEQ DDEVTRGPVN
PYSSSPMDHS LLMSNSLDDK QDPLQAEDRR RRSSLTQLVE VPSRVCAACD RSCLECYGAL
ASQCSTCSPG SQLRKILNET FCYAYVVRST GMASVVDISK MDDRDTQQYM TGTTVLLLVS
VIFTLMGVAV AGGIVYHRRA MARSNELYSR VSLVPGDESD SDEDELFTAH FPARKSGVNI
YRDEAPSEKI FEEDEISHLV P
