LINT_DROME
ID LINT_DROME Reviewed; 1693 AA.
AC B7YZU2; A0A0B4LFV3; A1Z7M1; Q8SY35;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Serine protease filzig {ECO:0000312|FlyBase:FBgn0286782};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE AltName: Full=Lumens interrupted {ECO:0000303|PubMed:29309404};
GN Name=flz {ECO:0000312|FlyBase:FBgn0286782};
GN Synonyms=lint {ECO:0000303|PubMed:29309404};
GN ORFNames=CG8213 {ECO:0000312|FlyBase:FBgn0286782};
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:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|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.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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|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 [3] {ECO:0000312|EMBL:AAL68238.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL68238.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL68238.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29309404; DOI=10.1371/journal.pgen.1007146;
RA Rosa J.B., Metzstein M.M., Ghabrial A.S.;
RT "An Ichor-dependent apical extracellular matrix regulates seamless tube
RT shape and integrity.";
RL PLoS Genet. 14:E1007146-E1007146(2018).
CC -!- FUNCTION: Probable endopeptidase. In tracheal terminal cells, acts
CC downstream of ich to regulate seamless tube growth and/or maintenance
CC probably by processing lumenal matrix proteins.
CC {ECO:0000305|PubMed:29309404}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:29309404};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C {ECO:0000312|FlyBase:FBgn0286782};
CC IsoId=B7YZU2-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0286782};
CC IsoId=B7YZU2-2; Sequence=VSP_059688;
CC Name=D {ECO:0000312|FlyBase:FBgn0286782};
CC IsoId=B7YZU2-3; Sequence=VSP_059689, VSP_059690;
CC -!- DEVELOPMENTAL STAGE: Detected in embryo at stage 13 in the posterior
CC spiracles and foregut primordium. By stage 15, expressed specifically
CC in epithelia secreting cuticle, including the trachea, foregut, hindgut
CC and epidermis. {ECO:0000269|PubMed:29309404}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. RNAi-mediated knockdown in
CC tracheal terminal cells results in cystic dilations and discontinuities
CC of the apical membrane; terminal cells are severely pruned with
CC terminal branches largely devoid of lumenal membrane, except for
CC isolated inclusions. {ECO:0000269|PubMed:29309404}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AE013599; AAF59009.4; -; Genomic_DNA.
DR EMBL; AE013599; ACL83076.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56019.1; -; Genomic_DNA.
DR EMBL; AY075422; AAL68238.1; -; mRNA.
DR RefSeq; NP_001137622.1; NM_001144150.2. [B7YZU2-1]
DR RefSeq; NP_001286221.1; NM_001299292.1. [B7YZU2-3]
DR RefSeq; NP_610435.4; NM_136591.5. [B7YZU2-2]
DR AlphaFoldDB; B7YZU2; -.
DR SMR; B7YZU2; -.
DR IntAct; B7YZU2; 14.
DR STRING; 7227.FBpp0271893; -.
DR MEROPS; S01.B34; -.
DR GlyGen; B7YZU2; 4 sites.
DR PaxDb; B7YZU2; -.
DR DNASU; 35902; -.
DR EnsemblMetazoa; FBtr0273384; FBpp0271892; FBgn0286782. [B7YZU2-2]
DR EnsemblMetazoa; FBtr0273385; FBpp0271893; FBgn0286782. [B7YZU2-1]
DR EnsemblMetazoa; FBtr0339307; FBpp0308413; FBgn0286782. [B7YZU2-3]
DR GeneID; 35902; -.
DR KEGG; dme:Dmel_CG8213; -.
DR UCSC; CG8213-RB; d. melanogaster.
DR CTD; 35902; -.
DR FlyBase; FBgn0286782; flz.
DR VEuPathDB; VectorBase:FBgn0286782; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000164686; -.
DR HOGENOM; CLU_252530_0_0_1; -.
DR InParanoid; B7YZU2; -.
DR OMA; DAQNAYF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; B7YZU2; -.
DR BioGRID-ORCS; 35902; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35902; -.
DR PRO; PR:B7YZU2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0286782; Expressed in embryonic/larval epidermis (Drosophila) and 10 other tissues.
DR ExpressionAtlas; B7YZU2; baseline.
DR Genevisible; B7YZU2; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098595; C:perivitelline space; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IEP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR GO; GO:0060439; P:trachea morphogenesis; IMP:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Serine protease;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1693
FT /note="Serine protease filzig"
FT /evidence="ECO:0000255"
FT /id="PRO_0000445007"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..68
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..1693
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 1449..1691
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 170..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1495
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 1544
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 1642
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 1480..1496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 1608..1627
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 1638..1667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1418..1437
FT /note="HSTSRTLPTPNLAFHSPSTE -> Q (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_059688"
FT VAR_SEQ 1418..1430
FT /note="HSTSRTLPTPNLA -> PRRKHKRRNQKTT (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_059689"
FT VAR_SEQ 1431..1693
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_059690"
SQ SEQUENCE 1693 AA; 182674 MW; 738D3F1109D38688 CRC64;
MFKWVTPAST ATLSRCTLPA TTAATTTTTA MAATRTATTT TRTTRPQLLS IALTSLIIIV
ASFVPTTSGF RSIETNGGGR KLFGGYRITP KHCRATKTLP SSDPRANGPT ICMFNHECAQ
RGGEVVGACM DGFLFGACCQ IPPTHELAST LINEAQNAYF QQHQQQTKLQ QSAAQSSFES
YGEQQQSLSE EQVAQQPSQN IYDQQNLDKV YQQLDSSSSI SPPNGAYGDE PQQQEYQSES
EQPVRDENAY PTSSSSTEAT QSQSSSASVE FEQEPSQPAD ASNDQTTQKI NKQPVQPPNF
HVHKHSVTIN SPSSPPQNDD FVMQVLSTLP PEHADDHHIV FTTEVPTKIT SGLQDQTSSE
SNSFEEVSST PAATQKPKPK PTQMPTQKTT QKATQKPTPK PTQKAKPKPV PQLAESMKRP
IQQKPQQVAK PKPSPKPAQS TNNHHHNHLI LDGGEFTHSD ITHPGADADL VEDLQFSTGY
GPQPVYAEPP KQQQQQQPAE QSYISSSTSA KRPTTGHNSP TTVSSITTHV DSIESIILQL
NNTSHGPSYN VVSQQTPSYG YPGAAVVQTE PAAQNPTFYQ ENESEKVQES DSQSDYGYTT
TVNYESFYDK VSDEQDASAA VSQSAEMPTA RPGYGEDVSA VLEDHTMPAN GYHDAEAPVA
PQTSEFNKMP VMGIAYPVDM SYMEEEGNLP ATAAGYGQMS SDSYEASTES TYQKLSTVQT
EEPQPTYVRP TTNANKQNRP VASYIGMVTM QHYNPQPGNG DYQAQVPPEV SVSSHTTKVQ
EQMDETSNGY QQSETTSGYV SPPTAVPAPA QRPQYDAVQG DASSERPVLV TASPRPRPKP
STKRPAVKRP ISGESTKKKP QPQPSAGAYN QEKISEHSTR KPVSNGYDKV PESPITHIQI
KKPSATQHKE QEQTGYPRPA SPAGYEQTTA AAPAPAAPSL NYDKPDAPPS QYDQPSAPSA
SYDQLAPMPS LNYNEQHASS PGRKPSTAKP ISTSYVTGPS TPRPPATVDY HYDNVPPLFM
ADDKLDAFIQ STAENIVGST PGNYQPPLVA TASTPAYAHR PTSSGSYGHK KPGFVQINGT
PKPPRPTVLI TPKPTAINLV TYSSLSDDSN KLASSTSSYV TGRPGVQGVS SNDFKDPGYF
GSSPVHVAFT QSTTEAVYAV PSDDKPAFPG YFGPTPSYPA FSVPGEKVGQ NVMEETYTSP
NDFVNFPPVR NPNLNMSAAS SAVTSDLDLS TPAFVEDVVL KDKMHTLVHK LVASLQGNFE
ALADMIEEPG SNKTVATYQA GAGGTAKPVR VVTTRKPVRT ATTTRPKVTT KKPVTRVTTK
APNKKTSAVS TTTRKPATRR TTVAAKVTTT TRRPATKKPT RRVSSTVKTT TVSSARPADD
EIVDEEDEED VNPNPSDNEI DQGATLSSYG GANGRKIHST SRTLPTPNLA FHSPSTECGV
RPHVKSGRIV GGKGSTFGAY PWQVLVREST WLGLFTKNKC GGVLITSRYV ITAAHCQPGF
LASLVAVMGE FDISGDLESK RSVTKNVKRV IVHRQYDPAT FENDLALLEL DSPVQFDTHI
VPICMPNDVA DFTGRMATVT GWGRLKYGGG VPSVLQEVQV PIIENSVCQE MFHTAGHNKK
ILTSFLCAGY ANGQKDSCEG DSGGPLVLQR PDGRYELAGT VSHGIKCAAP YLPGVYMRTT
FYKPWLRSIT GVK
