HAYAN_DROME
ID HAYAN_DROME Reviewed; 637 AA.
AC A8JUP7; A2RVC7; M9PJQ8; Q8SY50; Q9VWU2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine protease Hayan {ECO:0000305|PubMed:22227521};
DE EC=3.4.21.- {ECO:0000269|PubMed:22227521};
DE Flags: Precursor;
GN Name=Hayan {ECO:0000312|FlyBase:FBgn0030925};
GN ORFNames=CG6361 {ECO:0000312|FlyBase:FBgn0030925};
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:AAL68205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL68205.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:ABM92792.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABM92792.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INDUCTION BY WOUNDING AND BACTERIA, AND DISRUPTION PHENOTYPE.
RX PubMed=22227521; DOI=10.1038/emboj.2011.476;
RA Nam H.J., Jang I.H., You H., Lee K.A., Lee W.J.;
RT "Genetic evidence of a redox-dependent systemic wound response via Hayan
RT protease-phenoloxidase system in Drosophila.";
RL EMBO J. 31:1253-1265(2012).
CC -!- FUNCTION: Serine protease which, by converting prophenoloxidase 1
CC (PPO1) into its active form, plays an essential role in the
CC melanization immune response to physical or septic wounding. May
CC function in diverse PPO1-activating cascades that are negatively
CC controlled by different serpin proteins; Spn27A and Spn28D in the
CC hemolymph, and Spn28D and Spn77BA in the trachea. Also required in the
CC systematic wound response by mediating the redox-dependent activation
CC of the JNK cytoprotective cascade in neuronal tissues after integument
CC wounding. {ECO:0000269|PubMed:22227521}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22227521}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0030925};
CC IsoId=A8JUP7-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0030925};
CC IsoId=A8JUP7-2; Sequence=VSP_058363;
CC -!- INDUCTION: Up-regulated after wounding to the integument. Levels are
CC higher with septic wounding, using either Gram-negative or Gram-
CC positive bacteria. {ECO:0000269|PubMed:22227521}.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile with no obvious phenotype.
CC Reduced adult survival after wounding of the thorax, especially when
CC the injury completely penetrates the thorax (strong wound). Wounding
CC coupled with septic infection (septic injury) does not further reduce
CC survival. Survival after wounding is increased when flies ingest the
CC oxidant paraquat. Impaired melanization at the wound site. In pupae,
CC aseptic and septic-injury does not induce the cleavage of PPO1, and in
CC adults and larvae PPO1 activity is abolished.
CC {ECO:0000269|PubMed:22227521}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM92792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE014298; ABW09449.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48845.2; -; Genomic_DNA.
DR EMBL; AE014298; AGB95526.2; -; Genomic_DNA.
DR EMBL; AY075342; AAL68205.1; -; mRNA.
DR EMBL; BT029918; ABM92792.1; ALT_INIT; mRNA.
DR RefSeq; NP_001097020.1; NM_001103550.2. [A8JUP7-1]
DR RefSeq; NP_001259684.2; NM_001272755.2. [A8JUP7-1]
DR RefSeq; NP_573296.2; NM_133068.3. [A8JUP7-2]
DR AlphaFoldDB; A8JUP7; -.
DR SMR; A8JUP7; -.
DR STRING; 7227.FBpp0111913; -.
DR MEROPS; S01.B45; -.
DR PaxDb; A8JUP7; -.
DR DNASU; 32831; -.
DR EnsemblMetazoa; FBtr0074630; FBpp0074401; FBgn0030925. [A8JUP7-2]
DR EnsemblMetazoa; FBtr0113000; FBpp0111913; FBgn0030925. [A8JUP7-1]
DR EnsemblMetazoa; FBtr0343048; FBpp0309794; FBgn0030925. [A8JUP7-1]
DR GeneID; 32831; -.
DR KEGG; dme:Dmel_CG6361; -.
DR UCSC; CG6361-RA; d. melanogaster.
DR UCSC; CG6361-RB; d. melanogaster. [A8JUP7-1]
DR CTD; 32831; -.
DR FlyBase; FBgn0030925; Hayan.
DR VEuPathDB; VectorBase:FBgn0030925; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000168826; -.
DR InParanoid; A8JUP7; -.
DR OMA; PLAQCND; -.
DR PhylomeDB; A8JUP7; -.
DR BioGRID-ORCS; 32831; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hayan; fly.
DR GenomeRNAi; 32831; -.
DR PRO; PR:A8JUP7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030925; Expressed in arthropod fat body and 28 other tissues.
DR ExpressionAtlas; A8JUP7; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IGI:FlyBase.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035008; P:positive regulation of melanization defense response; IMP:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IGI:FlyBase.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR GO; GO:0035007; P:regulation of melanization defense response; IMP:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR022700; CLIP.
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; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51888; CLIP; 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; Disulfide bond; Hydrolase; Immunity;
KW Melanin biosynthesis; Protease; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..637
FT /note="Serine protease Hayan"
FT /id="PRO_5006947370"
FT DOMAIN 31..79
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 385..632
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 95..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 477
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 582
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 32..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 42..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 48..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 371..497
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 414..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 543..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 578..609
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 88..347
FT /note="DRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQN
FT FFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQS
FT VGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPN
FT NNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRD
FT KDTQPQEPWNDVSNNLDADPAPSIFNPAETR -> E (in isoform A)"
FT /id="VSP_058363"
SQ SEQUENCE 637 AA; 70116 MW; B2CC895C9CA0F363 CRC64;
MAMISARRYF LLGLLVLTTS AYVTVGDEGD PCQVRSDIPG ICLSSSACEN IRGYLKSGTL
STSQVPSCGF GAREEIICCP TVACCATDRG REVQFHATSS ERSSLPEPKR EPTPEPEPLP
PTTTEGKRER ESRLDENQNF FDFNKLLSTT VKPQKTHESL KLPTQESMKT PTHESMKMPT
HESMKLPTHE PMKLPIQSVG AWGIAPSKTQ PIASTQRSFM EPEWGREPRI VNRPLTTPRS
RPQRPNNSNF NTNPSPNNNN LIHLVNDRLR EQGMQIEPAR EVPMVLQTTP TPTPAPTPTQ
LIDPFEPYRF RGQDRDKDTQ PQEPWNDVSN NLDADPAPSI FNPAETRPTT PNPNPSRVNL
PEKERPSVAA CEKIRSGGKP LTVHILDGER VDRGVYPHMA AIAYNSFGSA AFRCGGSLIA
SRFVLTAAHC VNSDDSTPSF VRLGALNIEN PEPGYQDINV IDVQIHPDYS GSSKYYDIAI
LQLAEDAKES DVIRPACLYT DRSDPPANYK YFVAGWGVMN VTNRAVSKIL LRAALDLVPA
DECNASFAEQ PSANRTLRRG VIASQLCAAD KNQRKDACQG DSGGPLILEI DDVDGTYSIV
GVISSGFGCA TKTPGLYTRV SSFLDYIEGI VWPSNRF
