SNAK_DROME
ID SNAK_DROME Reviewed; 435 AA.
AC P05049; Q29QH0; Q9VFZ7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine protease snake;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=snk; ORFNames=CG7996;
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], AND FUNCTION.
RX PubMed=11486795; DOI=10.1038/323688a0;
RA Delotto R., Spierer P.;
RT "A gene required for the specification of dorsal-ventral pattern in
RT Drosophila appears to encode a serine protease.";
RL Nature 323:688-692(1986).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CLEAVAGE OF EASTER, AND SUBCELLULAR LOCATION.
RX PubMed=9477324; DOI=10.1242/dev.125.7.1261;
RA Misra S., Hecht P., Maeda R., Anderson K.V.;
RT "Positive and negative regulation of Easter, a member of the serine
RT protease family that controls dorsal-ventral patterning in the Drosophila
RT embryo.";
RL Development 125:1261-1267(1998).
CC -!- FUNCTION: Component of the extracellular signaling pathway that
CC establishes the dorsal-ventral pathway of the embryo. Three proteases;
CC ndl, gd and snk process easter to create active easter. Active easter
CC defines cell identities along the dorsal-ventral continuum by
CC activating the spz ligand for the Tl receptor in the ventral region of
CC the embryo. {ECO:0000269|PubMed:11486795}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9477324}.
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 -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
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DR EMBL; X04513; CAA28197.1; -; mRNA.
DR EMBL; AE014297; AAF54897.1; -; Genomic_DNA.
DR EMBL; BT024420; ABC86482.1; -; mRNA.
DR PIR; A24702; A24702.
DR RefSeq; NP_001097766.1; NM_001104296.2.
DR RefSeq; NP_524338.2; NM_079614.3.
DR AlphaFoldDB; P05049; -.
DR SMR; P05049; -.
DR BioGRID; 66694; 3.
DR STRING; 7227.FBpp0111746; -.
DR MEROPS; S01.200; -.
DR PaxDb; P05049; -.
DR DNASU; 41607; -.
DR EnsemblMetazoa; FBtr0082716; FBpp0082184; FBgn0003450.
DR EnsemblMetazoa; FBtr0112833; FBpp0111746; FBgn0003450.
DR GeneID; 41607; -.
DR KEGG; dme:Dmel_CG7996; -.
DR UCSC; CG7996-RA; d. melanogaster.
DR CTD; 41607; -.
DR FlyBase; FBgn0003450; snk.
DR VEuPathDB; VectorBase:FBgn0003450; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000168826; -.
DR HOGENOM; CLU_006842_0_3_1; -.
DR InParanoid; P05049; -.
DR OMA; VDIKWGC; -.
DR OrthoDB; 1144875at2759; -.
DR PhylomeDB; P05049; -.
DR Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
DR BioGRID-ORCS; 41607; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41607; -.
DR PRO; PR:P05049; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003450; Expressed in egg chamber and 4 other tissues.
DR ExpressionAtlas; P05049; baseline and differential.
DR Genevisible; P05049; DM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IGI:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IDA:FlyBase.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR GO; GO:0031638; P:zymogen activation; 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 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..435
FT /note="Serine protease snake"
FT /id="PRO_0000028132"
FT DOMAIN 92..138
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 186..432
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 93..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 104..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 110..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 179..303
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 220..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 346..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 377..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 53..54
FT /note="AT -> QA (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> R (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> T (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..123
FT /note="CILAYQCLHVIREYRVHGTR -> ASWPISGSTSSESIGCMA (in Ref.
FT 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> V (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..252
FT /note="SKPPDMVRLGAR -> ANHRTWFAWRP (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..313
FT /note="LPELQIP -> CGAPHT (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> S (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..376
FT /note="PGGRDT -> QAQGH (in Ref. 1; CAA28197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48458 MW; 6ECEA32D3CE41B32 CRC64;
MIILWSLIVH LQLTCLHLIL QTPNLEALDA LEIINYQTTK YTIPEVWKEQ PVATIGEDVD
DQDTEDEESY LKFGDDAEVR TSVSEGLHEG AFCRRSFDGR SGYCILAYQC LHVIREYRVH
GTRIDICTHR NNVPVICCPL ADKHVLAQRI SATKCQEYNA AARRLHLTDT GRTFSGKQCV
PSVPLIVGGT PTRHGLFPHM AALGWTQGSG SKDQDIKWGC GGALVSELYV LTAAHCATSG
SKPPDMVRLG ARQLNETSAT QQDIKILIIV LHPKYRSSAY YHDIALLKLT RRVKFSEQVR
PACLWQLPEL QIPTVVAAGW GRTEFLGAKS NALRQVDLDV VPQMTCKQIY RKERRLPRGI
IEGQFCAGYL PGGRDTCQGD SGGPIHALLP EYNCVAFVVG ITSFGKFCAA PNAPGVYTRL
YSYLDWIEKI AFKQH
