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Protein

Serine protease snake

Gene

snk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei235 – 2351Charge relay systemBy similarity
Active sitei283 – 2831Charge relay systemBy similarity
Active sitei381 – 3811Charge relay systemBy similarity

GO - Molecular functioni

  • peptidase activity Source: FlyBase
  • serine-type endopeptidase activity Source: FlyBase
  • serine-type peptidase activity Source: FlyBase

GO - Biological processi

  • dorsal/ventral axis specification Source: FlyBase
  • maternal specification of dorsal/ventral axis, oocyte, germ-line encoded Source: FlyBase
  • protein processing Source: FlyBase
  • proteolysis Source: FlyBase
  • Toll signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.200.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease snake (EC:3.4.21.-)
Gene namesi
Name:snk
ORF Names:CG7996
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003450. snk.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • extracellular region Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 435408Serine protease snakePRO_0000028132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi179 ↔ 303PROSITE-ProRule annotation
Disulfide bondi220 ↔ 236PROSITE-ProRule annotation
Disulfide bondi346 ↔ 366PROSITE-ProRule annotation
Disulfide bondi377 ↔ 408PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP05049.
PRIDEiP05049.

Expressioni

Gene expression databases

BgeeiP05049.
ExpressionAtlasiP05049. differential.
GenevisibleiP05049. DM.

Interactioni

Protein-protein interaction databases

BioGridi66694. 3 interactions.
STRINGi7227.FBpp0111746.

Structurei

3D structure databases

ProteinModelPortaliP05049.
SMRiP05049. Positions 126-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini186 – 432247Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000130336.
InParanoidiP05049.
OMAiCQEYNSA.
OrthoDBiEOG75B84T.
PhylomeDBiP05049.

Family and domain databases

InterProiIPR022700. CLIP.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00680. CLIP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIILWSLIVH LQLTCLHLIL QTPNLEALDA LEIINYQTTK YTIPEVWKEQ
60 70 80 90 100
PVATIGEDVD DQDTEDEESY LKFGDDAEVR TSVSEGLHEG AFCRRSFDGR
110 120 130 140 150
SGYCILAYQC LHVIREYRVH GTRIDICTHR NNVPVICCPL ADKHVLAQRI
160 170 180 190 200
SATKCQEYNA AARRLHLTDT GRTFSGKQCV PSVPLIVGGT PTRHGLFPHM
210 220 230 240 250
AALGWTQGSG SKDQDIKWGC GGALVSELYV LTAAHCATSG SKPPDMVRLG
260 270 280 290 300
ARQLNETSAT QQDIKILIIV LHPKYRSSAY YHDIALLKLT RRVKFSEQVR
310 320 330 340 350
PACLWQLPEL QIPTVVAAGW GRTEFLGAKS NALRQVDLDV VPQMTCKQIY
360 370 380 390 400
RKERRLPRGI IEGQFCAGYL PGGRDTCQGD SGGPIHALLP EYNCVAFVVG
410 420 430
ITSFGKFCAA PNAPGVYTRL YSYLDWIEKI AFKQH
Length:435
Mass (Da):48,458
Last modified:May 10, 2004 - v2
Checksum:i6ECEA32D3CE41B32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 542AT → QA in CAA28197 (PubMed:11486795).Curated
Sequence conflicti91 – 911A → R in CAA28197 (PubMed:11486795).Curated
Sequence conflicti96 – 961S → T in CAA28197 (PubMed:11486795).Curated
Sequence conflicti104 – 12320CILAY…VHGTR → ASWPISGSTSSESIGCMA in CAA28197 (PubMed:11486795).CuratedAdd
BLAST
Sequence conflicti171 – 1711G → V in CAA28197 (PubMed:11486795).Curated
Sequence conflicti241 – 25212SKPPD…RLGAR → ANHRTWFAWRP in CAA28197 (PubMed:11486795).CuratedAdd
BLAST
Sequence conflicti307 – 3137LPELQIP → CGAPHT in CAA28197 (PubMed:11486795).Curated
Sequence conflicti341 – 3411V → S in CAA28197 (PubMed:11486795).Curated
Sequence conflicti371 – 3766PGGRDT → QAQGH in CAA28197 (PubMed:11486795).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04513 mRNA. Translation: CAA28197.1.
AE014297 Genomic DNA. Translation: AAF54897.1.
BT024420 mRNA. Translation: ABC86482.1.
PIRiA24702.
RefSeqiNP_001097766.1. NM_001104296.2.
NP_524338.2. NM_079614.3.
UniGeneiDm.2435.

Genome annotation databases

EnsemblMetazoaiFBtr0082716; FBpp0082184; FBgn0003450.
FBtr0112833; FBpp0111746; FBgn0003450.
GeneIDi41607.
KEGGidme:Dmel_CG7996.
UCSCiCG7996-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04513 mRNA. Translation: CAA28197.1.
AE014297 Genomic DNA. Translation: AAF54897.1.
BT024420 mRNA. Translation: ABC86482.1.
PIRiA24702.
RefSeqiNP_001097766.1. NM_001104296.2.
NP_524338.2. NM_079614.3.
UniGeneiDm.2435.

3D structure databases

ProteinModelPortaliP05049.
SMRiP05049. Positions 126-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66694. 3 interactions.
STRINGi7227.FBpp0111746.

Protein family/group databases

MEROPSiS01.200.

Proteomic databases

PaxDbiP05049.
PRIDEiP05049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082716; FBpp0082184; FBgn0003450.
FBtr0112833; FBpp0111746; FBgn0003450.
GeneIDi41607.
KEGGidme:Dmel_CG7996.
UCSCiCG7996-RA. d. melanogaster.

Organism-specific databases

CTDi41607.
FlyBaseiFBgn0003450. snk.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000130336.
InParanoidiP05049.
OMAiCQEYNSA.
OrthoDBiEOG75B84T.
PhylomeDBiP05049.

Miscellaneous databases

GenomeRNAii41607.
PROiP05049.

Gene expression databases

BgeeiP05049.
ExpressionAtlasiP05049. differential.
GenevisibleiP05049. DM.

Family and domain databases

InterProiIPR022700. CLIP.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00680. CLIP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease."
    Delotto R., Spierer P.
    Nature 323:688-692(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Positive and negative regulation of Easter, a member of the serine protease family that controls dorsal-ventral patterning in the Drosophila embryo."
    Misra S., Hecht P., Maeda R., Anderson K.V.
    Development 125:1261-1267(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF EASTER, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSNAK_DROME
AccessioniPrimary (citable) accession number: P05049
Secondary accession number(s): Q29QH0, Q9VFZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 10, 2004
Last modified: June 8, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.