DSK_DROSI
ID DSK_DROSI Reviewed; 141 AA.
AC B2ZB99; B4QUX7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Drosulfakinins {ECO:0000303|PubMed:17632121};
DE Contains:
DE RecName: Full=Drosulfakinin-0 {ECO:0000303|PubMed:17632121};
DE Short=DSK-0 {ECO:0000303|PubMed:17632121};
DE Contains:
DE RecName: Full=Drosulfakinin-1 {ECO:0000303|PubMed:17632121};
DE AltName: Full=Drosulfakinin I {ECO:0000303|PubMed:17632121};
DE Short=DSK-I {ECO:0000303|PubMed:17632121};
DE Contains:
DE RecName: Full=Drosulfakinin-2 {ECO:0000303|PubMed:17632121};
DE AltName: Full=Drosulfakinin II {ECO:0000303|PubMed:17632121};
DE Short=DSK-II {ECO:0000303|PubMed:17632121};
DE Flags: Precursor;
GN Name=Dsk {ECO:0000312|EMBL:ACC99373.1}; ORFNames=GD19701;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:ACC99373.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ke F.;
RT "A molecular phylogeny for the Drosophila melanogaster subgroup.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3] {ECO:0000305}
RP IDENTIFICATION, AMIDATION AT PHE-82 AND PHE-122, AND SULFATION AT TYR-117.
RX PubMed=17632121; DOI=10.1016/j.jinsphys.2007.06.001;
RA Palmer G.C., Tran T., Duttlinger A., Nichols R.;
RT "The drosulfakinin 0 (DSK 0) peptide encoded in the conserved Dsk gene
RT affects adult Drosophila melanogaster crop contractions.";
RL J. Insect Physiol. 53:1125-1133(2007).
CC -!- FUNCTION: Drosulfakinin-0 (DSK 0) plays diverse biological roles
CC including regulating gut muscle contraction in adults but not in
CC larvae. {ECO:0000250|UniProtKB:P09040}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09040}.
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000255}.
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DR EMBL; EU635464; ACC99373.1; -; Genomic_DNA.
DR EMBL; CM000364; EDX11558.1; -; Genomic_DNA.
DR RefSeq; XP_002102055.1; XM_002102019.2.
DR AlphaFoldDB; B2ZB99; -.
DR STRING; 7240.B2ZB99; -.
DR EnsemblMetazoa; FBtr0219611; FBpp0218103; FBgn0191192.
DR GeneID; 6726642; -.
DR HOGENOM; CLU_1847224_0_0_1; -.
DR OMA; FGDRRNQ; -.
DR PhylomeDB; B2ZB99; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR Bgee; FBgn0191192; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:EnsemblMetazoa.
DR GO; GO:0071855; F:neuropeptide receptor binding; IEA:EnsemblMetazoa.
DR GO; GO:0008343; P:adult feeding behavior; IEA:EnsemblMetazoa.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0008345; P:larval locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:EnsemblMetazoa.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:EnsemblMetazoa.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:EnsemblMetazoa.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:EnsemblMetazoa.
DR GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB.
DR InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR InterPro; IPR013259; Sulfakinin.
DR Pfam; PF08257; Sulfakinin; 2.
DR PROSITE; PS00259; GASTRIN; 2.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Neuropeptide;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..73
FT /evidence="ECO:0000269|PubMed:17632121"
FT /id="PRO_0000351180"
FT PEPTIDE 76..82
FT /note="Drosulfakinin-0"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT /id="PRO_0000351181"
FT PROPEP 86..111
FT /evidence="ECO:0000269|PubMed:17632121"
FT /id="PRO_0000351182"
FT PEPTIDE 114..122
FT /note="Drosulfakinin-1"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT /id="PRO_0000351183"
FT PEPTIDE 126..139
FT /note="Drosulfakinin-2"
FT /evidence="ECO:0000250|UniProtKB:P09040"
FT /id="PRO_0000351184"
FT MOD_RES 82
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 117
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 122
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 134
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09040"
FT MOD_RES 139
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P09040"
FT CONFLICT 19
FT /note="V -> L (in Ref. 1; ACC99373)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> P (in Ref. 1; ACC99373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 16114 MW; D9D5345400815A80 CRC64;
MGLRSCTHLA TLFMTLWAVA FCFLVVVPIP AQTTSLQNAK DDRRLQELES KIGAESDQTN
ANLVGPSFSR FGDRRNQKAI SFGRRVPLIS RPMIPIELDL LMDNDDERTK AKRFDDYGHM
RFGKRGGDDQ FDDYGHMRFG R
