ID   DSK_DROMA               Reviewed;         141 AA.
AC   B2ZB96;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 23.
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:ACC99370.1};
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
RN   [1] {ECO:0000312|EMBL:ACC99370.1}
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] {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; EU635461; ACC99370.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2ZB96; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
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   Secreted; Signal; Sulfation.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..73
FT                   /evidence="ECO:0000269|PubMed:17632121"
FT                   /id="PRO_0000351165"
FT   PEPTIDE         76..82
FT                   /note="Drosulfakinin-0"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT                   /id="PRO_0000351166"
FT   PROPEP          86..111
FT                   /evidence="ECO:0000269|PubMed:17632121"
FT                   /id="PRO_0000351167"
FT   PEPTIDE         114..122
FT                   /note="Drosulfakinin-1"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT                   /id="PRO_0000351168"
FT   PEPTIDE         126..139
FT                   /note="Drosulfakinin-2"
FT                   /evidence="ECO:0000250|UniProtKB:P09040"
FT                   /id="PRO_0000351169"
FT   REGION          51..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   141 AA;  16154 MW;  782950AEB7462538 CRC64;
     MGLRSCTHLA TLFMTLWALA FCFLVVVPIP AQTTSLQNAK DDRRLQELES KIGAESDQPN
     ANLVGPSFSR FGDRRNQKTI SFGRRVPLIS RPMIPIELDL LMDNDDERTK AKRFDDYGHM
     RFGKRGGDDQ FDDYGHMRFG R