ID   DSK_DROYA               Reviewed;         137 AA.
AC   B2ZBA1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
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:ACC99375.1}; ORFNames=GE25375;
GN   and
GN   ORFNames=GE14608;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:ACC99375.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (DSK).
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] (DSK AND GE25375).
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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-81 AND PHE-118, AND SULFATION AT TYR-113.
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; EU635466; ACC99375.1; -; Genomic_DNA.
DR   EMBL; CH898474; EDX00615.1; -; Genomic_DNA.
DR   EMBL; CM000160; EDW95618.1; -; Genomic_DNA.
DR   RefSeq; XP_002087296.1; XM_002087260.2.
DR   RefSeq; XP_002095906.1; XM_002095870.2.
DR   AlphaFoldDB; B2ZBA1; -.
DR   SMR; B2ZBA1; -.
DR   STRING; 7245.FBpp0259618; -.
DR   EnsemblMetazoa; FBtr0261126; FBpp0259618; FBgn0232204.
DR   EnsemblMetazoa; FBtr0271893; FBpp0270385; FBgn0242452.
DR   GeneID; 6535250; -.
DR   KEGG; dya:Dyak_GE14608; -.
DR   KEGG; dya:Dyak_GE25375; -.
DR   eggNOG; ENOG502SESC; Eukaryota.
DR   HOGENOM; CLU_1847224_0_0_1; -.
DR   OrthoDB; 1534835at2759; -.
DR   PhylomeDB; B2ZBA1; -.
DR   Proteomes; UP000002282; Chromosome 3R.
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..31
FT                   /evidence="ECO:0000255"
FT   PROPEP          32..74
FT                   /evidence="ECO:0000269|PubMed:17632121"
FT                   /id="PRO_0000351190"
FT   PEPTIDE         75..81
FT                   /note="Drosulfakinin-0"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT                   /id="PRO_0000351191"
FT   PROPEP          85..107
FT                   /evidence="ECO:0000269|PubMed:17632121"
FT                   /id="PRO_0000351192"
FT   PEPTIDE         110..118
FT                   /note="Drosulfakinin-1"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT                   /id="PRO_0000351193"
FT   PEPTIDE         122..135
FT                   /note="Drosulfakinin-2"
FT                   /evidence="ECO:0000250|UniProtKB:P09040"
FT                   /id="PRO_0000351194"
FT   MOD_RES         81
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT   MOD_RES         113
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT   MOD_RES         118
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT   MOD_RES         130
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09040"
FT   MOD_RES         135
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P09040"
SQ   SEQUENCE   137 AA;  15673 MW;  7FA7AA3348490F45 CRC64;
     MGLRSCTHFA TLVIPLWALA FCFLVVVPVP AQTNLQTSKG DRRLQDLESN MGAESDQPNA
     NLVRPSLSRF GDKRNQKIIT FGRRVPRPMI PIELDLLMDN DDENTKAKRF DDYGHMRFGK
     RGGDDQFDDY GHMRFGR