DSK_DROTE
ID DSK_DROTE Reviewed; 138 AA.
AC B2ZBA0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 24.
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:ACC99374.1};
OS Drosophila teissieri (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7243;
RN [1] {ECO:0000312|EMBL:ACC99374.1}
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-119, AND SULFATION AT TYR-114.
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; EU635465; ACC99374.1; -; Genomic_DNA.
DR AlphaFoldDB; B2ZBA0; -.
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_0000351185"
FT PEPTIDE 76..82
FT /note="Drosulfakinin-0"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT /id="PRO_0000351186"
FT PROPEP 86..108
FT /evidence="ECO:0000269|PubMed:17632121"
FT /id="PRO_0000351187"
FT PEPTIDE 111..119
FT /note="Drosulfakinin-1"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT /id="PRO_0000351188"
FT PEPTIDE 123..136
FT /note="Drosulfakinin-2"
FT /evidence="ECO:0000250|UniProtKB:P09040"
FT /id="PRO_0000351189"
FT MOD_RES 82
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 114
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 119
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:17632121"
FT MOD_RES 131
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09040"
FT MOD_RES 136
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P09040"
SQ SEQUENCE 138 AA; 15678 MW; 5B39D41D9D51C548 CRC64;
MGLRSCTHFA TLVMPLWALA FCFLVLVPVP AQTTSLQISK GDRRLQDLES NMGAESDQPN
ANLVGTSLSR FGDKRNQKII TFGRRVPRPI IPIELDLLMD NDDENTKAKR FDDYGHMRFG
KRGGDDQFDD YGHMRFGR