ID   SK1_PERAM               Reviewed;          11 AA.
AC   P36885;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Sulfakinin-1;
DE            Short=PerAm-SK-1;
DE   AltName: Full=Perisulfakinin;
DE            Short=Pea-SK-I;
OS   Periplaneta americana (American cockroach) (Blatta americana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC   Blattinae; Periplaneta.
OX   NCBI_TaxID=6978;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT PHE-11, AND SULFATION AT TYR-6.
RC   TISSUE=Corpora cardiaca;
RX   PubMed=2615921; DOI=10.1016/0143-4179(89)90038-3;
RA   Veenstra J.A.;
RT   "Isolation and structure of two gastrin/CCK-like neuropeptides from the
RT   American cockroach homologous to the leucosulfakinins.";
RL   Neuropeptides 14:145-149(1989).
RN   [2]
RP   PROTEIN SEQUENCE, AMIDATION AT PHE-11, AND SULFATION AT TYR-6.
RX   PubMed=10406966; DOI=10.1046/j.1432-1327.1999.00532.x;
RA   Predel R., Brandt W., Kellner R., Rapus J., Nachman R.J., Gaede G.;
RT   "Post-translational modifications of the insect sulfakinins: sulfation,
RT   pyroglutamate-formation and O-methylation of glutamic acid.";
RL   Eur. J. Biochem. 263:552-560(1999).
RN   [3]
RP   PROTEIN SEQUENCE, AND AMIDATION AT PHE-11.
RC   TISSUE=Corpora cardiaca;
RX   PubMed=19257902; DOI=10.1186/1471-2148-9-50;
RA   Roth S., Fromm B., Gaede G., Predel R.;
RT   "A proteomic approach for studying insect phylogeny: CAPA peptides of
RT   ancient insect taxa (Dictyoptera, Blattoptera) as a test case.";
RL   BMC Evol. Biol. 9:50-50(2009).
CC   -!- FUNCTION: Stimulates hindgut contractions.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
CC   -!- CAUTION: PubMed:10406966 reported, in addition to the presence of
CC       glutamate methyl ester, the partial formation of pyroglutamic acid by
CC       the N-terminal glutamic acid. These are most probably artifacts of
CC       isolation. {ECO:0000305}.
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DR   PIR; A60656; A60656.
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   InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR   InterPro; IPR013259; Sulfakinin.
DR   Pfam; PF08257; Sulfakinin; 1.
DR   PROSITE; PS00259; GASTRIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Hormone; Neuropeptide; Secreted;
KW   Sulfation.
FT   PEPTIDE         1..11
FT                   /note="Sulfakinin-1"
FT                   /id="PRO_0000043893"
FT   MOD_RES         6
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10406966,
FT                   ECO:0000269|PubMed:2615921"
FT   MOD_RES         11
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:10406966,
FT                   ECO:0000269|PubMed:19257902, ECO:0000269|PubMed:2615921"
SQ   SEQUENCE   11 AA;  1445 MW;  8B4E0680E86B5AAA CRC64;
     EQFDDYGHMR F