ID   CR23_RANSP              Reviewed;          25 AA.
AC   P69033; P56235; P82117;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Splendipherin {ECO:0000303|PubMed:10519546};
OS   Ranoidea splendida (Magnificent tree frog) (Litoria splendida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=30345;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Parotoid gland, and Rostral gland;
RX   PubMed=10519546; DOI=10.1038/46724;
RA   Wabnitz P.A., Bowie J.H., Tyler M.J., Wallace J.C., Smith B.P.;
RT   "Aquatic sex pheromone from a male tree frog.";
RL   Nature 401:444-445(1999).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=10601876; DOI=10.1046/j.1432-1327.2000.01010.x;
RA   Wabnitz P.A., Bowie J.H., Tyler M.J., Wallace J.C., Smith B.P.;
RT   "Differences in the skin peptides of the male and female Australian tree
RT   frog Litoria splendida. The discovery of the aquatic male sex pheromone
RT   splendipherin, together with Phe8 caerulein and a new antibiotic peptide
RT   caerin 1.10.";
RL   Eur. J. Biochem. 267:269-275(2000).
RN   [3]
RP   FUNCTION.
RX   PubMed=11784303; DOI=10.1046/j.0014-2956.2002.02630.x;
RA   Doyle J., Llewellyn L.E., Brinkworth C.S., Bowie J.H., Wegener K.L.,
RA   Rozek T., Wabnitz P.A., Wallace J.C., Tyler M.J.;
RT   "Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation
RT   of lesuerin from the skin secretion of the Australian stony creek frog
RT   Litoria lesueuri.";
RL   Eur. J. Biochem. 269:100-109(2002).
CC   -!- FUNCTION: Acts as a male sex pheromone that attracts females
CC       (PubMed:10519546, PubMed:10601876). Has no antimicrobial activity
CC       (PubMed:10519546, PubMed:10601876). Strongly inhibits the formation of
CC       NO by neuronal nitric oxide synthase (nNOS) at micromolar
CC       concentrations (PubMed:11784303). Acts by a non-competitive mechanism,
CC       probably by binding to calcium/calmodulin and as a consequence blocking
CC       calmodulin attachment to nNOS (By similarity).
CC       {ECO:0000250|UniProtKB:P56249, ECO:0000269|PubMed:10519546,
CC       ECO:0000269|PubMed:10601876, ECO:0000269|PubMed:11784303}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10519546,
CC       ECO:0000269|PubMed:10601876}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands. {ECO:0000305|PubMed:10519546, ECO:0000305|PubMed:10601876}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P69033; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005186; F:pheromone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR032021; Frog_Litoria.
DR   Pfam; PF16049; Antimicrobial24; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Direct protein sequencing; Pheromone; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Splendipherin"
FT                   /evidence="ECO:0000269|PubMed:10519546,
FT                   ECO:0000269|PubMed:10601876"
FT                   /id="PRO_0000043744"
SQ   SEQUENCE   25 AA;  2366 MW;  DDD82C36B49186B8 CRC64;
     GLVSSIGKAL GGLLADVVKS KGQPA