ID   CR31_LITRO              Reviewed;          22 AA.
AC   P86505;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Caerin-3.1 {ECO:0000303|PubMed:16124032};
OS   Litoria rothii (Roth's tree frog) (Hyla rothii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Litoria.
OX   NCBI_TaxID=336074;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AMIDATION AT LYS-22.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:16124032};
RX   PubMed=16124032; DOI=10.1002/rcm.2098;
RA   Brinkworth C.S., Bowie J.H., Bilusich D., Tyler M.J.;
RT   "The rothein peptides from the skin secretion of Roth's tree frog Litoria
RT   rothii. Sequence determination using positive and negative ion electrospray
RT   mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 19:2716-2724(2005).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=19539637; DOI=10.1016/j.toxicon.2009.06.009;
RA   Sherman P.J., Jackway R.J., Nicholson E., Musgrave I.F., Boontheung P.,
RA   Bowie J.H.;
RT   "Activities of seasonably variable caerulein and rothein skin peptides from
RT   the tree frogs Litoria splendida and Litoria rothii.";
RL   Toxicon 54:828-835(2009).
CC   -!- FUNCTION: Antibacterial peptide with narrow spectrum of activity.
CC       Inhibits the formation of NO by neuronal nitric oxide synthase.
CC       {ECO:0000269|PubMed:16124032, ECO:0000269|PubMed:19539637}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16124032}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000269|PubMed:16124032}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during summer.
CC       {ECO:0000269|PubMed:19539637}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86505; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..22
FT                   /note="Caerin-3.1"
FT                   /evidence="ECO:0000269|PubMed:16124032"
FT                   /id="PRO_0000394433"
FT   MOD_RES         22
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:16124032"
SQ   SEQUENCE   22 AA;  2385 MW;  1D4411E2E9D43739 CRC64;
     GLWQKIKDKA SELVSGIVEG VK