CR16_LITRO
ID CR16_LITRO Reviewed; 25 AA.
AC P86503;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Caerin-1.16 {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, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AMIDATION AT LEU-25.
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 wide spectrum of activity. Induces
CC contraction of intestinal smooth muscle in isolated guinea pig ileum
CC through binding to CCK2R. Induces proliferation of mouse splenocytes.
CC Has no activity through opioid receptors. {ECO:0000269|PubMed:16124032,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P86503; -.
DR SMR; P86503; -.
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:0070665; P:positive regulation of leukocyte proliferation; IDA:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:UniProtKB.
DR InterPro; IPR010000; Caerin_1.
DR Pfam; PF07440; Caerin_1; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..25
FT /note="Caerin-1.16"
FT /evidence="ECO:0000269|PubMed:16124032"
FT /id="PRO_0000394429"
FT MOD_RES 25
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:16124032"
SQ SEQUENCE 25 AA; 2594 MW; 82B97580BB0EB36D CRC64;
GLFSVLGAVA KHVLPHVVPV IAEKL