ID   CAE12_LITRO             Reviewed;          10 AA.
AC   P86507;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 8.
DE   RecName: Full=Caerulein 1.2 {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, PYROGLUTAMATE FORMATION AT GLN-1,
RP   SULFATION AT TYR-4, AND AMIDATION AT PHE-10.
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: Induces contraction of intestinal smooth muscle in isolated
CC       guinea pig ileum. {ECO:0000269|PubMed:16124032,
CC       ECO:0000269|PubMed:19539637}.
CC   -!- FUNCTION: Induces contraction of isolated smooth muscle.
CC       {ECO:0000269|PubMed:16124032}.
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 and winter.
CC       {ECO:0000269|PubMed:19539637}.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000255}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Direct protein sequencing;
KW   Pyrrolidone carboxylic acid; Secreted; Sulfation.
FT   PEPTIDE         1..10
FT                   /note="Caerulein 1.2"
FT                   /evidence="ECO:0000269|PubMed:16124032"
FT                   /id="PRO_0000394469"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:16124032"
FT   MOD_RES         4
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:16124032"
FT   MOD_RES         10
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:16124032"
SQ   SEQUENCE   10 AA;  1306 MW;  99DBFCD37861BB5A CRC64;
     QQDYTGWFDF