ID   CZS12_CRUCA             Reviewed;          75 AA.
AC   A0A193H397; C0HK07;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Cruzioseptin-12 {ECO:0000312|EMBL:ANN87768.1};
DE            Short=CZS-12 {ECO:0000303|PubMed:27321580};
DE   Flags: Precursor;
OS   Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Cruziohyla.
OX   NCBI_TaxID=318249 {ECO:0000312|EMBL:ANN87768.1};
RN   [1] {ECO:0000312|EMBL:ANN87768.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-72, SUBCELLULAR
RP   LOCATION, AMIDATION AT GLN-72, MASS SPECTROMETRY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000312|EMBL:ANN87768.1};
RX   PubMed=27321580; DOI=10.1016/j.jprot.2016.06.017;
RA   Proano-Bolanos C., Zhou M., Wang L., Coloma L.A., Chen T., Shaw C.;
RT   "Peptidomic approach identifies cruzioseptins, a new family of potent
RT   antimicrobial peptides in the splendid leaf frog, Cruziohyla calcarifer.";
RL   J. Proteomics 146:1-13(2016).
CC   -!- FUNCTION: Has antimicrobial activity.
CC       {ECO:0000250|UniProtKB:A0A193H362}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27321580}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:27321580}.
CC   -!- MASS SPECTROMETRY: Mass=2775.54; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:27321580};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Cruzioseptin subfamily. {ECO:0000305}.
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   EMBL; KX065088; ANN87768.1; -; mRNA.
DR   AlphaFoldDB; A0A193H397; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000303|PubMed:27321580"
FT                   /id="PRO_0000439483"
FT   PEPTIDE         46..72
FT                   /note="Cruzioseptin-12"
FT                   /evidence="ECO:0000269|PubMed:27321580"
FT                   /id="PRO_0000439484"
FT   PROPEP          74..75
FT                   /evidence="ECO:0000303|PubMed:27321580"
FT                   /id="PRO_0000439485"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000305|PubMed:27321580"
SQ   SEQUENCE   75 AA;  8407 MW;  009C04F9CDD21AC1 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKREEE NEEVQEDDDQ SEEKRGFLDV VKHVGKAVGK
     AALNAVNDLV NQGEQ