CR11_RANSP
ID CR11_RANSP Reviewed; 25 AA.
AC P62568; P56226;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Caerin-1.1 {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Caerin-1.1.1 {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Caerin-1.1.2 {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Caerin-1.1.4 {ECO:0000250|UniProtKB:Q800R2};
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, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Parotoid gland;
RA Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT "Peptides from Australian frogs. Structures of the caerins and caeridin 1
RT from Litoria splendida.";
RL J. Chem. Soc. Perkin Trans. I 1:3173-3178(1992).
RN [2]
RP FUNCTION, STRUCTURE BY NMR OF 1-25, AND AMIDATION AT LEU-25.
RX PubMed=9266696; DOI=10.1111/j.1432-1033.1997.00545.x;
RA Wong H., Bowie J.H., Carver J.A.;
RT "The solution structure and activity of caerin 1.1, an antimicrobial
RT peptide from the Australian green tree frog, Litoria splendida.";
RL Eur. J. Biochem. 247:545-557(1997).
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: [Caerin-1.1]: Antimicrobial peptide with antibacterial and
CC antiviral activities (PubMed:9266696). Adopt an alpha helical
CC conformation which can disrupt bacterial membranes (PubMed:9266696).
CC Inhibits the formation of NO by neuronal nitric oxide synthase (nNOS)
CC at micromolar concentrations (PubMed:11784303). Acts by a non-
CC competitive mechanism, probably by binding to calcium/calmodulin and as
CC a consequence blocking calmodulin attachment to nNOS (By similarity).
CC {ECO:0000250|UniProtKB:P81252, ECO:0000269|PubMed:11784303,
CC ECO:0000269|PubMed:9266696}.
CC -!- FUNCTION: [Caerin-1.1.1]: Is inactive. {ECO:0000269|PubMed:9266696}.
CC -!- FUNCTION: [Caerin-1.1.4]: Is inactive. {ECO:0000269|PubMed:9266696}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC glands. {ECO:0000305|Ref.1}.
CC -!- DOMAIN: Contains two amphipathic alpha helix regions separated by a
CC region of less-defined helicity and greater flexibility.
CC {ECO:0000305|PubMed:9266696}.
CC -!- PTM: The major product is Caerin-1.1; in addition, different peptides
CC are produced that are missing some amino acid residues at the N-
CC terminus. Caerin-1.1.1 is inactive.
CC -!- MASS SPECTROMETRY: [Caerin-1.1]: Mass=2582; Method=FAB;
CC Evidence={ECO:0000269|Ref.1};
CC -!- MASS SPECTROMETRY: [Caerin-1.1.1]: Mass=2412; Method=FAB;
CC Evidence={ECO:0000269|Ref.1};
CC -!- MASS SPECTROMETRY: [Caerin-1.1.2]: Mass=2299; Method=FAB;
CC Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Caerin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P62568; -.
DR PCDDB; P62568; -.
DR SMR; P62568; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 Antiviral defense; Direct protein sequencing; Immunity; Innate immunity;
KW Secreted.
FT PEPTIDE 1..25
FT /note="Caerin-1.1"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000010171"
FT PEPTIDE 1..23
FT /note="Caerin-1.1.4"
FT /evidence="ECO:0000250|UniProtKB:Q800R2"
FT /id="PRO_0000450230"
FT PEPTIDE 3..25
FT /note="Caerin-1.1.1"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000010172"
FT PEPTIDE 4..25
FT /note="Caerin-1.1.2"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000010173"
FT MOD_RES 25
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9266696"
SQ SEQUENCE 25 AA; 2585 MW; D8A5A460BB0EBE00 CRC64;
GLLSVLGSVA KHVLPHVVPV IAEHL
