XEN1_XENLA
ID XEN1_XENLA Reviewed; 84 AA.
AC Q09022; Q9PRX9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Xenoxin-1;
DE Flags: Precursor;
GN Name=xenoxin-1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-84.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=8393864; DOI=10.1016/s0021-9258(19)85442-x;
RA Kolbe H.V.J., Huber A., Cordier P., Rasmussen U.B., Bouchon B.,
RA Jaquinod M., Vlasak R., Delot E.C., Kreil G.;
RT "Xenoxins, a family of peptides from dorsal gland secretion of Xenopus
RT laevis related to snake venom cytotoxins and neurotoxins.";
RL J. Biol. Chem. 268:16458-16464(1993).
RN [2]
RP PROTEIN SEQUENCE OF 19-84, AND MASS SPECTROMETRY.
RC TISSUE=Dorsal skin;
RX PubMed=8203742; DOI=10.1006/abio.1994.1086;
RA James S., Gibbs B.F., Toney K., Bennett H.P.J.;
RT "Purification of antimicrobial peptides from an extract of the skin of
RT Xenopus laevis using heparin-affinity HPLC: characterization by ion-spray
RT mass spectrometry.";
RL Anal. Biochem. 217:84-90(1994).
CC -!- FUNCTION: Lacks alpha-neurotoxic activity, has apparently no
CC antibacterial activity, nor anti-coagulant potency.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC -!- MASS SPECTROMETRY: Mass=7227.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8203742};
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DR EMBL; X72673; CAA51225.1; -; mRNA.
DR PIR; I51698; I51698.
DR RefSeq; NP_001079296.1; NM_001085827.1.
DR AlphaFoldDB; Q09022; -.
DR SMR; Q09022; -.
DR PRIDE; Q09022; -.
DR GeneID; 378596; -.
DR KEGG; xla:378596; -.
DR CTD; 378596; -.
DR Xenbase; XB-GENE-6252635; xenoxin1.L.
DR OrthoDB; 1853023at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 378596; Expressed in zone of skin and 8 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8203742,
FT ECO:0000269|PubMed:8393864"
FT CHAIN 19..84
FT /note="Xenoxin-1"
FT /id="PRO_0000010304"
FT DISULFID 21..42
FT DISULFID 35..55
FT DISULFID 61..76
FT /evidence="ECO:0000250"
FT DISULFID 77..82
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 9263 MW; 0CC8FADA3B2D776C CRC64;
MRYAIVFFLV CVITLGEALK CVNLQANGIK MTQECAKEDT KCLTLRSLKK TLKFCASGRT
CTTMKIMSLP GEQITCCEGN MCNA