XEN2_XENLA
ID XEN2_XENLA Reviewed; 66 AA.
AC P38951;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Xenoxin-2;
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 PROTEIN SEQUENCE.
RC TISSUE=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).
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.
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DR AlphaFoldDB; P38951; -.
DR SMR; P38951; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
FT CHAIN 1..66
FT /note="Xenoxin-2"
FT /id="PRO_0000190096"
FT DISULFID 3..24
FT /evidence="ECO:0000250"
FT DISULFID 17..37
FT /evidence="ECO:0000250"
FT DISULFID 43..58
FT /evidence="ECO:0000250"
FT DISULFID 59..64
FT /evidence="ECO:0000250"
SQ SEQUENCE 66 AA; 7346 MW; 39AB6B2E77217B30 CRC64;
LKCVNLQANG IKMTQECAKE DNKCLTLRSL KKTLKFCASD RICKTMKIMS LPGEKITCCE
GNMCNA