WAPN_NAJNG
ID WAPN_NAJNG Reviewed; 51 AA.
AC P60589; P83769;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Nawaprin;
OS Naja nigricollis (Black-necked spitting cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8654;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND STRUCTURE BY NMR.
RC TISSUE=Venom;
RX PubMed=12878611; DOI=10.1074/jbc.m305322200;
RA Torres A.M., Wong H.Y., Desai M., Moochhala S., Kuchel P.W., Kini R.M.;
RT "Identification of a novel family of proteins in snake venoms. Purification
RT and structural characterization of nawaprin from Naja nigricollis snake
RT venom.";
RL J. Biol. Chem. 278:40097-40104(2003).
CC -!- FUNCTION: Damages membranes of susceptible bacteria. Has no hemolytic
CC activity. Not toxic to mice. Does not inhibit the proteinases elastase
CC and cathepsin G. {ECO:0000250|UniProtKB:P83952}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=5288.5; Mass_error=0.08; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12878611};
CC -!- SIMILARITY: Belongs to the snake waprin family. {ECO:0000305}.
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DR PDB; 1UDK; NMR; -; A=1-51.
DR PDBsum; 1UDK; -.
DR AlphaFoldDB; P60589; -.
DR SMR; P60589; -.
DR MEROPS; I17.004; -.
DR EvolutionaryTrace; P60589; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 4.10.75.10; -; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF00095; WAP; 1.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR PROSITE; PS51390; WAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Secreted.
FT CHAIN 1..51
FT /note="Nawaprin"
FT /id="PRO_0000188988"
FT DOMAIN 1..50
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 7..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:12878611"
FT DISULFID 20..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:12878611"
FT DISULFID 24..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:12878611"
FT DISULFID 30..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722,
FT ECO:0000269|PubMed:12878611"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1UDK"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1UDK"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1UDK"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1UDK"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1UDK"
SQ SEQUENCE 51 AA; 5296 MW; 27674128D7498CCC CRC64;
NEKSGSCPDM SMPIPPLGIC KTLCNSDSGC PNVQKCCKNG CGFMTCTTPV P