ID   PN16_PHONI              Reviewed;         128 AA.
AC   P84032;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=U24-ctenitoxin-Pn1a;
DE            Short=U24-CNTX-Pn1a;
DE   AltName: Full=Venom protein PN16C3;
OS   Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria.
OX   NCBI_TaxID=6918;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND VARIANTS GLY-31; TYR-119 AND ASN-126.
RC   TISSUE=Venom;
RA   Richardson M., Pimenta A.M.C., Bemquerer M.P., Santoro M.M.,
RA   Figueiredo S.G., Cordeiro M.N.;
RT   "Protein PN16C3 from venom of Phoneutria nigriventer has sequence
RT   similarities with inhibitors of cysteinyl proteinases.";
RL   Submitted (JUN-2004) to UniProtKB.
CC   -!- FUNCTION: Cysteine proteinase inhibitor.
CC       {ECO:0000250|UniProtKB:P81439}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=14778.05; Mass_error=0.03; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
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DR   AlphaFoldDB; P84032; -.
DR   SMR; P84032; -.
DR   ArachnoServer; AS000010; U24-ctenitoxin-Pn1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.800.10; -; 2.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   Pfam; PF00086; Thyroglobulin_1; 2.
DR   SMART; SM00211; TY; 2.
DR   SUPFAM; SSF57610; SSF57610; 2.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW   Secreted; Thiol protease inhibitor.
FT   CHAIN           1..128
FT                   /note="U24-ctenitoxin-Pn1a"
FT                   /id="PRO_0000058475"
FT   DOMAIN          4..67
FT                   /note="Thyroglobulin type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DOMAIN          72..127
FT                   /note="Thyroglobulin type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        7..27
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        38..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        47..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        107..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   VARIANT         31
FT                   /note="S -> G"
FT                   /evidence="ECO:0000269|Ref.1"
FT   VARIANT         119
FT                   /note="H -> Y"
FT                   /evidence="ECO:0000269|Ref.1"
FT   VARIANT         126
FT                   /note="K -> N"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   128 AA;  14788 MW;  0CC710D7DBBB62CA CRC64;
     ARPKSDCEKH RESTEKTGTI MKLIPKCKEN SDYEELQCYE DSKFCVCYDK KGHAASPIST
     KVKECGCYLK QKERKDSGRE SAIIPQCEED GKWAKKQLWE FNKSCWCVDE KGEQVGKIHH
     DCDSLKCE