PN47_PHONI
ID PN47_PHONI Reviewed; 245 AA.
AC P84033;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=U21-ctenitoxin-Pn1a;
DE Short=U21-CNTX-Pn1a;
DE EC=3.4.21.-;
DE AltName: Full=Proteinase PN47;
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, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:16278100};
RX PubMed=16278100; DOI=10.1016/j.cbpc.2005.09.010;
RA Richardson M., Pimenta A.M., Bemquerer M.P., Santoro M.M., Beirao P.S.,
RA Lima M.E., Figueiredo S.G., Bloch C. Jr., Vasconcelos E.A., Campos F.A.,
RA Gomes P.C., Cordeiro M.N.;
RT "Comparison of the partial proteomes of the venoms of Brazilian spiders of
RT the genus Phoneutria.";
RL Comp. Biochem. Physiol. 142:173-187(2006).
CC -!- FUNCTION: Protease. Hydrolyzes gelatin and succinyl casein.
CC {ECO:0000269|PubMed:16278100}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16278100}.
CC -!- MASS SPECTROMETRY: Mass=22088.99; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16278100};
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR AlphaFoldDB; P84033; -.
DR SMR; P84033; -.
DR PRIDE; P84033; -.
DR ArachnoServer; AS000011; U21-ctenitoxin-Pn1a (N-terminal fragment).
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW Serine protease.
FT CHAIN 1..245
FT /note="U21-ctenitoxin-Pn1a"
FT /id="PRO_0000058476"
FT DOMAIN 1..245
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 45
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT DISULFID 30..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 161..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 192..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 245 AA; 26776 MW; EDDEB2E8B02101D4 CRC64;
IVYGTVTTPG KYPWMVSIHE RVKDVMKQAC GGAILNENWI VTAAHCFDQP IILKDYEVYV
GIVSWLHKNA PTVQKFQLSK IIIHDKYVKD GFANDIALIK TATPIDIKGS KYGVNGICFP
SGATDPSGEA TVIGWGMIRG GGPISAELRQ VTLPLVPWQK CKQIYGHPDS EFEYIQVVPS
MLCAGGNGKD ACQFDSGGPL FQYDKKGVAT LIGTVANGAD CAYAHYPGMY MKVSAFRSWM
DKVMT
