ISOHC_AGEAP
ID ISOHC_AGEAP Reviewed; 243 AA.
AC Q9TXD8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Venom peptide isomerase heavy chain;
DE EC=5.-.-.-;
OS Agelenopsis aperta (North American funnel-web spider) (Agelenopsis
OS gertschi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Agelenidae; Agelenopsis.
OX NCBI_TaxID=6908;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION AT ASN-127, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=7622482; DOI=10.1074/jbc.270.28.16719;
RA Shikata Y., Watanabe T., Teramoto T., Inoue A., Kawakami Y., Nishizawa Y.,
RA Katayama K., Kuwada M.;
RT "Isolation and characterization of a peptide isomerase from funnel web
RT spider venom.";
RL J. Biol. Chem. 270:16719-16723(1995).
CC -!- FUNCTION: Peptide isomerase that inverts the chirality at the Ser-81 of
CC omega-Aga IVB. Acts cofactor-independently.
CC {ECO:0000269|PubMed:7622482}.
CC -!- SUBUNIT: Heterodimer with venom peptide isomerase light chain;
CC disulfide-linked. {ECO:0000269|PubMed:7622482}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7622482}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:7622482}.
CC -!- PTM: N-linked glycan at Asn-127 consists of Man3-GlcNAc2-Fuc.
CC {ECO:0000269|PubMed:7622482}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR AlphaFoldDB; Q9TXD8; -.
DR SMR; Q9TXD8; -.
DR iPTMnet; Q9TXD8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; Glycoprotein; Isomerase;
KW Secreted.
FT CHAIN 1..243
FT /note="Venom peptide isomerase heavy chain"
FT /id="PRO_0000404523"
FT DOMAIN 1..243
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7622482"
FT DISULFID 31..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7622482"
FT DISULFID 116
FT /note="Interchain (with C-9 in venom peptide isomerase
FT light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7622482"
FT DISULFID 159..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7622482"
FT DISULFID 190..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:7622482"
SQ SEQUENCE 243 AA; 26511 MW; 582EC10BEAA058E2 CRC64;
IVGGKTAKFG DYPWMVSIQQ KNKKGTFDHI CGGAIINVNW ILTAAHCFDQ PIVKSDYRAY
VGLRSILHTK ENTVQRLELS KIVLHPGYKP KKDPDDIALI KVAKPIVIGN YANGICVPKG
VTNPEGNATV IGWGKISSGG KQVNTLQEVT IPIIPWKKCK EIYGDEFSEF EYSQITPYMI
CAGAEGKDSC QADSGGPLFQ IDANGVATLI GTVANGADCG YKHYPGVYMK VSSYTNWMSK
NMV
