NAS8_STECR
ID NAS8_STECR Reviewed; 418 AA.
AC D2KBH9;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Zinc metalloproteinase nas-8 {ECO:0000305};
DE EC=3.4.24.21 {ECO:0000269|PubMed:20670659};
DE AltName: Full=Nematode astacin 8 {ECO:0000250|UniProtKB:Q18439};
DE AltName: Full=Sc-AST {ECO:0000303|PubMed:20670659};
DE Flags: Precursor;
OS Steinernema carpocapsae (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=34508 {ECO:0000312|EMBL:ACZ98149.1};
RN [1] {ECO:0000312|EMBL:ACZ98149.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=Breton {ECO:0000312|EMBL:ACZ98149.1};
RX PubMed=20670659; DOI=10.1016/j.molbiopara.2010.07.004;
RA Jing Y., Toubarro D., Hao Y., Simoes N.;
RT "Cloning, characterisation and heterologous expression of an astacin
RT metalloprotease, Sc-AST, from the entomoparasitic nematode Steinernema
RT carpocapsae.";
RL Mol. Biochem. Parasitol. 174:101-108(2010).
CC -!- FUNCTION: Metalloprotease. {ECO:0000269|PubMed:20670659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of peptide bonds in substrates containing five or
CC more amino acids, preferentially with Ala in P1', and Pro in P2'.;
CC EC=3.4.24.21; Evidence={ECO:0000269|PubMed:20670659};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- ACTIVITY REGULATION: Inhibited by ethylene glycol-bis(2-
CC aminoethylether)-N,N,N,N-tetraacetic acid (EGTA),
CC ethylenediaminetetraacetic acid (EDTA) and o-phenanthroline.
CC {ECO:0000269|PubMed:20670659}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20670659};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:20670659};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in first, second and fourth juveniles.
CC Not expressed in eggs and adults. {ECO:0000269|PubMed:20670659}.
CC -!- INDUCTION: Induced upon parasitic infection of insects.
CC {ECO:0000269|PubMed:20670659}.
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DR EMBL; GU199041; ACZ98149.1; -; mRNA.
DR AlphaFoldDB; D2KBH9; -.
DR SMR; D2KBH9; -.
DR MEROPS; M12.A21; -.
DR BRENDA; 3.4.24.21; 5892.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..100
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442253"
FT CHAIN 101..418
FT /note="Zinc metalloproteinase nas-8"
FT /evidence="ECO:0000255"
FT /id="PRO_5005126157"
FT DOMAIN 101..296
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 347..381
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 143..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 165..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 347..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 354..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 361..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 418 AA; 47458 MW; 0D16ABD2B90FE6E6 CRC64;
MMNRASLCRI AVLLCILHLS HLIDSTYAQS YLTEKDFLAP LYDDDAITLS DDDFDNARKL
STEMVNSQKK RRVLSHQKYY RGDIRGRAAW TSKLKSGVRR NGVTSVIKRW PNGRIPYVIS
SQYNERERAV LARAFQEYHS RTCIRFVPRT SFDQDYLYIG KIDGCYSDVG RAGGRQELSL
DDGCLQYNTA IHELMHSVGF YHEHERWDRD QYITILWNNI DKDAYDQFGR VDLTESSYYG
QAYDYYSVMH YDSLAFSKNG FETLVAKRPE MTAVIGSAID FSPIDLLKIN KLYNCPAPNT
IDISQISGNG WQGGGMGPRA PLPQVNLPLP PPPPLPTNPA IAIVGECSDR TNLCWRWLDR
CRSYFFEKIM KEFCALSCGY CVPTNAVSKA APAIPLQPTL SIAEGPEGPM PPLYQRFG
