NAS36_HAECO
ID NAS36_HAECO Reviewed; 612 AA.
AC D5FM37;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Zinc metalloproteinase nas-36 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:20800010};
DE AltName: Full=Nematode astacin 36 {ECO:0000250|UniProtKB:Q18206};
DE Flags: Precursor;
GN Name=nas-36 {ECO:0000312|EMBL:ACZ64272.1};
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6289 {ECO:0000312|EMBL:ACZ64272.1};
RN [1] {ECO:0000312|EMBL:ACZ64272.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20800010; DOI=10.1017/s0031182010001113;
RA Stepek G., McCormack G., Birnie A.J., Page A.P.;
RT "The astacin metalloprotease moulting enzyme NAS-36 is required for normal
RT cuticle ecdysis in free-living and parasitic nematodes.";
RL Parasitology 138:237-248(2011).
CC -!- FUNCTION: Metalloprotease (PubMed:20800010). Involved in molting, a
CC process during larval stages in which a new cuticle is formed and the
CC old cuticle is shed (By similarity). {ECO:0000250|UniProtKB:Q18206,
CC ECO:0000269|PubMed:20800010}.
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 1,10-phenanthroline.
CC {ECO:0000269|PubMed:20800010}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; FJ812519; ACZ64272.1; -; Genomic_DNA.
DR AlphaFoldDB; D5FM37; -.
DR SMR; D5FM37; -.
DR MEROPS; M12.319; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR033957; NAS-36.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10127:SF849; PTHR10127:SF849; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..122
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442252"
FT CHAIN 123..612
FT /note="Zinc metalloproteinase nas-36"
FT /evidence="ECO:0000255"
FT /id="PRO_5005126565"
FT DOMAIN 123..320
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 320..355
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 365..478
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 503..552
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 166..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 190..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 329..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 345..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 365..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 515..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 519..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 531..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 612 AA; 68068 MW; 182E9BFC671FBA76 CRC64;
MLLLVLLFVF ISATNASDVG RRELEKHFDV GDSSLDSVGD VLLKLKKLAH QRAFGNREFG
HDAEEDSKKP VAISVLQPTV AKDVSPYLFE GDIFLSKKQA INILKEVSGI ESKSKPNVRG
RRSFDASPES KWPTTAPIKY RFHESIDFYA VSNIIKAIRY WENVTCLEFE NSPDVADNED
FIEFFQGQGC YSMIGRNGGR QGVSIGENCV KAGVIEHEIG HAIGMWHEQS RPDAQSYIKV
ESDFILPSYV SDFLQRDKDI DTLGLPYDLG SVMHYGSTAF SVDQSSKTLI TRDPLYQSTI
GQRETLSFLD IETINKAYCS DRCSGSNDCK NGGYPHPKQC DTCLCPNGLS GPKCEDFEPP
RKAECGGKIV VKEEWQSIES PGFPDPGYDP DQKCNWVFEV AGKRIEFEFI EEFSFLCTST
CVDYVEMKIS ADLRPTGFRW CCFNIPKGSF VSELNIAVII FRSQLTNDVG FKLQARATDL
PARTTPAPVV ITTTPVPTTI EGTDQWAEWG SWSQCSRSCG GCGIMSRVRV CRTKQCKGRR
QEFSTCNLKA CPIDKHCAKL LANDKICNGR VCTKASQALS GCLEPQCCPP FINVDGTCQS
DSPLLNDFEL AK
