NAS26_CAEEL
ID NAS26_CAEEL Reviewed; 414 AA.
AC Q22710;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc metalloproteinase nas-26;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 26;
DE AltName: Full=Tollish protein 1;
DE Flags: Precursor;
GN Name=toh-1; Synonyms=nas-26; ORFNames=T24A11.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
RA Finelli A.L., Savage C., Cho S.H., Padgett R.W.;
RT "Tollish genes in C. elegans.";
RL (er) Worm Breeder's Gazette 14(2):46(1996).
RN [3]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=14653817; DOI=10.1046/j.1432-1033.2003.03891.x;
RA Moehrlen F., Hutter H., Zwilling R.;
RT "The astacin protein family in Caenorhabditis elegans.";
RL Eur. J. Biochem. 270:4909-4920(2003).
CC -!- FUNCTION: Metalloprotease. {ECO:0000250|UniProtKB:A8Q2D1}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; Z49072; CAA88882.4; -; Genomic_DNA.
DR PIR; T25213; T25213.
DR RefSeq; NP_497769.3; NM_065368.5.
DR AlphaFoldDB; Q22710; -.
DR SMR; Q22710; -.
DR STRING; 6239.T24A11.3; -.
DR MEROPS; M12.A17; -.
DR EPD; Q22710; -.
DR PaxDb; Q22710; -.
DR PeptideAtlas; Q22710; -.
DR EnsemblMetazoa; T24A11.3.1; T24A11.3.1; WBGene00006591.
DR GeneID; 175491; -.
DR KEGG; cel:CELE_T24A11.3; -.
DR UCSC; T24A11.3; c. elegans.
DR CTD; 175491; -.
DR WormBase; T24A11.3; CE35909; WBGene00006591; toh-1.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_2_1; -.
DR InParanoid; Q22710; -.
DR OMA; NQIFVIY; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q22710; -.
DR PRO; PR:Q22710; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006591; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 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 Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..61
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442673"
FT CHAIN 62..414
FT /note="Zinc metalloproteinase nas-26"
FT /id="PRO_0000028930"
FT DOMAIN 62..264
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 251..307
FT /note="EGF-like"
FT DOMAIN 308..414
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 126..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 267..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 289..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 308..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 358..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 414 AA; 47140 MW; B8B381B421239D1B CRC64;
MTSSLVLILA PLALVAIGEA AFGNSSKIFE IPGLEVMASD KYPHFTTIET VSRTKVHRHR
REVIAGQIYD WNSYEIPFQI WGGDYNFQSL IRRGIRMWED STCLRFKENQ QSRDAIRYVL
EKGDSCFTEY IGRNGGHQDI IIGSECAEEY VVAHETGHAL GFWHTHQRPD RDRHISINWK
NVMEEATASF MPFRSMLQAF GIRQVSPRRV PYDYGSLMHY HAVAHAVKVS DFTIVPKELK
YVTTMGTEKM AFLDAKVIND IYCPNACQGR NHLNCLAGGY PDPNNCNVCR CPEGLGGPDC
GRLQPSPCGG EIHASDQWQT LSSPSGRDVH CYWRISVPEG SRVRFRLSDG EFPCSYGCQS
YVEIKHKLDV RLTGFRSCCY RPKEDTVSES NQIFVIYHPN GRTARFSLRF RRQA
