NAS35_CAEEL
ID NAS35_CAEEL Reviewed; 592 AA.
AC P98060; Q6AHR4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc metalloproteinase dpy-31 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 35 {ECO:0000303|PubMed:14653817};
DE AltName: Full=Procollagen C-proteinase {ECO:0000303|PubMed:15579684};
DE AltName: Full=Tollish protein 2 {ECO:0000303|Ref.2};
DE Flags: Precursor;
GN Name=dpy-31 {ECO:0000303|PubMed:15579684, ECO:0000312|WormBase:R151.5a};
GN Synonyms=nas-35 {ECO:0000303|PubMed:14653817}, toh-2 {ECO:0000303|Ref.2};
GN ORFNames=R151.5 {ECO:0000312|WormBase:R151.5a};
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], AND ALTERNATIVE SPLICING.
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).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-280; GLY-339 AND LEU-469.
RX PubMed=15579684; DOI=10.1534/genetics.104.027953;
RA Novelli J., Ahmed S., Hodgkin J.;
RT "Gene interactions in Caenorhabditis elegans define DPY-31 as a candidate
RT procollagen C-proteinase and SQT-3/ROL-4 as its predicted major target.";
RL Genetics 168:1259-1273(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Metalloprotease which cleaves the carboxyl terminus of
CC procollagens, such as sqt-3, to mature collagens (By similarity).
CC Involved in cuticular collagen maturation (PubMed:15579684).
CC {ECO:0000250|UniProtKB:A8Q2D1, ECO:0000269|PubMed:15579684}.
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}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis, rectal and vulval
CC epithelial cells and amphid socket cells.
CC {ECO:0000269|PubMed:15579684}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the 2-fold embryonic stage
CC and continues throughout larval development and adulthood. In larvae,
CC expressed in the hypodermis but not in seam cells.
CC {ECO:0000269|PubMed:15579684}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality in 5 percent of the progeny. {ECO:0000269|PubMed:15579684}.
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DR EMBL; FO081317; CCD70758.1; -; Genomic_DNA.
DR RefSeq; NP_001022731.1; NM_001027560.3.
DR AlphaFoldDB; P98060; -.
DR SMR; P98060; -.
DR STRING; 6239.R151.5a; -.
DR MEROPS; M12.321; -.
DR iPTMnet; P98060; -.
DR EPD; P98060; -.
DR PaxDb; P98060; -.
DR PeptideAtlas; P98060; -.
DR EnsemblMetazoa; R151.5a.1; R151.5a.1; WBGene00006592.
DR EnsemblMetazoa; R151.5a.2; R151.5a.2; WBGene00006592.
DR GeneID; 176014; -.
DR KEGG; cel:CELE_R151.5; -.
DR UCSC; R151.5b; c. elegans.
DR CTD; 176014; -.
DR WormBase; R151.5a; CE27200; WBGene00006592; dpy-31.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_3_1; -.
DR InParanoid; P98060; -.
DR OMA; CMDYVEV; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; P98060; -.
DR BRENDA; 3.4.24.21; 1045.
DR PRO; PR:P98060; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006592; Expressed in pharyngeal muscle cell (C elegans) and 4 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:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
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; 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 Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 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; PS01186; EGF_2; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..127
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442682"
FT CHAIN 128..592
FT /note="Zinc metalloproteinase dpy-31"
FT /id="PRO_0000028939"
FT DOMAIN 127..326
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 349..361
FT /note="EGF-like"
FT /evidence="ECO:0000255"
FT DOMAIN 371..487
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 490..540
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 22..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 170..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 193..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 371..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 502..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 506..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 518..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MUTAGEN 280
FT /note="H->Y: In e2920; temperature sensitive mutant. At the
FT permissive temperature of 15 degrees Celsius, few animals
FT survive and are short and stouter."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 339
FT /note="G->E: In ju345; temperature sensitive mutant. At the
FT permissive temperature of 15 degrees Celsius, 80 percent of
FT animals are viable. Severe lethality in a sqt-3 (sc8)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 469
FT /note="L->P: In e2770; temperature sensitive mutant. At the
FT permissive temperature of 15 degrees Celsius, few animals
FT survive and are short and stouter, with impaired col-19
FT assembly in the alae. At the restrictive temperature of 25
FT degrees Celsius, embryonic lethal at the 3-fold stage with
FT few surviving animals arresting at the L1 larval stage."
FT /evidence="ECO:0000269|PubMed:15579684"
FT MUTAGEN 469
FT /note="L->S: Partially lethal."
FT /evidence="ECO:0000269|PubMed:15579684"
SQ SEQUENCE 592 AA; 67257 MW; 01F2633B0BE53443 CRC64;
MHKIFIIFGL LSLCAAHSLR DLSNKDEEDP PSSAPGVRKR RMMSEEDQKT VDYYMDKLNK
LADEKHPEEI ERHKNPELVA WDRKRDSVLN PEEQGKFFQG DIVLYPEQAK ALYEQALTEG
KTRVKRKFIG SNLRRWDASR PIIYAFDGSH TQREQRIIEL ALEHWHNITC LNFQRNDQAN
SGNRIVFTDV DGCASNVGRH PLGEEQLVSL APECIRLGVI AHEVAHALGF WHEQSRPDRD
QYVTVRWENI DKDSKGQFLK EDPDDVDNAG VPYDYGSIMH YRSKAFSKFD DLYTISTYVT
DYQKTIGQRD QLSFNDIRLM NKIYCSAVCP SKLPCQRGGY TDPRRCDRCR CPDGFTGQYC
EQVMPGYGAT CGGKISLTRS TTRISSPGYP REFKEGQECS WLLVAPPGHI VEFQFIGEFE
MYCKIRHSLC MDYVEVRNST DFANTGMRYC CYGTPPTRIR SATTDMVVLF RSFYRGGKGF
EARARAVPEA GNWNSWSPWT ACSATCGACG SRMRTRTCPP GNACSGEPVE TQICNTQACT
GMCAQKREEE GQCGGFLSLL RGVRCRQEKT VMAPCENACC PGFTLQRGRC VR
