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Database: UniProt
Entry: P98060
LinkDB: P98060
Original site: P98060 
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   10-APR-2019, entry version 150.
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,
GN   ECO:0000312|WormBase:R151.5a};
GN   Synonyms=nas-35 {ECO:0000303|PubMed:14653817},
GN   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
RP   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
RT   investigating 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
RP   MASS 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
RT   to identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
RP   PHENOTYPE, 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
RT   candidate procollagen C-proteinase and SQT-3/ROL-4 as its predicted
RT   major target.";
RL   Genetics 168:1259-1273(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-167, AND IDENTIFICATION BY
RP   MASS 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
CC       stage and continues throughout larval development and adulthood.
CC       In larvae, 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.
CC       {ECO:0000269|PubMed:15579684}.
DR   EMBL; FO081317; CCD70758.1; -; Genomic_DNA.
DR   RefSeq; NP_001022731.1; NM_001027560.3.
DR   UniGene; Cel.16899; -.
DR   ProteinModelPortal; 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   PRIDE; P98060; -.
DR   EnsemblMetazoa; R151.5a; R151.5a; 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   eggNOG; ENOG410ZPX7; LUCA.
DR   HOGENOM; HOG000020944; -.
DR   InParanoid; P98060; -.
DR   OMA; EFEMYCK; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; P98060; -.
DR   PRO; PR:P98060; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006592; Expressed in 6 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
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   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; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW   Zymogen.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19    127       {ECO:0000250|UniProtKB:P13497}.
FT                                /FTId=PRO_0000442682.
FT   CHAIN       128    592       Zinc metalloproteinase dpy-31.
FT                                /FTId=PRO_0000028939.
FT   DOMAIN      127    326       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      349    361       EGF-like. {ECO:0000255}.
FT   DOMAIN      371    487       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      490    540       TSP type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   ACT_SITE    223    223       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       222    222       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       226    226       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       232    232       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    167    167       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754521,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    438    438       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    170    325       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    193    214       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    371    399       {ECO:0000255|PROSITE-ProRule:PRU00059}.
FT   DISULFID    502    534       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    506    539       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    518    524       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   MUTAGEN     280    280       H->Y: In e2920; temperature sensitive
FT                                mutant. At the permissive temperature of
FT                                15 degrees Celsius, few animals survive
FT                                and are short and stouter.
FT                                {ECO:0000269|PubMed:15579684}.
FT   MUTAGEN     339    339       G->E: In ju345; temperature sensitive
FT                                mutant. At the permissive temperature of
FT                                15 degrees Celsius, 80 percent of animals
FT                                are viable. Severe lethality in a sqt-3
FT                                (sc8) mutant background.
FT                                {ECO:0000269|PubMed:15579684}.
FT   MUTAGEN     469    469       L->P: In e2770; temperature sensitive
FT                                mutant. At the permissive temperature of
FT                                15 degrees Celsius, few animals survive
FT                                and are short and stouter, with impaired
FT                                col-19 assembly in the alae. At the
FT                                restrictive temperature of 25 degrees
FT                                Celsius, embryonic lethal at the 3-fold
FT                                stage with few surviving animals
FT                                arresting at the L1 larval stage.
FT                                {ECO:0000269|PubMed:15579684}.
FT   MUTAGEN     469    469       L->S: Partially lethal.
FT                                {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
//
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