NAS34_CAEEL
ID NAS34_CAEEL Reviewed; 605 AA.
AC Q21059;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc metalloproteinase nas-34;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Defective hatching protein 1;
DE AltName: Full=Nematode astacin 34;
DE Flags: Precursor;
GN Name=hch-1; Synonyms=nas-34; ORFNames=F40E10.1;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Bristol N2;
RX PubMed=8861940; DOI=10.1002/j.1460-2075.1996.tb00786.x;
RA Hishida R., Ishihara T., Kondo K., Katsura I.;
RT "hch-1, a gene required for normal hatching and normal migration of a
RT neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1.";
RL EMBO J. 15:4111-4122(1996).
RN [2]
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 [3]
RP 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-322, 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 (By similarity). Required for normal hatching
CC and migration of neuroblasts. May act by degrading eggshell proteins at
CC hatching (PubMed:8861940). {ECO:0000250|UniProtKB:A8Q2D1,
CC ECO:0000269|PubMed:8861940}.
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 hypodermal cells. First expressed in
CC the dorsal and lateral surface area of the middle and posterior region
CC of embryos. At later stages, it localizes to lateral surface regions,
CC probably corresponding to hypodermal seam cells. In L1 larvae, it is
CC expressed in seam cells and in a few cells anterior to the nerve ring.
CC {ECO:0000269|PubMed:8861940}.
CC -!- DEVELOPMENTAL STAGE: In embryos, it is first expressed just before
CC elongation. {ECO:0000269|PubMed:8861940}.
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DR EMBL; D85744; BAA12861.1; -; mRNA.
DR EMBL; Z69792; CAB61002.1; -; Genomic_DNA.
DR PIR; S71630; S71630.
DR RefSeq; NP_510440.1; NM_078039.5.
DR AlphaFoldDB; Q21059; -.
DR SMR; Q21059; -.
DR STRING; 6239.F40E10.1; -.
DR MEROPS; M12.A25; -.
DR iPTMnet; Q21059; -.
DR EPD; Q21059; -.
DR PaxDb; Q21059; -.
DR PeptideAtlas; Q21059; -.
DR EnsemblMetazoa; F40E10.1.1; F40E10.1.1; WBGene00001828.
DR GeneID; 181564; -.
DR KEGG; cel:CELE_F40E10.1; -.
DR UCSC; F40E10.1; c. elegans.
DR CTD; 181564; -.
DR WormBase; F40E10.1; CE24964; WBGene00001828; hch-1.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000163716; -.
DR HOGENOM; CLU_017286_1_4_1; -.
DR InParanoid; Q21059; -.
DR OMA; QYWARKS; -.
DR OrthoDB; 241999at2759; -.
DR PhylomeDB; Q21059; -.
DR PRO; PR:Q21059; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001828; Expressed in embryo and 5 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:0035188; P:hatching; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0001764; P:neuron migration; 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; 2.60.120.290; -; 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 Pfam; PF01400; Astacin; 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.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..124
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442681"
FT CHAIN 125..605
FT /note="Zinc metalloproteinase nas-34"
FT /id="PRO_0000028938"
FT DOMAIN 124..322
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 317..357
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 366..469
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 525..566
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 479..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 165..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 191..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 325..345
FT /evidence="ECO:0000250"
FT DISULFID 347..356
FT /evidence="ECO:0000250"
FT DISULFID 366..388
FT /evidence="ECO:0000250"
FT DISULFID 415..436
FT /evidence="ECO:0000250"
FT DISULFID 531..551
FT /evidence="ECO:0000250"
FT DISULFID 537..560
FT /evidence="ECO:0000250"
FT DISULFID 541..565
FT /evidence="ECO:0000250"
SQ SEQUENCE 605 AA; 66259 MW; E32E67A0F2674809 CRC64;
MVSYWPVLIV LCLLPICHAK SYFADFVNGK GPFKQADALK FMDKMTILNK LQADILGIPQ
PDEFSALDFE DKIESKPDEI PYLFEGDMVL TDEQMDLIIK NVRDQYWARK SSTNEFLYAI
RGKRSMTSFL SERWSFPVPY YIDTSSGVNT NAVLAGVAKW EQETCARFTR LNSYSSSSRQ
NALRFISGNG CYSNIGKVSR FPQDVSIGWG CTSLGTVCHE IGHALGFYHE QARYDRDDYV
SILTQNIQDM YLSQFTKQSA SSMVDYGVGY DYGSVMHYDQ AAFSSTGGNT IATRDPNFQA
TIGQRVAPSF ADVKRINFAY CNSTCSNYLD CQNGGYINPN DCNNCKCPPG FGGQLCDVAG
TNSNGCGAGD ITATSSIQTI SASGALTCNY VIKAPVGAKV YFQMTAATFS RYSPCTTNYL
EINYGRDFSR VGARFCASYP TISLSETNTL VVIYKGVNGA RFSLNYRYDP VTFSTSAPTT
TSTTTTTAPI TVPTVSPTTT TTRQTTTTAR TSTTTTTTQA PPTTTTSTSQ CASWSACSAQ
CGGCGTQSRR CGTYVETVYC NTNPCTGGYC CRPFFYVTSF GTGYCRRPGA DTPAAPQRYV
EQRKG
