NAS33_CAEEL
ID NAS33_CAEEL Reviewed; 644 AA.
AC P55114; Q7Z0M0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc metalloproteinase nas-33;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 33;
DE Flags: Precursor;
GN Name=nas-33; ORFNames=K04E7.3;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 147-448, AND NOMENCLATURE.
RC STRAIN=Bristol N2;
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; FO080549; CCD64584.1; -; Genomic_DNA.
DR EMBL; AJ561221; CAD99221.1; -; mRNA.
DR PIR; T16557; T16557.
DR RefSeq; NP_509086.2; NM_076685.2.
DR AlphaFoldDB; P55114; -.
DR SMR; P55114; -.
DR STRING; 6239.K04E7.3; -.
DR MEROPS; M12.A34; -.
DR PaxDb; P55114; -.
DR EnsemblMetazoa; K04E7.3.1; K04E7.3.1; WBGene00003551.
DR GeneID; 186987; -.
DR KEGG; cel:CELE_K04E7.3; -.
DR UCSC; K04E7.3; c. elegans.
DR CTD; 186987; -.
DR WormBase; K04E7.3; CE40705; WBGene00003551; nas-33.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_450736_0_0_1; -.
DR InParanoid; P55114; -.
DR OMA; INCQHGG; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; P55114; -.
DR PRO; PR:P55114; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003551; Expressed in adult organism and 1 other tissue.
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; 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 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 PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442680"
FT CHAIN ?..644
FT /note="Zinc metalloproteinase nas-33"
FT /id="PRO_0000028937"
FT DOMAIN 193..385
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 380..420
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 421..546
FT /note="CUB"
FT DOMAIN 547..596
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 40..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 254..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 388..408
FT /evidence="ECO:0000250"
FT DISULFID 410..419
FT /evidence="ECO:0000250"
FT DISULFID 559..590
FT /evidence="ECO:0000250"
FT DISULFID 563..595
FT /evidence="ECO:0000250"
FT DISULFID 574..580
FT /evidence="ECO:0000250"
SQ SEQUENCE 644 AA; 72526 MW; D71FA85A52CA1674 CRC64;
MLFVSILISQ FVTCLTQPDF FERPPPPDWF FPGPLRPWGP PPPWHRNRGP PPFGPPPPWD
RPPPPWRRPP WHRRPPWGLP PPPPPPEPEP QQDQPQVMFS QDIDKVVNSV NQNTAAFQRP
GESYDKVIQI MSSYFNRKSG SQYDINTVIP SSGIYNNEMA ANSKIAAVMF ESDMALTVSQ
MNKVAQNGFR VKRKMNLNGT TWSRNIPYRF LDTDGNWQSQ ITNGLRHYER NTCIRFSLNG
GGSDYLVFSK GEGCYSSVGR LGGPQEISIG DGCETLGIIT HEVGHALGFW HEQARPERDS
YVRINRQNAI NGLEGQFDKR SWSEVNEYSL PYDYGSVMHY GPKSFSKSST MNTVEPVDPA
FINTIGNRVE PSFLDLKLLN TAFCSNICTN RINCQHGGYA DPNNCGQCTC PTGLEGTYCE
RLQTSNCGVE LPRADYSWRN ISYSGSSDCY WRIVSANGGN VRFELTYVMY RCSPVCEEFV
EMKAEYSHEA TGYRQCCKAV LGERISKGNS VLIISKATQN SQFVLRYRED GTAPTQRPPP
VRVAAPRSYS LLWSGWTRCS ENCGSCGTQY RERCTSTTNC LRSAKQTRVC NTQPCAQGTT
RGKRSVLQTQ ISHRVKRLNG WCCARFVLSR GVCVPVRTGV THPN
