NAS32_CAEEL
ID NAS32_CAEEL Reviewed; 651 AA.
AC O16977; Q7Z0M1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc metalloproteinase nas-32;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 32;
DE Flags: Precursor;
GN Name=nas-32; ORFNames=T02B11.7;
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 291-367, 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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20109220; DOI=10.1186/1471-213x-10-14;
RA Park J.O., Pan J., Moehrlen F., Schupp M.O., Johnsen R., Baillie D.L.,
RA Zapf R., Moerman D.G., Hutter H.;
RT "Characterization of the astacin family of metalloproteases in C.
RT elegans.";
RL BMC Dev. Biol. 10:14-14(2010).
CC -!- FUNCTION: Metalloprotease. {ECO:0000250|UniProtKB:P07584}.
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 pharyngeal, anal depressor, intestinal
CC and vulva muscles, head neurons and head mesodermal cell.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; FO081565; CCD72452.1; -; Genomic_DNA.
DR EMBL; AJ561220; CAD99220.1; -; mRNA.
DR PIR; T32205; T32205.
DR RefSeq; NP_503351.3; NM_070950.4.
DR AlphaFoldDB; O16977; -.
DR SMR; O16977; -.
DR BioGRID; 43668; 1.
DR STRING; 6239.T02B11.7; -.
DR MEROPS; M12.A40; -.
DR PaxDb; O16977; -.
DR EnsemblMetazoa; T02B11.7.1; T02B11.7.1; WBGene00003550.
DR GeneID; 178595; -.
DR KEGG; cel:CELE_T02B11.7; -.
DR UCSC; T02B11.7; c. elegans.
DR CTD; 178595; -.
DR WormBase; T02B11.7; CE50805; WBGene00003550; nas-32.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_421052_0_0_1; -.
DR InParanoid; O16977; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; O16977; -.
DR PRO; PR:O16977; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003550; Expressed in larva 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; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-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; IPR003582; ShKT_dom.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript 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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..202
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442679"
FT CHAIN 203..651
FT /note="Zinc metalloproteinase nas-32"
FT /id="PRO_0000028936"
FT DOMAIN 203..394
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 380..433
FT /note="EGF-like"
FT DOMAIN 434..554
FT /note="CUB"
FT DOMAIN 610..647
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT ACT_SITE 292
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 BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 264..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 395..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 415..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 434..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 495..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 610..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 619..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 628..644
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 651 AA; 72761 MW; 01982B5BBDEC9FB8 CRC64;
MRRFFICYIG FLSIFLDFIL ADKDNNSEEE RDRKFDWKFE NENGKPEHET VTVPKLPDGS
YFWKWTWNSR INSTTAATPT STVTTSTSAP TTSPRVYKLK SEARKSLRKA LRGVPPEKRK
KQLKKMGKKM MKIPKITKKE SNKLHKSYRK VKITENPPAL DMFEVNERAG LNEYLFQGDI
NLNNNQIAKI SSEQSSKSRR KKRQIDNLAQ FWPGKVVYYY FDSGLTTTVQ QIVRDAITFL
ESNTCLKFEL NSTATNRIFS GVGCYSDTGM LGGEQTLSLG YGCEVTGTAA HEIAHTLGLF
HTQMRSDRDD YVTIDLTDVP ESSQQNFIKL TEATSTNLVD YEYGSFMHYS GRAFVSSGGV
DSIVPKDPVM VYTMGGRIVT FLDLKMLNTH YSCSCPTILS CGNGGFTNPA NCSVCICPYG
FGGALCTERT DYGCGSTLTA TDTWQQETYT FGNASNSATA RPSAVYCNHW IQAPVGKQIQ
FRIDSTYNTQ CVYGCTFNGV EPKLKSDMTI TQARYCCDEF NAEIMTADFG VNPMPVFSFN
RYYKTTYTWS YRYVDSNVTA CADTSDKATC LSLKSAKEQG CSIYDTAQLK VMCAATMDLC
GKVASDDGTC KDRFPKSQCS TYSTNGMCTQ QPPLAAEFSC AETCGFCTNP V
