ID NAS27_CAEEL Reviewed; 428 AA.
AC O17264; Q7Z0M4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Zinc metalloproteinase nas-27;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 27;
DE Flags: Precursor;
GN Name=nas-27; ORFNames=T23F4.4;
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 200-229, 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; FO081745; CCD73622.1; -; Genomic_DNA.
DR EMBL; AJ561216; CAD99217.1; -; mRNA.
DR PIR; T32401; T32401.
DR RefSeq; NP_493926.2; NM_061525.3.
DR AlphaFoldDB; O17264; -.
DR SMR; O17264; -.
DR STRING; 6239.T23F4.4.1; -.
DR MEROPS; M12.A44; -.
DR GlyCosmos; O17264; 2 sites, No reported glycans.
DR PaxDb; 6239-T23F4-4; -.
DR EnsemblMetazoa; T23F4.4.1; T23F4.4.1; WBGene00003545.
DR GeneID; 188809; -.
DR KEGG; cel:CELE_T23F4.4; -.
DR UCSC; T23F4.4; c. elegans.
DR AGR; WB:WBGene00003545; -.
DR WormBase; T23F4.4; CE36020; WBGene00003545; nas-27.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000168554; -.
DR HOGENOM; CLU_017286_1_5_1; -.
DR InParanoid; O17264; -.
DR OMA; CCDEHIY; -.
DR OrthoDB; 1845810at2759; -.
DR PhylomeDB; O17264; -.
DR PRO; PR:O17264; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003545; Expressed in larva and 1 other cell type or 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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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 PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF862; ZINC METALLOPROTEINASE NAS-27; 1.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 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; 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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..57
FT /evidence="ECO:0000255"
FT /id="PRO_0000442674"
FT CHAIN 58..428
FT /note="Zinc metalloproteinase nas-27"
FT /id="PRO_0000028931"
FT DOMAIN 58..255
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 250..291
FT /note="EGF-like"
FT DOMAIN 306..428
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 120..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 258..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 281..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 306..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 366..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 428 AA; 48983 MW; C3DF49EAF6EE6E72 CRC64;
MQILPIFFPL LITSLHAIPR GRRAVRNRNE GDINSLVGVG QYLYQGDIAV VKSRARRAVI
RQKHKKWKLP MPYSFDRNFP SRSRQRVLEA MQFWSEKTCV TFHENRYVYP HVSIFEGNGC
WSFVGKQPSL REQSLSLERS CTDHTFVVAH EIAHTLGFYH EHARGDRDQF ISIDYSNVNP
NLTFAFAKES EKQLDHQEAA YEYGSVMHYS VDQFAVNTNR PVIYARDQKF AQAMGNRMRA
TFQDVSRMNV LYNCHERCAN TLNRCQQGGY PAPSDCSQCV CPDGFGGNFC ETIEAHSVGQ
KDNSDCGGVL WASETSQTFY GAVRTRVHSN SVLPTPEHCF WHIRASQGKS IEIQIKNIIS
PCSMSCSFNA LELKLSNFTM TGPRFCCDEH IYNRYSQPKV FQSEGPLAVI GAYARYDYLD
FNIEYRAV
//
