NAS15_CAEEL
ID NAS15_CAEEL Reviewed; 571 AA.
AC P55115; Q7Z0N1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc metalloproteinase nas-15;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 15;
DE Flags: Precursor;
GN Name=nas-15; ORFNames=T04G9.2;
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 107-384, 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 marginal cells and muscles.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; FO080299; CCD62714.1; -; Genomic_DNA.
DR EMBL; AJ561208; CAD99210.1; -; mRNA.
DR PIR; B89451; B89451.
DR RefSeq; NP_508154.2; NM_075753.5.
DR AlphaFoldDB; P55115; -.
DR SMR; P55115; -.
DR BioGRID; 45379; 1.
DR STRING; 6239.T04G9.2; -.
DR MEROPS; M12.A41; -.
DR EPD; P55115; -.
DR PaxDb; P55115; -.
DR PeptideAtlas; P55115; -.
DR EnsemblMetazoa; T04G9.2.1; T04G9.2.1; WBGene00003534.
DR GeneID; 180426; -.
DR KEGG; cel:CELE_T04G9.2; -.
DR UCSC; T04G9.2; c. elegans.
DR CTD; 180426; -.
DR WormBase; T04G9.2; CE38541; WBGene00003534; nas-15.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_0_1_1; -.
DR InParanoid; P55115; -.
DR OMA; PDRGCYS; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; P55115; -.
DR PRO; PR:P55115; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003534; Expressed in pharyngeal muscle cell (C elegans) and 3 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: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; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 3.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 3.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 3.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442662"
FT CHAIN ?..571
FT /note="Zinc metalloproteinase nas-15"
FT /id="PRO_0000028919"
FT DOMAIN 114..307
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 354..388
FT /note="ShKT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 437..471
FT /note="ShKT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 536..571
FT /note="ShKT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 407..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 178..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 354..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 361..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 370..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 437..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 444..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 453..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 536..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 543..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 552..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 571 AA; 62831 MW; F3C2FA4C6B16073F CRC64;
MREYVLIFLV APVFAAILGP YDIPPELPPL NDENFFDRSH SEYETVLTPE DFELGTRITA
AMAHDNGDDI WDSDAMYSKD RFEGDIANDN LNASTAELFA NGGSGKSEDG KWYNAIKNRL
QLWPEGRIPY TISSQYSSYS RSLIAASMQE YASHTCIRWV PKEAADVNYV HIYPDRGCYS
MVGKMGGKQS LSLGSGCIQK GIILHELMHA VGFFHEQSRT DRDDHITIMW NNIQAGMQGQ
FEKYGHGTIQ SLGTGYDYGS IMHYGTKAFS RNGQPTMIPK KNGATIGQRN GFSKVDKFKI
NTLYGCPVEG EKPTTSAPTS GPIVITVKPV VITTGKPPVI QTVSPAVPLK PSECRNLRGD
CDDLAKQGWC IRNPGWMRAN CPISCGMCIP TKETQKPYVQ TTTQAATTTA RPQKPVTQPI
QPLPPVPPLP PTTPEDCEDL RVDCLVLVSQ RYCKISQNFM KSYCAKSCGF CFKPPPTEIP
DNRPTVVTTR PLVTLPPAVI RSRSPAPPVS TTTKAAPTTS TTSAAPYSPT PLPSECSDRK
HFCSHWKSAG FCEGIFMNYM KKNCPASCGL C
