NAS14_CAEEL
ID NAS14_CAEEL Reviewed; 503 AA.
AC Q19269; Q7Z0N2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Zinc metalloproteinase nas-14;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 14;
DE Flags: Precursor;
GN Name=nas-14; ORFNames=F09E8.6;
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 217-355, 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 muscles and mc cells.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; Z73896; CAA98057.2; -; Genomic_DNA.
DR EMBL; AJ561207; CAD99209.1; -; mRNA.
DR PIR; T20658; T20658.
DR RefSeq; NP_502533.2; NM_070132.2.
DR AlphaFoldDB; Q19269; -.
DR SMR; Q19269; -.
DR STRING; 6239.F09E8.6; -.
DR MEROPS; M12.A23; -.
DR EPD; Q19269; -.
DR PaxDb; Q19269; -.
DR PeptideAtlas; Q19269; -.
DR EnsemblMetazoa; F09E8.6.1; F09E8.6.1; WBGene00003533.
DR GeneID; 184247; -.
DR KEGG; cel:CELE_F09E8.6; -.
DR UCSC; F09E8.6; c. elegans.
DR CTD; 184247; -.
DR WormBase; F09E8.6; CE35854; WBGene00003533; nas-14.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000154856; -.
DR HOGENOM; CLU_017286_0_1_1; -.
DR InParanoid; Q19269; -.
DR OMA; MTNDQRA; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q19269; -.
DR PRO; PR:Q19269; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003533; 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; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 2.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 2.
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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442661"
FT CHAIN ?..503
FT /note="Zinc metalloproteinase nas-14"
FT /id="PRO_0000028918"
FT DOMAIN 116..312
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 380..414
FT /note="ShKT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DOMAIN 469..503
FT /note="ShKT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 317..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 182..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 380..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 387..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 396..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 469..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 476..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 485..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 503 AA; 56911 MW; 1E28A52ECC044B27 CRC64;
MRLLYSLFHC SAFLVGFTLS VGVLPIPNEH AASIKAKFDD YAEHYLLPED FHNAETAPVK
KPTDAEIESM QNSLLFEGDI MGVPEIEKSD ILKRLRDDPL LDEDEIFRKP FHSALNLVTY
PDKLWPEGQV PYMLEEGMTN DQRTAIAQAF DEYKTKTCVR FVPKTDDDFD YIYVKRNVAF
GCSSYVGRAG GNQTVSLEVD KCFSKGIIAH ELMHALGFFH EHSRTDRDDF VDINEDNIRP
GMMRNFEKYP RKIIDSLGMP YDYESVMHYH KLAFSRNGKP TIIPKDNEAD VGQRYKLSEM
DSKKVNKLYQ CGEYSKTSST TTTTTTTTTT TTTEEPTTTT EVEEKPKDKK VSSTTTTTKK
PTTTTTTTPK PVERSRNKKC EDLNAHCGMW EQLGHCQHSV KYMAHYCRKA CNLCEVEVTT
TTTTTPKPVP RNKEKENKSA SSTTRGTSTA TSTTPKTTTT TTSAPKEKCE DKNLFCSYWA
KIGECNSESK FMKIFCKASC GKC
