NAS11_CAEEL
ID NAS11_CAEEL Reviewed; 579 AA.
AC Q21432; Q65ZJ6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc metalloproteinase nas-11;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 11;
DE Flags: Precursor;
GN Name=nas-11; ORFNames=K11G12.1;
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], AND ALTERNATIVE SPLICING.
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 NOMENCLATURE, AND DISRUPTION PHENOTYPE.
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q21432-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q21432-2; Sequence=VSP_012354, VSP_012355;
CC -!- TISSUE SPECIFICITY: Expressed in the anterior part of the intestine,
CC CEP neurons and to a lesser extent in hypodermis.
CC {ECO:0000269|PubMed:20109220}.
CC -!- DISRUPTION PHENOTYPE: Defects lead to retarded growth.
CC {ECO:0000269|PubMed:14653817}.
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DR EMBL; FO081325; CCD70792.1; -; Genomic_DNA.
DR EMBL; FO081325; CCD70793.1; -; Genomic_DNA.
DR PIR; T16617; T16617.
DR RefSeq; NP_001024789.1; NM_001029618.4. [Q21432-1]
DR RefSeq; NP_001024790.1; NM_001029619.5. [Q21432-2]
DR AlphaFoldDB; Q21432; -.
DR SMR; Q21432; -.
DR BioGRID; 45867; 2.
DR DIP; DIP-24488N; -.
DR STRING; 6239.K11G12.1a; -.
DR MEROPS; M12.A36; -.
DR iPTMnet; Q21432; -.
DR EPD; Q21432; -.
DR PaxDb; Q21432; -.
DR PeptideAtlas; Q21432; -.
DR EnsemblMetazoa; K11G12.1a.1; K11G12.1a.1; WBGene00003530. [Q21432-1]
DR EnsemblMetazoa; K11G12.1b.1; K11G12.1b.1; WBGene00003530. [Q21432-2]
DR GeneID; 180938; -.
DR KEGG; cel:CELE_K11G12.1; -.
DR UCSC; K11G12.1b; c. elegans. [Q21432-1]
DR CTD; 180938; -.
DR WormBase; K11G12.1a; CE36313; WBGene00003530; nas-11. [Q21432-1]
DR WormBase; K11G12.1b; CE37260; WBGene00003530; nas-11. [Q21432-2]
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_030134_0_0_1; -.
DR InParanoid; Q21432; -.
DR OMA; FITINWS; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q21432; -.
DR PRO; PR:Q21432; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003530; Expressed in adult organism and 2 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; IPR017368; Peptidase_M12A_astacin-9/10/11.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 1.
DR PIRSF; PIRSF038055; Nas9/Nas10/Nas11; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
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..328
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442658"
FT CHAIN 329..579
FT /note="Zinc metalloproteinase nas-11"
FT /id="PRO_0000028915"
FT DOMAIN 329..536
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 539..575
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 35..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 375..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 401..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 539..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 546..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 555..572
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT VAR_SEQ 400..455
FT /note="FCGLSYVGRADPANPVYLSFGCDNNKGVAIHETMHALGVAHQHLRNDRDQFI
FT TINW -> LTKELQFMKQCMRSELPISTFAMIVINLLLLIGVTLIHNNTMHLLWWIQNC
FT TLHTE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012354"
FT VAR_SEQ 456..579
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012355"
SQ SEQUENCE 579 AA; 65031 MW; 2E98DC8E8AAAB744 CRC64;
MTPSLVFLIV VIVVVEGQGW RPWDRFNHPG NFGNWGGNNW GTRQRNQEPH DIPPPVPPPG
FRGNNDRFGG NIIKVVEIID LGKSKNRGDI LSDFKDVHKK HRHLGRKEWK GKVKQFCHRF
PGHPNCRRGK VPDQKELEEM IGQFSKGGIG RFLKRVPKIY IEDPLARVDP KLKGFLENAG
RGFGHVSSEH VNKLRDICKR RKCREQPESA KKTRELFTQK LADFETKIAG KDKTDSVQLR
FDRTLQIKEA LLEKGNLTAD IVPVDNGVYD LDTMLTEEQA NILLNELNKA GVGDDEIPLP
DADTDDEDDD DSTNSASGAA PGSSRLKKSA LYFEGNLIKK WDPSSPIRYV LDSSLEDLDK
NDVRAAIYEI EKNTCIRFKE LSSPPTGSHI VYYKVDSPTF CGLSYVGRAD PANPVYLSFG
CDNNKGVAIH ETMHALGVAH QHLRNDRDQF ITINWSNIDP QQYDAFVVVD SKLYTSYGVK
YAYDSIMHYN GYTAAQNIAI PTMNPKTNSA VNLKVLGQRQ KMGTTDIELL KKMYCQPGCD
DKNVYCGAWA LKDLCKNPGH DQYMAANCKK SCGLCAIGK
