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NAS30_CAEEL
ID   NAS30_CAEEL             Reviewed;         741 AA.
AC   Q9N2V2; Q9N2V3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 5.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Zinc metalloproteinase nas-30;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 30;
DE   Flags: Precursor;
GN   Name=nas-30 {ECO:0000312|WormBase:Y95B8A.1a};
GN   ORFNames=Y95B8A.1 {ECO:0000312|WormBase:Y95B8A.1a};
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   IDENTIFICATION, AND NOMENCLATURE.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:Y95B8A.1a};
CC         IsoId=Q9N2V2-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:Y95B8A.1b};
CC         IsoId=Q9N2V2-2; Sequence=VSP_060783, VSP_060784;
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DR   EMBL; BX284601; CCD73542.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD73556.1; -; Genomic_DNA.
DR   RefSeq; NP_490794.1; NM_058393.4. [Q9N2V2-2]
DR   RefSeq; NP_490795.3; NM_058394.3.
DR   AlphaFoldDB; Q9N2V2; -.
DR   SMR; Q9N2V2; -.
DR   IntAct; Q9N2V2; 2.
DR   STRING; 6239.Y95B8A.1; -.
DR   MEROPS; M12.A46; -.
DR   EPD; Q9N2V2; -.
DR   PaxDb; Q9N2V2; -.
DR   PeptideAtlas; Q9N2V2; -.
DR   EnsemblMetazoa; Y95B8A.1a.1; Y95B8A.1a.1; WBGene00003548. [Q9N2V2-1]
DR   EnsemblMetazoa; Y95B8A.1b.1; Y95B8A.1b.1; WBGene00003548. [Q9N2V2-2]
DR   GeneID; 190803; -.
DR   KEGG; cel:CELE_Y95B8A.1; -.
DR   UCSC; Y95B8A.1; c. elegans. [Q9N2V2-1]
DR   UCSC; Y95B8A.2; c. elegans.
DR   CTD; 190803; -.
DR   WormBase; Y95B8A.1a; CE54010; WBGene00003548; nas-30. [Q9N2V2-1]
DR   WormBase; Y95B8A.1b; CE24691; WBGene00003548; nas-30. [Q9N2V2-2]
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00940000167997; -.
DR   HOGENOM; CLU_017286_6_0_1; -.
DR   InParanoid; Q9N2V2; -.
DR   OMA; EDYNTDF; -.
DR   OrthoDB; 681837at2759; -.
DR   PhylomeDB; Q9N2V2; -.
DR   PRO; PR:Q9N2V2; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00022383; Expressed in larva and 3 other tissues.
DR   ExpressionAtlas; Q9N2V2; baseline and differential.
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; 2.60.120.290; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000442677"
FT   CHAIN           ?..741
FT                   /note="Zinc metalloproteinase nas-30"
FT                   /id="PRO_0000028934"
FT   DOMAIN          324..516
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          539..550
FT                   /note="EGF-like"
FT   DOMAIN          550..648
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   REGION          71..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        413
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         422
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        364..515
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        385..404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        519..539
FT                   /evidence="ECO:0000250"
FT   DISULFID        541..550
FT                   /evidence="ECO:0000250"
FT   DISULFID        562..583
FT                   /evidence="ECO:0000250"
FT   DISULFID        610..630
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         114..128
FT                   /note="ADAPPVYRQPRTKAE -> GDDDDNIDMSLTRLG (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060783"
FT   VAR_SEQ         129..741
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060784"
SQ   SEQUENCE   741 AA;  80722 MW;  F5A77F7B2F19EF25 CRC64;
     MRISSLLFLT FLAGIVQAQD FLAMFKPFLG GGGGGGNPFA NPQAIGGLFQ QFAGGNGGGF
     GQLLAGAMAP KPAPAAAGPR SAPAPTNEDY NTDIDVPAPK AKARAAPTPR RAQADAPPVY
     RQPRTKAEKI ERFRNIARTF SPFVYEVNTT PAPHFDNFIW QQNAPAVTPE PFTFAPFSFP
     TLATVAPPAP GPGGPTLEPF LPTTASPKLL AHNTARMIRE IASFSDGGRS RDQDFGAVQT
     LMQAFFEAVS SGNNGGAGAA AGAGTALGDA PMLQAHRDGT ELGANRALTN KLFESDMVLT
     VKQMKAIVLA AQEARNPHGR KKRKVITGSV YRWKSVIPFR FKGGDAKWKK LIREGLGLWE
     KETCVRWSEN GPGKDYVIFF RGSGCYSSVG RTGGSQLISI GYGCEDKGIV AHEVGHSLGF
     WHEQSRPDRD DYIHLRKDWI IKGTDGNFEK RSWEEIEDMG VPYDVGSVMH YGSNAFTKDW
     DQITIETKDS RYQGTIGQRQ KLSFIDVKQV NRLYCNSVCP VALPCMHGGY PDPNNCAVCK
     CPDGLGGKLC GRAAKGTDHD KCGGELTATA EWQEMVYKGK RTCNWKVKSP SGGRVRLVLT
     ELRYQCAPAC KAYIEIKHNT DFQQTGFRVC CFNKTYDVIS DQSEALILSN ANIVDYEVSY
     KLQWIQDNGK ALPPPKPTST WVPGKENRPF RGVENSGGTI EKFILQAIPK IRDSHRPLES
     ITSIVAEYGL ATLLGISHNG K
 
 
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