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;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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