NAS39_CAEEL
ID NAS39_CAEEL Reviewed; 951 AA.
AC Q20176;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc metalloproteinase nas-39;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 39;
DE Flags: Precursor;
GN Name=nas-39; ORFNames=F38E9.2;
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 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).
RN [3]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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, vulva and body wall
CC muscles, intestine and several neurons. {ECO:0000269|PubMed:20109220}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:20109220}.
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DR EMBL; FO081327; CCD70820.1; -; Genomic_DNA.
DR PIR; T30018; T30018.
DR RefSeq; NP_510672.2; NM_078271.4.
DR AlphaFoldDB; Q20176; -.
DR SMR; Q20176; -.
DR STRING; 6239.F38E9.2; -.
DR MEROPS; M12.A24; -.
DR PaxDb; Q20176; -.
DR EnsemblMetazoa; F38E9.2.1; F38E9.2.1; WBGene00003555.
DR EnsemblMetazoa; F38E9.2.2; F38E9.2.2; WBGene00003555.
DR UCSC; F38E9.2; c. elegans.
DR WormBase; F38E9.2; CE30977; WBGene00003555; nas-39.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000167878; -.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; Q20176; -.
DR OMA; VWKIMVS; -.
DR OrthoDB; 170905at2759; -.
DR PhylomeDB; Q20176; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q20176; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003555; Expressed in embryo and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 4.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 2.60.120.290; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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 InterPro; IPR034036; ZnMP_TLD/BMP1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 4.
DR Pfam; PF07645; EGF_CA; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000442685"
FT CHAIN ?..951
FT /note="Zinc metalloproteinase nas-39"
FT /id="PRO_0000028943"
FT DOMAIN 48..247
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 249..381
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 382..499
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 499..539
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 542..648
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 648..688
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 692..804
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 805..923
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 918..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 111..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 113..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 249..268
FT /evidence="ECO:0000250"
FT DISULFID 382..408
FT /evidence="ECO:0000250"
FT DISULFID 435..462
FT /evidence="ECO:0000250"
FT DISULFID 503..514
FT /evidence="ECO:0000250"
FT DISULFID 510..523
FT /evidence="ECO:0000250"
FT DISULFID 525..538
FT /evidence="ECO:0000250"
FT DISULFID 542..568
FT /evidence="ECO:0000250"
FT DISULFID 596..610
FT /evidence="ECO:0000250"
FT DISULFID 652..663
FT /evidence="ECO:0000250"
FT DISULFID 659..672
FT /evidence="ECO:0000250"
FT DISULFID 674..687
FT /evidence="ECO:0000250"
FT DISULFID 692..718
FT /evidence="ECO:0000250"
FT DISULFID 745..767
FT /evidence="ECO:0000250"
FT DISULFID 805..835
FT /evidence="ECO:0000250"
FT DISULFID 863..886
FT /evidence="ECO:0000250"
SQ SEQUENCE 951 AA; 107534 MW; B5D2A0B258163613 CRC64;
MRFSANIAII VNIIFLFIVV EFVLPTFIRS GDVRFRRYYR NNGRVSRAAT AKKERIWPEG
IIPFVIASNF SGEHQHLFLR AMRHWENFTC VSFVPRQPHH KHYITFTVDK CGCCSYVGRR
GEGPQAISIG KNCDKFGIVV HELGHVVGFW HEHTRPDRDM YVDIFYKSIQ TGQDYNFEKS
KPEEVDSLGE PYDFSSIMHY ARDTFSRGAF YDTILPKPNS GFRLEIGQRV QLSEGDIRQT
KKLYKCAECG GTLMQESGNL AIQHAGVCTW HIISPQGHTI FLNITGGLKL IIMIIFLTDE
KLEDLTEIFK PNILKKNQTY LHWKTFLIYY TNSFFHFEIL DRICGGDSLF RTIASSGNRM
LIQVRSSTPA ASLPFATYYA ICGGPIYANE GVIHSPKYPE SYPPNSDCQW TIHVDENSQV
AIEFVYFHLE QHKECIYDRL ILTEGISKNS KKDGKEMSET FCGLIEKKTI VSKTNQISLR
FFSDNSVQKT GFELRFTKEL NECATDKNIC HHYCVNTVGG FKCACRVGYS LSSNGFSCDS
TCGGYLKASN GSISSPNFPE MYPNSKTCIW EIEAPDGYHI FLNFTKFNVE GMKTECAYDY
VKIGDSEKLC GEYHEALLFT TPRNRVRIEF SSDSSVERDG FFANFIADFD ECQNDNAGCE
HTCQNRLGSY VCTCNPGYIL AEDKHNCKEG SCFFEVNAPA GDINSPNYPN DYPKGQNCSW
HFVTTPGHRL MLTFSSFQVE EHAQCKYDAV SVYDGGDGSA QLAGVFCGLA PPPLLLSSSN
ELYLTFSSDA SVSRRGFQAH YTSLCGGRLT AESTPGHIYS HATFSDSKYG KNQDCSWIVR
AKSPGRGVRI QFSTFNIESE EGCQYDYIEI YDGPEATLER LVGRFCGDTS PEVITSTGPE
LLLIMHTDNA EEEKGFVAEY REAPRSSSTK RTFVSKTRHS PLEEPIHDRN E
