NAS31_CAEEL
ID NAS31_CAEEL Reviewed; 611 AA.
AC Q7JLI1; Q20975; Q7Z0M2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zinc metalloproteinase nas-31;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE AltName: Full=Nematode astacin 31;
DE Flags: Precursor;
GN Name=nas-31; ORFNames=F58B4.1;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 246-296 (ISOFORMS A AND B), 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: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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q7JLI1-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q7JLI1-2; Sequence=VSP_012356, VSP_012357;
CC -!- TISSUE SPECIFICITY: Expressed in excretory cell and in amphid and
CC phasmid sheath glia. {ECO:0000269|PubMed:20109220}.
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DR EMBL; Z74038; CAE48502.1; -; Genomic_DNA.
DR EMBL; Z74038; CAA98497.2; -; Genomic_DNA.
DR EMBL; AJ561219; CAD99219.1; -; mRNA.
DR PIR; T22904; T22904.
DR RefSeq; NP_001023993.1; NM_001028822.2. [Q7JLI1-2]
DR RefSeq; NP_001023994.1; NM_001028823.3. [Q7JLI1-1]
DR AlphaFoldDB; Q7JLI1; -.
DR SMR; Q7JLI1; -.
DR STRING; 6239.F58B4.1b; -.
DR MEROPS; M12.310; -.
DR PaxDb; Q7JLI1; -.
DR EnsemblMetazoa; F58B4.1a.1; F58B4.1a.1; WBGene00003549. [Q7JLI1-2]
DR EnsemblMetazoa; F58B4.1b.1; F58B4.1b.1; WBGene00003549. [Q7JLI1-1]
DR GeneID; 186493; -.
DR KEGG; cel:CELE_F58B4.1; -.
DR UCSC; F58B4.1b; c. elegans. [Q7JLI1-1]
DR CTD; 186493; -.
DR WormBase; F58B4.1a; CE35881; WBGene00003549; nas-31. [Q7JLI1-2]
DR WormBase; F58B4.1b; CE35882; WBGene00003549; nas-31. [Q7JLI1-1]
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_5_1; -.
DR InParanoid; Q7JLI1; -.
DR OMA; FGTAAHE; -.
DR OrthoDB; 503774at2759; -.
DR PhylomeDB; Q7JLI1; -.
DR PRO; PR:Q7JLI1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003549; Expressed in larva 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:0018996; P:molting cycle, collagen and cuticulin-based cuticle; 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; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF01400; Astacin; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51670; SHKT; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..158
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442678"
FT CHAIN 159..611
FT /note="Zinc metalloproteinase nas-31"
FT /id="PRO_0000028935"
FT DOMAIN 159..354
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 340..396
FT /note="EGF-like"
FT DOMAIN 397..516
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 532..564
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 82..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 203..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 224..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 357..376
FT /evidence="ECO:0000250"
FT DISULFID 379..390
FT /evidence="ECO:0000250"
FT DISULFID 397..428
FT /evidence="ECO:0000250"
FT DISULFID 455..476
FT /evidence="ECO:0000250"
FT DISULFID 532..564
FT /evidence="ECO:0000250"
FT DISULFID 539..557
FT /evidence="ECO:0000250"
FT DISULFID 548..561
FT /evidence="ECO:0000250"
FT VAR_SEQ 540..578
FT /note="DFYKFFGMCRSKKIRSNCKFTCHDCNNNNASPFGSNFFN -> AAYAWNGFC
FT VNPFYSMQARHYYCAYTCGLCWMNNNNNFY (in isoform a)"
FT /evidence="ECO:0000303|PubMed:14653817"
FT /id="VSP_012356"
FT VAR_SEQ 579..611
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:14653817"
FT /id="VSP_012357"
SQ SEQUENCE 611 AA; 68854 MW; 9BDCE2B6B2C2780D CRC64;
MILQLLFYSL FTHLAVSQID VNQALNQNKL NIDTISSSAI SDAELEKTFP RTNLSRMRNA
LKSLRQNWSA KLQAMPARNY QNAGTNQENG ATEQQKPLRE KPRDRVKMEG DTLHQVNKAA
GLNDILYQGD MVLTDDQIAT ILEARDETTV STASRARRQA YRDRYYPSTT WGSSVYYYYD
RTATPKIVKA FEQAVAFWQN VTCINIMQSS TAINRIRVFK GQGCYSYVGR ISGVQDLSLG
TGCEEFGTAA HELGHALGFF HTQSRYDRDN YISINYANID PSYVEQFDKE TSNTNFNYGM
PYDYGSIMQY GATSASSNDK ATMIARDTEY QDTMGSDFVG FYDISMMNEH YKCKELCPAA
SSAQCKNGGF PSPRNCAICI CPSGYGGILC DQRPPGCGDS VTATTTWQTL TNTIGDGLPT
LRDNHTMCNY WVKAPDNQAV EIRISGLTTV TIDGCIFGGV EIKTHKDQKL TGYRYCSSAD
QNTVHRSTGS LVPIILFNRY ASTKAVLEYR AVTPSVDVSA TYTTFAPIVN SCQDLHPNCD
FYKFFGMCRS KKIRSNCKFT CHDCNNNNAS PFGSNFFNNN YNSFNNWYTN KNKNYYPYSN
SNNNKPWMWF F
