GenomeNet

Database: UniProt
Entry: Q7JLI1
LinkDB: Q7JLI1
Original site: Q7JLI1 
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   16-JAN-2019, entry version 110.
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
RP   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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 246-296 (ISOFORMS A AND B), AND
RP   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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in excretory cell and in amphid and
CC       phasmid sheath glia. {ECO:0000269|PubMed:20109220}.
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   UniGene; Cel.3339; -.
DR   ProteinModelPortal; Q7JLI1; -.
DR   STRING; 6239.F58B4.1b; -.
DR   MEROPS; M12.310; -.
DR   PaxDb; Q7JLI1; -.
DR   EnsemblMetazoa; F58B4.1a; F58B4.1a; WBGene00003549. [Q7JLI1-2]
DR   EnsemblMetazoa; F58B4.1b; F58B4.1b; 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   eggNOG; ENOG410ZPX7; LUCA.
DR   HOGENOM; HOG000018829; -.
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 3 organ(s), highest expression level in material anatomical entity.
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   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;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   PROPEP       18    158       {ECO:0000250|UniProtKB:P13497}.
FT                                /FTId=PRO_0000442678.
FT   CHAIN       159    611       Zinc metalloproteinase nas-31.
FT                                /FTId=PRO_0000028935.
FT   DOMAIN      159    354       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      340    396       EGF-like.
FT   DOMAIN      397    516       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      532    564       ShKT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01005}.
FT   COMPBIAS    176    179       Poly-Tyr.
FT   ACT_SITE    252    252       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       251    251       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       255    255       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       261    261       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD     53     53       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     67     67       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    424    424       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    203    353       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    224    243       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    357    376       {ECO:0000250}.
FT   DISULFID    379    390       {ECO:0000250}.
FT   DISULFID    397    428       {ECO:0000250}.
FT   DISULFID    455    476       {ECO:0000250}.
FT   DISULFID    532    564       {ECO:0000250}.
FT   DISULFID    539    557       {ECO:0000250}.
FT   DISULFID    548    561       {ECO:0000250}.
FT   VAR_SEQ     540    578       DFYKFFGMCRSKKIRSNCKFTCHDCNNNNASPFGSNFFN
FT                                -> AAYAWNGFCVNPFYSMQARHYYCAYTCGLCWMNNNNNF
FT                                Y (in isoform a).
FT                                {ECO:0000303|PubMed:14653817}.
FT                                /FTId=VSP_012356.
FT   VAR_SEQ     579    611       Missing (in isoform a).
FT                                {ECO:0000303|PubMed:14653817}.
FT                                /FTId=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
//
DBGET integrated database retrieval system