NAS36_CAEBR
ID NAS36_CAEBR Reviewed; 616 AA.
AC Q61EX6; A8XE85;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Zinc metalloproteinase nas-36;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:D5FM38};
DE AltName: Full=Nematode astacin 36;
DE Flags: Precursor;
GN Name=nas-36 {ECO:0000250|UniProtKB:Q18206}; ORFNames=CBG11886;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Mtalloprotease. Involved in molting, a process during larval
CC stages in which a new cuticle is formed and the old cuticle is shed.
CC {ECO:0000250|UniProtKB:D5FM38, ECO:0000250|UniProtKB:Q18206}.
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:0000255}.
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DR EMBL; HE601268; CAP30957.2; -; Genomic_DNA.
DR AlphaFoldDB; Q61EX6; -.
DR SMR; Q61EX6; -.
DR STRING; 6238.CBG11886; -.
DR MEROPS; M12.319; -.
DR PRIDE; Q61EX6; -.
DR EnsemblMetazoa; CBG11886.1; CBG11886.1; WBGene00032925.
DR WormBase; CBG11886; CBP28845; WBGene00032925; Cbr-nas-36.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_3_1; -.
DR InParanoid; Q61EX6; -.
DR OMA; GQGCYSM; -.
DR OrthoDB; 681837at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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; cd00041; CUB; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.20.100.10; -; 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; IPR017050; Metallopeptidase_nem.
DR InterPro; IPR033957; NAS-36.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10127:SF849; PTHR10127:SF849; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..125
FT /evidence="ECO:0000250|UniProtKB:P13497"
FT /id="PRO_0000442248"
FT CHAIN 126..616
FT /note="Zinc metalloproteinase nas-36"
FT /id="PRO_0000045126"
FT DOMAIN 126..321
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 316..357
FT /note="EGF-like"
FT DOMAIN 367..481
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 506..555
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 168..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 191..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 324..345
FT /evidence="ECO:0000250"
FT DISULFID 347..356
FT /evidence="ECO:0000250"
FT DISULFID 367..396
FT /evidence="ECO:0000250"
FT DISULFID 424..444
FT /evidence="ECO:0000250"
FT DISULFID 518..549
FT /evidence="ECO:0000250"
FT DISULFID 522..554
FT /evidence="ECO:0000250"
FT DISULFID 534..539
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 69517 MW; 4211D810EEC52952 CRC64;
MRRFCRLLFL NSLLSISICK AQNPAHLVAD EFKEHFNVEE KQLETVEELL LKMKKLAHSR
SFAGREFGHD AVEDSKKEVA ISTQQGTIDK KVSPFLFEGD IFLSRRQAVD ILKALSKDKT
KRLRRSFVSD KTATWKSLPI KYRFHESIDF YTISQIIAAI RFWEDSTCIT FENVSDAPVG
DYIEFFSGQG CYSMIGRNGG RQGISIGESC VKMGVIEHEI GHALGLWHEQ SRPDALGYVS
IERDFILPSY ISDFLQRDDE IDTLGIPYDL GSVMHYGSTA FSVDQKSKTV VTRDSLYQQT
IGQREKLSFY DVATINTAYC KEECKSEKTE CEYGGYMRPS KCSECLCPDG LGGEKCEKNE
DAKNAECGGI LELSDEWKTI ESPNYPDPGY EADQKCSWLL KAPKGKRVEI EFIEDFSFLC
TSTCVDFVEL KISDDLRNTG FRFCCYDKPE ISFVSQIDTA IVIFRSQLSA DIGFKIQVRS
TESEPRTTIA PTIITTTMAP ITVDTPNVWA DWGEWSMCSR TCGGCGIRSR VRSCRSKKCE
GRRQEFGTCN LKACPVDKHC AKLLSNNRLC NGKVCTKNDI AISSCDAPQC CPPFVNVDGM
CQSDQENHHD ELWLSI
