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NAS9_CAEEL
ID   NAS9_CAEEL              Reviewed;         546 AA.
AC   P91137; Q8I7H6; Q95Q69;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Zinc metalloproteinase nas-9;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:A8Q2D1};
DE   AltName: Full=Nematode astacin 9;
DE   Flags: Precursor;
GN   Name=nas-9; ORFNames=C37H5.9;
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   NOMENCLATURE, AND DISRUPTION PHENOTYPE.
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: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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=b;
CC         IsoId=P91137-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=P91137-2; Sequence=VSP_012353;
CC       Name=c;
CC         IsoId=P91137-3; Sequence=VSP_012352;
CC   -!- TISSUE SPECIFICITY: Expressed in hypodermis, uterus and spermatheca.
CC       {ECO:0000269|PubMed:20109220}.
CC   -!- DISRUPTION PHENOTYPE: Defects lead to embryonic lethality in 6% of
CC       population. {ECO:0000269|PubMed:14653817}.
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DR   EMBL; FO080813; CCD66988.1; -; Genomic_DNA.
DR   EMBL; FO080813; CCD66989.1; -; Genomic_DNA.
DR   EMBL; FO080813; CCD66990.1; -; Genomic_DNA.
DR   PIR; T25615; T25615.
DR   RefSeq; NP_504293.2; NM_071892.8. [P91137-3]
DR   RefSeq; NP_741531.1; NM_171452.1. [P91137-2]
DR   RefSeq; NP_741532.1; NM_171927.1. [P91137-1]
DR   AlphaFoldDB; P91137; -.
DR   SMR; P91137; -.
DR   BioGRID; 43925; 1.
DR   STRING; 6239.C37H5.9b; -.
DR   MEROPS; M12.A22; -.
DR   EPD; P91137; -.
DR   PaxDb; P91137; -.
DR   PeptideAtlas; P91137; -.
DR   EnsemblMetazoa; C37H5.9a.1; C37H5.9a.1; WBGene00003528. [P91137-2]
DR   EnsemblMetazoa; C37H5.9b.1; C37H5.9b.1; WBGene00003528. [P91137-1]
DR   EnsemblMetazoa; C37H5.9c.1; C37H5.9c.1; WBGene00003528. [P91137-3]
DR   EnsemblMetazoa; C37H5.9c.2; C37H5.9c.2; WBGene00003528. [P91137-3]
DR   GeneID; 178875; -.
DR   KEGG; cel:CELE_C37H5.9; -.
DR   UCSC; C37H5.9c.1; c. elegans. [P91137-1]
DR   CTD; 178875; -.
DR   WormBase; C37H5.9a; CE08632; WBGene00003528; nas-9. [P91137-2]
DR   WormBase; C37H5.9b; CE29710; WBGene00003528; nas-9. [P91137-1]
DR   WormBase; C37H5.9c; CE32825; WBGene00003528; nas-9. [P91137-3]
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00970000196429; -.
DR   InParanoid; P91137; -.
DR   OMA; MHETMHA; -.
DR   OrthoDB; 567013at2759; -.
DR   PhylomeDB; P91137; -.
DR   PRO; PR:P91137; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003528; 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: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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR017368; Peptidase_M12A_astacin-9/10/11.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF01549; ShK; 1.
DR   PIRSF; PIRSF038055; Nas9/Nas10/Nas11; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..300
FT                   /evidence="ECO:0000250|UniProtKB:P13497"
FT                   /id="PRO_0000442656"
FT   CHAIN           301..546
FT                   /note="Zinc metalloproteinase nas-9"
FT                   /id="PRO_0000028914"
FT   DOMAIN          308..507
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          510..546
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        347..506
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        372..392
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        510..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        517..539
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        526..543
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012352"
FT   VAR_SEQ         395..423
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_012353"
SQ   SEQUENCE   546 AA;  60977 MW;  EAB496C2E69AA476 CRC64;
     MIFLLFVVFP FVYAQLLPEL LAGFQNGRFR GGPDGFNRGP GGFHRGPDGF GGDPRGGVDL
     GHLIGNIAAN VGQEMGLNDA DVIGDLRGIS RGPRPSSMEW GRRARHFCRR YPGHPKCQRG
     QLPQFTDVPT IINTIIYNAG DLLPRVPTLN IHDPLAGLNS ELVGFIKSLQ SQFGQLSSQQ
     RNEIHDSCRS FKCDQQSPQN TQAKQELLTK MLAFDQAVGG KAAPAHDKVN LRFDRTQQVK
     QALLKRANLS HIIVPADNGV FDRDVLLTEH QANFLLNELG EAGRGADVGA GGGGGGRVPR
     SGVFFQESAV QKWDIWKPIQ YTLDDSLEES DKKDIRDALH EISINTCILF RYNATPKGYH
     LNYMKVDSTT FCGLSYVGRT DPANPIYLSF QCGDNRGVAM HETMHALGVS HQHLRLDRDK
     YIKIDWSNID PQHYDTFAIS DAKLYTSYGT KYAYDSIMHY NAYLGAKDPN KPTMIPLVNP
     QENTPKLGQR AKLTRGDIRL LKKMYCRPGC DDQNVHCGTW ALHGYCKMKE QMKWMNENCK
     ASCDKC
 
 
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