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Protein

Zinc metalloproteinase nas-39

Gene

nas-39

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Probable metalloprotease.By similarity

Catalytic activityi

Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi141Zinc; catalyticPROSITE-ProRule annotation1
Active sitei142PROSITE-ProRule annotation1
Metal bindingi145Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi151Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CEL-1474228. Degradation of the extracellular matrix.
R-CEL-1650814. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

MEROPSiM12.A24.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase nas-39 (EC:3.4.24.21)
Alternative name(s):
Nematode astacin 39
Gene namesi
Name:nas-39
ORF Names:F38E9.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF38E9.2; CE30977; WBGene00003555; nas-39.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000002894331 – 951Zinc metalloproteinase nas-39Add BLAST921

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi69N-linked (GlcNAc...)Sequence analysis1
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi249 ↔ 268By similarity
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Glycosylationi317N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi382 ↔ 408By similarity
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi503 ↔ 514By similarity
Disulfide bondi510 ↔ 523By similarity
Disulfide bondi525 ↔ 538By similarity
Disulfide bondi542 ↔ 568By similarity
Glycosylationi550N-linked (GlcNAc...)Sequence analysis1
Glycosylationi583N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi596 ↔ 610By similarity
Disulfide bondi652 ↔ 663By similarity
Disulfide bondi659 ↔ 672By similarity
Disulfide bondi674 ↔ 687By similarity
Disulfide bondi692 ↔ 718By similarity
Glycosylationi717N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi745 ↔ 767By similarity
Disulfide bondi805 ↔ 835By similarity
Disulfide bondi863 ↔ 886By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ20176.

Expressioni

Gene expression databases

BgeeiWBGene00003555.

Interactioni

Protein-protein interaction databases

STRINGi6239.F38E9.2.

Structurei

3D structure databases

ProteinModelPortaliQ20176.
SMRiQ20176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini249 – 381CUB 1PROSITE-ProRule annotationAdd BLAST133
Domaini382 – 499CUB 2PROSITE-ProRule annotationAdd BLAST118
Domaini499 – 539EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini542 – 648CUB 3PROSITE-ProRule annotationAdd BLAST107
Domaini648 – 688EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini692 – 804CUB 4PROSITE-ProRule annotationAdd BLAST113
Domaini805 – 923CUB 5PROSITE-ProRule annotationAdd BLAST119

Sequence similaritiesi

Belongs to the peptidase M12A family.Curated
Contains 5 CUB domains.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOGENOMiHOG000236339.
InParanoidiQ20176.
KOiK08076.
OMAiGHFCGYD.
OrthoDBiEOG091G009U.
PhylomeDBiQ20176.

Family and domain databases

CDDicd00041. CUB. 4 hits.
Gene3Di2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProiIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF00431. CUB. 4 hits.
PF07645. EGF_CA. 1 hit.
[Graphical view]
PIRSFiPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSiPR00480. ASTACIN.
SMARTiSM00042. CUB. 5 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 6 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01180. CUB. 5 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q20176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFSANIAII VNIIFLFIVV EFVLPTFIRS GDVRFRRYYR NNGRVSRAAT
60 70 80 90 100
AKKERIWPEG IIPFVIASNF SGEHQHLFLR AMRHWENFTC VSFVPRQPHH
110 120 130 140 150
KHYITFTVDK CGCCSYVGRR GEGPQAISIG KNCDKFGIVV HELGHVVGFW
160 170 180 190 200
HEHTRPDRDM YVDIFYKSIQ TGQDYNFEKS KPEEVDSLGE PYDFSSIMHY
210 220 230 240 250
ARDTFSRGAF YDTILPKPNS GFRLEIGQRV QLSEGDIRQT KKLYKCAECG
260 270 280 290 300
GTLMQESGNL AIQHAGVCTW HIISPQGHTI FLNITGGLKL IIMIIFLTDE
310 320 330 340 350
KLEDLTEIFK PNILKKNQTY LHWKTFLIYY TNSFFHFEIL DRICGGDSLF
360 370 380 390 400
RTIASSGNRM LIQVRSSTPA ASLPFATYYA ICGGPIYANE GVIHSPKYPE
410 420 430 440 450
SYPPNSDCQW TIHVDENSQV AIEFVYFHLE QHKECIYDRL ILTEGISKNS
460 470 480 490 500
KKDGKEMSET FCGLIEKKTI VSKTNQISLR FFSDNSVQKT GFELRFTKEL
510 520 530 540 550
NECATDKNIC HHYCVNTVGG FKCACRVGYS LSSNGFSCDS TCGGYLKASN
560 570 580 590 600
GSISSPNFPE MYPNSKTCIW EIEAPDGYHI FLNFTKFNVE GMKTECAYDY
610 620 630 640 650
VKIGDSEKLC GEYHEALLFT TPRNRVRIEF SSDSSVERDG FFANFIADFD
660 670 680 690 700
ECQNDNAGCE HTCQNRLGSY VCTCNPGYIL AEDKHNCKEG SCFFEVNAPA
710 720 730 740 750
GDINSPNYPN DYPKGQNCSW HFVTTPGHRL MLTFSSFQVE EHAQCKYDAV
760 770 780 790 800
SVYDGGDGSA QLAGVFCGLA PPPLLLSSSN ELYLTFSSDA SVSRRGFQAH
810 820 830 840 850
YTSLCGGRLT AESTPGHIYS HATFSDSKYG KNQDCSWIVR AKSPGRGVRI
860 870 880 890 900
QFSTFNIESE EGCQYDYIEI YDGPEATLER LVGRFCGDTS PEVITSTGPE
910 920 930 940 950
LLLIMHTDNA EEEKGFVAEY REAPRSSSTK RTFVSKTRHS PLEEPIHDRN

E
Length:951
Mass (Da):107,534
Last modified:October 1, 2002 - v3
Checksum:iB5D2A0B258163613
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081327 Genomic DNA. Translation: CCD70820.1.
PIRiT30018.
RefSeqiNP_510672.2. NM_078271.4.
UniGeneiCel.8940.

Genome annotation databases

EnsemblMetazoaiF38E9.2; F38E9.2; WBGene00003555.
GeneIDi3565986.
KEGGicel:CELE_F38E9.2.
UCSCiF38E9.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081327 Genomic DNA. Translation: CCD70820.1.
PIRiT30018.
RefSeqiNP_510672.2. NM_078271.4.
UniGeneiCel.8940.

3D structure databases

ProteinModelPortaliQ20176.
SMRiQ20176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F38E9.2.

Protein family/group databases

MEROPSiM12.A24.

Proteomic databases

PaxDbiQ20176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF38E9.2; F38E9.2; WBGene00003555.
GeneIDi3565986.
KEGGicel:CELE_F38E9.2.
UCSCiF38E9.2. c. elegans.

Organism-specific databases

CTDi3565986.
WormBaseiF38E9.2; CE30977; WBGene00003555; nas-39.

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOGENOMiHOG000236339.
InParanoidiQ20176.
KOiK08076.
OMAiGHFCGYD.
OrthoDBiEOG091G009U.
PhylomeDBiQ20176.

Enzyme and pathway databases

ReactomeiR-CEL-1474228. Degradation of the extracellular matrix.
R-CEL-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

PROiQ20176.

Gene expression databases

BgeeiWBGene00003555.

Family and domain databases

CDDicd00041. CUB. 4 hits.
Gene3Di2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProiIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF00431. CUB. 4 hits.
PF07645. EGF_CA. 1 hit.
[Graphical view]
PIRSFiPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSiPR00480. ASTACIN.
SMARTiSM00042. CUB. 5 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 6 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01180. CUB. 5 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNAS39_CAEEL
AccessioniPrimary (citable) accession number: Q20176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.