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Protein

Zinc metalloproteinase nas-27

Gene

nas-27

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Zinc; catalyticPROSITE-ProRule annotation
Active sitei151 – 1511PROSITE-ProRule annotation
Metal bindingi154 – 1541Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi160 – 1601Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.A44.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase nas-27 (EC:3.4.24.21)
Alternative name(s):
Nematode astacin 27
Gene namesi
Name:nas-27
ORF Names:T23F4.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiT23F4.4; CE36020; WBGene00003545; nas-27.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 428411Zinc metalloproteinase nas-27PRO_0000028931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis
Disulfide bondi254 ↔ 265PROSITE-ProRule annotation
Disulfide bondi258 ↔ 276PROSITE-ProRule annotation
Disulfide bondi281 ↔ 290PROSITE-ProRule annotation
Disulfide bondi306 ↔ 339PROSITE-ProRule annotation
Disulfide bondi366 ↔ 386PROSITE-ProRule annotation
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO17264.

Interactioni

Protein-protein interaction databases

STRINGi6239.T23F4.4.

Structurei

3D structure databases

ProteinModelPortaliO17264.
SMRiO17264. Positions 71-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 29142EGF-likeAdd
BLAST
Domaini306 – 428123CUBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M12A family.Curated
Contains 1 CUB domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000018177.
InParanoidiO17264.
KOiK08076.
OMAiCCDEHIY.
OrthoDBiEOG7TQV4J.
PhylomeDBiO17264.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR000859. CUB_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR017050. Metallopeptidase_nem.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
[Graphical view]
PIRSFiPIRSF036365. Astacin_nematoda. 1 hit.
PRINTSiPR00480. ASTACIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O17264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQILPIFFPL LITSLHAIPR GRRAVRNRNE GDINSLVGVG QYLYQGDIAV
60 70 80 90 100
VKSRARRAVI RQKHKKWKLP MPYSFDRNFP SRSRQRVLEA MQFWSEKTCV
110 120 130 140 150
TFHENRYVYP HVSIFEGNGC WSFVGKQPSL REQSLSLERS CTDHTFVVAH
160 170 180 190 200
EIAHTLGFYH EHARGDRDQF ISIDYSNVNP NLTFAFAKES EKQLDHQEAA
210 220 230 240 250
YEYGSVMHYS VDQFAVNTNR PVIYARDQKF AQAMGNRMRA TFQDVSRMNV
260 270 280 290 300
LYNCHERCAN TLNRCQQGGY PAPSDCSQCV CPDGFGGNFC ETIEAHSVGQ
310 320 330 340 350
KDNSDCGGVL WASETSQTFY GAVRTRVHSN SVLPTPEHCF WHIRASQGKS
360 370 380 390 400
IEIQIKNIIS PCSMSCSFNA LELKLSNFTM TGPRFCCDEH IYNRYSQPKV
410 420
FQSEGPLAVI GAYARYDYLD FNIEYRAV
Length:428
Mass (Da):48,983
Last modified:March 1, 2004 - v2
Checksum:iC3DF49EAF6EE6E72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081745 Genomic DNA. Translation: CCD73622.1.
AJ561216 mRNA. Translation: CAD99217.1.
PIRiT32401.
RefSeqiNP_493926.2. NM_061525.3.
UniGeneiCel.14311.

Genome annotation databases

EnsemblMetazoaiT23F4.4; T23F4.4; WBGene00003545.
GeneIDi188809.
KEGGicel:CELE_T23F4.4.
UCSCiT23F4.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081745 Genomic DNA. Translation: CCD73622.1.
AJ561216 mRNA. Translation: CAD99217.1.
PIRiT32401.
RefSeqiNP_493926.2. NM_061525.3.
UniGeneiCel.14311.

3D structure databases

ProteinModelPortaliO17264.
SMRiO17264. Positions 71-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.T23F4.4.

Protein family/group databases

MEROPSiM12.A44.

Proteomic databases

PaxDbiO17264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT23F4.4; T23F4.4; WBGene00003545.
GeneIDi188809.
KEGGicel:CELE_T23F4.4.
UCSCiT23F4.4. c. elegans.

Organism-specific databases

CTDi188809.
WormBaseiT23F4.4; CE36020; WBGene00003545; nas-27.

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000018177.
InParanoidiO17264.
KOiK08076.
OMAiCCDEHIY.
OrthoDBiEOG7TQV4J.
PhylomeDBiO17264.

Miscellaneous databases

NextBioi940160.
PROiO17264.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR000859. CUB_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR017050. Metallopeptidase_nem.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
[Graphical view]
PIRSFiPIRSF036365. Astacin_nematoda. 1 hit.
PRINTSiPR00480. ASTACIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "The astacin protein family in Caenorhabditis elegans."
    Moehrlen F., Hutter H., Zwilling R.
    Eur. J. Biochem. 270:4909-4920(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 200-229, NOMENCLATURE.
    Strain: Bristol N2.

Entry informationi

Entry nameiNAS27_CAEEL
AccessioniPrimary (citable) accession number: O17264
Secondary accession number(s): Q7Z0M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2004
Last modified: May 11, 2016
This is version 108 of the entry and version 2 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.