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Q18581 (ACN1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive angiotensin-converting enzyme-related protein
Alternative name(s):
ACE-like non-metallopeptidase protein 1
Gene names
Name:acn-1
ORF Names:C42D8.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for larval molting, male tail development, and formation of adult alae. Inactive as a metallopeptidase, due to a lack of active site residues. Ref.2

Tissue specificity

Expressed in embryonic and larval hypodermis, in the vulva during organogenesis, and in the ray papillae of the male tail. Ref.2

Sequence similarities

Belongs to the peptidase M2 family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmembrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetallopeptidase activity

Inferred from electronic annotation. Source: InterPro

peptidyl-dipeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q18581-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform b (identifier: Q18581-2)

The sequence of this isoform differs from the canonical sequence as follows:
     160-197: SSNYWKTDNL...YEAEAIKVLR → LTLNHFSSTT...TEKELHSLCS
     198-773: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 906887Inactive angiotensin-converting enzyme-related protein
PRO_0000028567

Regions

Compositional bias24 – 9370Pro-rich

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...) Ref.3 Ref.4
Glycosylation6531N-linked (GlcNAc...) Ref.4

Natural variations

Alternative sequence160 – 19738SSNYW…IKVLR → LTLNHFSSTTSHSSTGSAIP MKSIRLLLDGTEKELHSLCS in isoform b.
VSP_015490
Alternative sequence198 – 773576Missing in isoform b.
VSP_015491

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 50B3CD37EA62CBD3

FASTA906100,725
        10         20         30         40         50         60 
MKFHILLLLL VGACLPVFTQ EIKPKPELLP ADEAPKDPEA VFSEGEPFEL TDALDTPKNG 

        70         80         90        100        110        120 
SVPVPEPEPK PEPEPEPEPK PEPEPSPTPE PEPAIKFDNI ESEDYGDVAE TAASTQPDEL 

       130        140        150        160        170        180 
NTEVIEQLVD TFLNTGSIAS NKTNKGPVFA NPVAQALVNS SNYWKTDNLQ APGSIKDEEK 

       190        200        210        220        230        240 
LRSWLAGYEA EAIKVLREVA LSGWRYFNDA SPSLKLALDE AENVLTMFVR STSMQAKQFD 

       250        260        270        280        290        300 
MASVTDEKVM RQLGYVSFEG MSALAPSRFA DYSQAQAALN RDSKDSTICD KDVPPPCALQ 

       310        320        330        340        350        360 
KIDMDSIFRN EKDASRLQHL WVSYVTAIAK SKPSYNNIIT ISNEGAKLNG FANGGAMWRS 

       370        380        390        400        410        420 
AFDMSSKVHK AEFDLNKQID KIYSTIQPFY QLLHAYMRRQ LAGIYSNPVG LSKDGPIPAH 

       430        440        450        460        470        480 
LFGSLDGGDW SAHYEQTKPF EEESETPEAM LSAFNTQNYT TKKMFVTAYR YFKSAGFPHL 

       490        500        510        520        530        540 
PKSYWTSSIF ARVWSKDMIC HPAAALDMRA PNDFRVKACA QLGEPDFEQA HSLLVQTYYQ 

       550        560        570        580        590        600 
YLYKDQSLLF REQASPVITD AIANAFAHLS TNPHYLYSQK LVPSEHLDIK DSVIINKLYK 

       610        620        630        640        650        660 
ESLESFTKLP FTIAADNWRY ELFDGTVPKN KLNDRWWEIR NKYEGVRSPQ PYNTSNLDAL 

       670        680        690        700        710        720 
IHNSVSQVHS PATRTLISYV LKFQILKALC PEGTILSEGC ILSEDTTEKL RETMKLGSSI 

       730        740        750        760        770        780 
TWLKALEMIS GKGELDAQPL LEYYEPLINW LRNTNEIDQV VVGWDGEGTP FTVEEIPKTR 

       790        800        810        820        830        840 
QPGDGGNGLP SEDRVAFPGG ECVNGQECLL DSHCNGTICV CNDGLYTLEI GNTFNCVPGN 

       850        860        870        880        890        900 
PADSGFGDGK GGLVIGLFNN EVTTPEPSAE PEPTAKTTTK MPPRVRAATS PFSLYLTVLL 


IIYFAL 

« Hide

Isoform b [UniParc].

Checksum: DF2528B20E9D6CF6
Show »

FASTA33235,399

References

« Hide 'large scale' references
[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], ALTERNATIVE SPLICING.
Strain: Bristol N2.
[2]"An essential role in molting and morphogenesis of Caenorhabditis elegans for ACN-1, a novel member of the angiotensin-converting enzyme family that lacks a metallopeptidase active site."
Brooks D.R., Appleford P.J., Murray L., Isaac R.E.
J. Biol. Chem. 278:52340-52346(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[3]"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
[4]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159 AND ASN-653, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080659 Genomic DNA. Translation: CCD65566.1.
FO080659 Genomic DNA. Translation: CCD65567.1.
PIRT15792.
RefSeqNP_001024453.1. NM_001029282.3. [Q18581-1]
NP_001024454.1. NM_001029283.3. [Q18581-2]
UniGeneCel.38713.

3D structure databases

ProteinModelPortalQ18581.
SMRQ18581. Positions 177-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ18581. 1 interaction.
MINTMINT-3385438.
STRING6239.C42D8.5a.

Proteomic databases

PaxDbQ18581.
PRIDEQ18581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC42D8.5a; C42D8.5a; WBGene00000039. [Q18581-1]
GeneID180780.
KEGGcel:CELE_C42D8.5.
UCSCC42D8.5b.1. c. elegans. [Q18581-1]

Organism-specific databases

CTD180780.
WormBaseC42D8.5a; CE30627; WBGene00000039; acn-1.
C42D8.5b; CE37212; WBGene00000039; acn-1.

Phylogenomic databases

eggNOGNOG71044.
GeneTreeENSGT00520000055576.
HOGENOMHOG000020340.
InParanoidQ18581.
KOK01283.
OMARDGANEG.
PhylomeDBQ18581.

Family and domain databases

InterProIPR006149. EB_dom.
IPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01683. EB. 1 hit.
PF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
ProtoNetSearch...

Other

NextBio910922.
PROQ18581.

Entry information

Entry nameACN1_CAEEL
AccessionPrimary (citable) accession number: Q18581
Secondary accession number(s): Q65ZH6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase