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Protein

Endothelin-converting enzyme 2

Gene

Ece2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May limit beta-amyloid peptide accumulation in brain. May also have methyltransferase activity.1 Publication

Catalytic activityi

Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301S-adenosyl-L-homocysteineBy similarity
Binding sitei41 – 411S-adenosyl-L-homocysteine; via amide nitrogenBy similarity
Binding sitei66 – 661S-adenosyl-L-homocysteine; via carbonyl oxygenBy similarity
Binding sitei130 – 1301S-adenosyl-L-homocysteineBy similarity
Metal bindingi718 – 7181Zinc; catalyticBy similarity
Active sitei719 – 7191By similarity
Metal bindingi722 – 7221Zinc; catalyticBy similarity
Metal bindingi778 – 7781Zinc; catalyticBy similarity
Active sitei782 – 7821Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Methyltransferase, Protease, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM13.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelin-converting enzyme 2
Short name:
ECE-2
Including the following 2 domains:
Methyltransferase-like region (EC:2.1.1.-)
Endothelin-converting enzyme 2 region (EC:3.4.24.71)
Gene namesi
Name:Ece2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1101356. Ece2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 178178CytoplasmicSequence analysisAdd
BLAST
Transmembranei179 – 19921HelicalSequence analysisAdd
BLAST
Topological domaini200 – 881682LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic vesicle membrane Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are fertile and healthy, and do not display any abnormality in terms of growth or aging. However, they have elevated concentrations of beta-amyloid-40 and beta-amyloid-42 in brain.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881Endothelin-converting enzyme 2PRO_0000310760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphotyrosineBy similarity
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence analysis
Isoform 2 (identifier: Q80Z60-2)
Modified residuei174 – 1741PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ80Z60.
MaxQBiQ80Z60.
PaxDbiQ80Z60.
PeptideAtlasiQ80Z60.
PRIDEiQ80Z60.

PTM databases

iPTMnetiQ80Z60.
PhosphoSiteiQ80Z60.

Expressioni

Tissue specificityi

Expressed at high levels in central nervous system. Expressed in adrenal glands, ovary and uterus, and at low levels in heart.1 Publication

Developmental stagei

Weakly expressed in mesenchyme and parts of neural tube at E10.5. At E13.5, expressed in anterior part of neural tube, dorsal root ganglia, bilateral sympathetic trunk and heart.1 Publication

Gene expression databases

BgeeiQ80Z60.
CleanExiMM_ECE2.
ExpressionAtlasiQ80Z60. baseline and differential.
GenevisibleiQ80Z60. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113475.

Structurei

3D structure databases

ProteinModelPortaliQ80Z60.
SMRiQ80Z60. Positions 20-161, 212-881.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 160160Methyltransferase-like regionAdd
BLAST
Regioni88 – 892S-adenosyl-L-homocysteine bindingBy similarity
Regioni113 – 1142S-adenosyl-L-homocysteine bindingBy similarity
Regioni200 – 881682Endothelin-converting enzyme 2 regionAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily.Curated
In the C-terminal section; belongs to the peptidase M13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2352. Eukaryota.
KOG3624. Eukaryota.
COG3590. LUCA.
GeneTreeiENSGT00760000119162.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ80Z60.
KOiK01415.
PhylomeDBiQ80Z60.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
3.40.50.150. 1 hit.
InterProiIPR029733. ECE2.
IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF127. PTHR11733:SF127. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80Z60-1) [UniParc]FASTAAdd to basket

Also known as: ECE-2a-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.

« Hide

        10         20         30         40         50
MASPRTPVSP PELPEKNFQY RQVQYWDQRY KDAADSGPYE WFGDFASFRA
60 70 80 90 100
LLEPELCPED RILVLGCGNS ALSYELFLGG FPNVTSVDYS PVVVAAMQVR
110 120 130 140 150
YAHVPSLRWE TMDVRALDFP SGSFDVVLEK GTLDAMLAGE PDPWNVSSEG
160 170 180 190 200
VHTVDQVLSE VGFQKRTRQL FGSHTQLELV LAGLILVLAA LLLGCLVALW
210 220 230 240 250
VHRDPAHSTC VTEACIRVAG KILESLDRGV SPCQDFYQFS CGGWIRRNPL
260 270 280 290 300
PNGRSRWNTF NSLWDQNQAI LKHLLENTTF NSSSEAERKT RSFYLSCLQS
310 320 330 340 350
ERIEKLGAKP LRDLIDKIGG WNITGPWDED SFMDVLKAVA GTYRATPFFT
360 370 380 390 400
VYVSADSKRS YSNITQVDQS GLFLPSRDYY LNRTANEKVL TAYLDYMVEL
410 420 430 440 450
GVLLGGQPTS TREQMQQVLE LEIQLANITV PQDQRRDEEK IYHKMSISEL
460 470 480 490 500
QALAPAVDWL EFLSFLLSPL ELGDSEPVVV YGMSYLQQVS ELINRTEPSI
510 520 530 540 550
LNNYLIWNLV QKTTSSLDQR FETAQEKLLE TLYGTKKSCT PRWQTCISNT
560 570 580 590 600
DDALGFALGS LFVKATFDRQ SKEIAEGMIN EIRSAFEETL GDLVWMDEKT
610 620 630 640 650
RLAAKEKADA IYDMIGFPDF ILEPKELDDV YYGYEVSEDS FFQNMLNLYN
660 670 680 690 700
FSAKVMADQL RKPPSRDQWS MTPQTVNAYY LPTKNEIVFP AGILQPPFYA
710 720 730 740 750
HNHPKALNFG GIGVVMDHEL THAFDDQGRE YDKEGNLRPW WQNESLTAFQ
760 770 780 790 800
NHTACMEEQY SQYQVNGERL NGLQTLGENI ADNGGLKAAY NAYKAWLRKH
810 820 830 840 850
GEEQPLPAVG LTNHQLFFVG FAQVWCSVRT PESSHEGLVT DPHSPARFRV
860 870 880
LGTLSNSRDF LRHFGCPVGS PMNPGQLCEV W
Length:881
Mass (Da):99,707
Last modified:November 13, 2007 - v2
Checksum:i79A3F7BF128F8BAA
GO
Isoform 2 (identifier: Q80Z60-2) [UniParc]FASTAAdd to basket

Also known as: ECE-2a-2

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: S → SEMVEYKRAKLRDEESPEITVEGRATRDSL

Show »
Length:910
Mass (Da):103,097
Checksum:iF5D1C5680EEA575F
GO
Isoform 3 (identifier: Q80Z60-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-260: VGFQKRTRQL...PNGRSRWNTF → VSRLLVPGGR...NEDFLSAIQL
     261-881: Missing.

Show »
Length:255
Mass (Da):28,531
Checksum:i250B2EF4520D7E47
GO

Sequence cautioni

The sequence AAO72356.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAO72357.1 differs from that shown. Reason: Erroneous initiation. Curated
Isoform 3 : The sequence BAB25257.1 differs from that shown. Reason: Frameshift at position 226. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601E → V in BAB25257 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 1591S → SEMVEYKRAKLRDEESPEIT VEGRATRDSL in isoform 2. 1 PublicationVSP_029335
Alternative sequencei161 – 260100VGFQK…RWNTF → VSRLLVPGGRFISMTSAGPH FRIRHYAQSRYDWSLRHTTY SSGFHFHFYIMHKGRALSVS QLALGAQILSSPSPPASPCF LQDSDNEDFLSAIQL in isoform 3. 2 PublicationsVSP_029336Add
BLAST
Alternative sequencei261 – 881621Missing in isoform 3. 2 PublicationsVSP_029339Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007407 mRNA. Translation: BAB25019.1.
AK007791 mRNA. Translation: BAB25257.1. Frameshift.
BC115541 mRNA. Translation: AAI15542.1.
AF489569 mRNA. Translation: AAO72356.1. Different initiation.
AF489570 mRNA. Translation: AAO72357.1. Different initiation.
CCDSiCCDS37290.1. [Q80Z60-3]
CCDS49793.1. [Q80Z60-2]
CCDS49794.1. [Q80Z60-1]
RefSeqiNP_079738.2. NM_025462.2. [Q80Z60-3]
NP_808809.1. NM_177940.1.
NP_808810.1. NM_177941.1.
UniGeneiMm.263319.

Genome annotation databases

EnsembliENSMUST00000115522; ENSMUSP00000111184; ENSMUSG00000022842. [Q80Z60-3]
GeneIDi107522.
KEGGimmu:107522.
UCSCiuc007yqh.1. mouse. [Q80Z60-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007407 mRNA. Translation: BAB25019.1.
AK007791 mRNA. Translation: BAB25257.1. Frameshift.
BC115541 mRNA. Translation: AAI15542.1.
AF489569 mRNA. Translation: AAO72356.1. Different initiation.
AF489570 mRNA. Translation: AAO72357.1. Different initiation.
CCDSiCCDS37290.1. [Q80Z60-3]
CCDS49793.1. [Q80Z60-2]
CCDS49794.1. [Q80Z60-1]
RefSeqiNP_079738.2. NM_025462.2. [Q80Z60-3]
NP_808809.1. NM_177940.1.
NP_808810.1. NM_177941.1.
UniGeneiMm.263319.

3D structure databases

ProteinModelPortaliQ80Z60.
SMRiQ80Z60. Positions 20-161, 212-881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113475.

Protein family/group databases

MEROPSiM13.003.

PTM databases

iPTMnetiQ80Z60.
PhosphoSiteiQ80Z60.

Proteomic databases

EPDiQ80Z60.
MaxQBiQ80Z60.
PaxDbiQ80Z60.
PeptideAtlasiQ80Z60.
PRIDEiQ80Z60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115522; ENSMUSP00000111184; ENSMUSG00000022842. [Q80Z60-3]
GeneIDi107522.
KEGGimmu:107522.
UCSCiuc007yqh.1. mouse. [Q80Z60-3]

Organism-specific databases

CTDi9718.
MGIiMGI:1101356. Ece2.

Phylogenomic databases

eggNOGiKOG2352. Eukaryota.
KOG3624. Eukaryota.
COG3590. LUCA.
GeneTreeiENSGT00760000119162.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ80Z60.
KOiK01415.
PhylomeDBiQ80Z60.

Miscellaneous databases

PROiQ80Z60.
SOURCEiSearch...

Gene expression databases

BgeeiQ80Z60.
CleanExiMM_ECE2.
ExpressionAtlasiQ80Z60. baseline and differential.
GenevisibleiQ80Z60. MM.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
3.40.50.150. 1 hit.
InterProiIPR029733. ECE2.
IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF127. PTHR11733:SF127. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Pancreas.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  3. "Molecular isolation and characterization of novel four subisoforms of ECE-2."
    Ikeda S., Emoto N., Alimsardjono H., Yokoyama M., Matsuo M.
    Biochem. Biophys. Res. Commun. 293:421-426(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-881 (ISOFORMS 1 AND 2).
  4. "Disruption of ECE-1 and ECE-2 reveals a role for endothelin-converting enzyme-2 in murine cardiac development."
    Yanagisawa H., Hammer R.E., Richardson J.A., Emoto N., Williams S.C., Takeda S., Clouthier D.E., Yanagisawa M.
    J. Clin. Invest. 105:1373-1382(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  5. "Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme."
    Eckman E.A., Watson M., Marlow L., Sambamurti K., Eckman C.B.
    J. Biol. Chem. 278:2081-2084(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiECE2_MOUSE
AccessioniPrimary (citable) accession number: Q80Z60
Secondary accession number(s): Q14BY3
, Q80Z59, Q9D8Q9, Q9D928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: July 6, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.