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Protein

Endothelin-converting enzyme 2

Gene

ECE2

Organism
Bos taurus (Bovine)
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.

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

Enzyme regulationi

Inhibited by phosphoramidon.

pH dependencei

Optimum pH is 5.5. Inactive at neutral pH.

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 bindingi720 – 7201Zinc; catalyticPROSITE-ProRule annotation
Active sitei721 – 7211PROSITE-ProRule annotation
Metal bindingi724 – 7241Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi780 – 7801Zinc; catalyticPROSITE-ProRule annotation
Active sitei784 – 7841Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: UniProtKB
  • methyltransferase activity Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • brain development Source: UniProtKB
  • cardioblast differentiation Source: UniProtKB
  • embryo development Source: UniProtKB
  • heart development Source: UniProtKB
  • peptide hormone processing Source: UniProtKB
  • regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  • vasoconstriction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Methyltransferase, Protease, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ10711.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 178178CytoplasmicSequence analysisAdd
BLAST
Transmembranei179 – 19921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini200 – 883684LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 883883Endothelin-converting enzyme 2PRO_0000078222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphotyrosineBy similarity
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence analysis
Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ10711.
PRIDEiQ10711.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in liver, kidney, adrenal gland, testis and endothelial cells. Isoform 3 and isoform 4 are expressed in brain and adrenal gland.1 Publication

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042778.

Structurei

3D structure databases

ProteinModelPortaliQ10711.
SMRiQ10711. Positions 19-160.
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 – 883684Endothelin-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.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ10711.
KOiK01415.

Family and domain databases

CDDicd08662. M13. 1 hit.
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.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q10711-1) [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
MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD
60 70 80 90 100
LLEPELRPLD RILVLGCGNS ALSYELFLGG FPDVTSVDYS SVVVAAMRAR
110 120 130 140 150
YAHVPTLRWE TMDVRALGFP SGSFDVVLEK GTLDALLTGE QDPWTVSSEG
160 170 180 190 200
VHTVDQVLNE AGFRKRTSRL LGLHTQLELV LAGVSLLLAA LLLGCLVALG
210 220 230 240 250
VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ FSCGGWIRRN
260 270 280 290 300
PLPDGRSRWN NSNSLWDQNQ AILKHLLENT TFNSSSEAER KTQRFYLSCL
310 320 330 340 350
QVERIEELGA HALRDLIDKI GGWNVTGPWD QDNFMEVLKA VAGTYRATPF
360 370 380 390 400
FTVYVSADSK SSNSNIIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME
410 420 430 440 450
ELGMLLGGQP TSTREQMRQV LELEIQLANI TVPQDQRRDE EKIYHKMSIA
460 470 480 490 500
ELQALAPSMD WLEFLSFLLS PLELGDSEPV VVYGTDYLQQ VSELINRTEP
510 520 530 540 550
SVLNNYLIWN LVQKTTSSLD HRFESAQEKL LETLYGTKKS CTPRWQTCIS
560 570 580 590 600
NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRVAFEE ALGHLVWMDE
610 620 630 640 650
KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEVSE DSFFQNMLNL
660 670 680 690 700
YNFSAKVMAD QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF
710 720 730 740 750
YTCNHPQALN FGGIGVVMGH ELTHAFDDQG REYDKEGNLR PWWQNESLAA
760 770 780 790 800
FRNHTACIEE QYSQYQVNGE KLNGRQTLGE NIADNGGLKA AYNAYKAWLR
810 820 830 840 850
KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL VTDPHSPARF
860 870 880
RVLGTLSNSR DFLRHFGCPV GSPMNSGQLC EVW
Length:883
Mass (Da):99,601
Last modified:November 13, 2007 - v2
Checksum:i3079A02496E82BE8
GO
Isoform 2 (identifier: Q10711-2) [UniParc]FASTAAdd to basket
Also known as: ECE-2a-2

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: A → MVEYKRATLRDEDAPETPVEGGASPDAVEA

Show »
Length:912
Mass (Da):102,717
Checksum:i6BA7F597283C189B
GO
Isoform 3 (identifier: Q10711-3) [UniParc]FASTAAdd to basket
Also known as: ECE-2b-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MACLGPSAQV...VHTVDQVLNE → MRVALQELGGGGN

Show »
Length:736
Mass (Da):83,129
Checksum:i7ECD124469751D91
GO
Isoform 4 (identifier: Q10711-4) [UniParc]FASTAAdd to basket
Also known as: ECE-2b-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MACLGPSAQV...VHTVDQVLNE → MRVALQELGGGGN
     161-161: A → MVEYKRATLRDEDAPETPVEGGASPDAVEA

Show »
Length:765
Mass (Da):86,244
Checksum:i12C3FE747881E1FF
GO
Isoform 5 (identifier: Q10711-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-255: AGFRKRTSRL...WIRRNPLPDG → VSRVLVPAGR...HEDFLSAIQL
     256-883: Missing.

Show »
Length:255
Mass (Da):28,396
Checksum:i2B7566ABDFED9C0F
GO

Sequence cautioni

The sequence AAA82927 differs from that shown. Reason: Frameshift at position 78. Curated
The sequence AAO72360 differs from that shown. Reason: Frameshift at position 78. Curated
The sequence AAO72361 differs from that shown. Reason: Frameshift at position 78. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 160160MACLG…QVLNE → MRVALQELGGGGN in isoform 3 and isoform 4. 1 PublicationVSP_029329Add
BLAST
Alternative sequencei161 – 25595AGFRK…PLPDG → VSRVLVPAGRFISLTSAAPH FRTRHYAQAHYGWSLRHATY GNGFQFHFYLMQKGKELSVA QLAVGAQILSPPRPPTPSCF LQDSDHEDFLSAIQL in isoform 5. 1 PublicationVSP_029330Add
BLAST
Alternative sequencei161 – 1611A → MVEYKRATLRDEDAPETPVE GGASPDAVEA in isoform 2 and isoform 4. 1 PublicationVSP_029331
Alternative sequencei256 – 883628Missing in isoform 5. 1 PublicationVSP_029332Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF489573 mRNA. Translation: AAO72360.1. Frameshift.
AF489574 mRNA. Translation: AAO72361.1. Frameshift.
BC142117 mRNA. Translation: AAI42118.1.
U27341 mRNA. Translation: AAA82927.1. Frameshift.
RefSeqiNP_001300993.1. NM_001314064.1.
UniGeneiBt.4840.

Genome annotation databases

GeneIDi281134.
KEGGibta:281134.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF489573 mRNA. Translation: AAO72360.1. Frameshift.
AF489574 mRNA. Translation: AAO72361.1. Frameshift.
BC142117 mRNA. Translation: AAI42118.1.
U27341 mRNA. Translation: AAA82927.1. Frameshift.
RefSeqiNP_001300993.1. NM_001314064.1.
UniGeneiBt.4840.

3D structure databases

ProteinModelPortaliQ10711.
SMRiQ10711. Positions 19-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042778.

Protein family/group databases

MEROPSiM13.003.

Proteomic databases

PaxDbiQ10711.
PRIDEiQ10711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281134.
KEGGibta:281134.

Organism-specific databases

CTDi9718.

Phylogenomic databases

eggNOGiKOG2352. Eukaryota.
KOG3624. Eukaryota.
COG3590. LUCA.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ10711.
KOiK01415.

Enzyme and pathway databases

SABIO-RKQ10711.

Family and domain databases

CDDicd08662. M13. 1 hit.
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.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECE2_BOVIN
AccessioniPrimary (citable) accession number: Q10711
Secondary accession number(s): A5PJH8, Q547G8, Q865C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: September 7, 2016
This is version 121 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.