ID ECE1_BOVIN Reviewed; 754 AA.
AC P42891; A2VDM9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 156.
DE RecName: Full=Endothelin-converting enzyme 1;
DE Short=ECE-1;
DE EC=3.4.24.71;
GN Name=ECE1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7805846; DOI=10.1016/0014-5793(94)01277-6;
RA Schmidt M., Kroeger B., Jacob E., Seulberger H., Subkowski T., Otter R.,
RA Meyer T., Schmalzing G., Hillen H.;
RT "Molecular characterization of human and bovine endothelin converting
RT enzyme (ECE-1).";
RL FEBS Lett. 356:238-243(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PPP1R16B.
RX PubMed=26806547; DOI=10.1016/j.biocel.2016.01.016;
RA Boratko A., Vereb Z., Petrovski G., Csortos C.;
RT "TIMAP-protein phosphatase 1-complex controls endothelin-1 production via
RT ECE-1 dephosphorylation.";
RL Int. J. Biochem. Cell Biol. 73:11-18(2016).
CC -!- FUNCTION: Converts big endothelin-1 to endothelin-1.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to
CC form endothelin 1.; EC=3.4.24.71;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoramidon.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC PPP1R16B (PubMed:26806547). {ECO:0000250|UniProtKB:P42892,
CC ECO:0000269|PubMed:26806547}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z35306; CAA84547.1; -; mRNA.
DR EMBL; BC133320; AAI33321.1; -; mRNA.
DR PIR; S51010; S47268.
DR RefSeq; XP_005203129.1; XM_005203072.3.
DR AlphaFoldDB; P42891; -.
DR SMR; P42891; -.
DR STRING; 9913.ENSBTAP00000070717; -.
DR BindingDB; P42891; -.
DR ChEMBL; CHEMBL2340; -.
DR MEROPS; M13.002; -.
DR GlyCosmos; P42891; 10 sites, No reported glycans.
DR SwissPalm; P42891; -.
DR PaxDb; 9913-ENSBTAP00000055669; -.
DR PeptideAtlas; P42891; -.
DR Ensembl; ENSBTAT00000037770.5; ENSBTAP00000037593.4; ENSBTAG00000002977.6.
DR Ensembl; ENSBTAT00000076810.1; ENSBTAP00000071468.1; ENSBTAG00000002977.6.
DR GeneID; 281133; -.
DR CTD; 1889; -.
DR VEuPathDB; HostDB:ENSBTAG00000002977; -.
DR VGNC; VGNC:28302; ECE1.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000156050; -.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; P42891; -.
DR OrthoDB; 202716at2759; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR SABIO-RK; P42891; -.
DR PRO; PR:P42891; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000002977; Expressed in granulosa cell and 107 other cell types or tissues.
DR ExpressionAtlas; P42891; baseline and differential.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; ISS:AgBase.
DR CDD; cd08662; M13; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1380.10; Neutral endopeptidase , domain2; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733:SF130; ENDOTHELIN-CONVERTING ENZYME 1; 1.
DR PANTHER; PTHR11733; ZINC METALLOPROTEASE FAMILY M13 NEPRILYSIN-RELATED; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..754
FT /note="Endothelin-converting enzyme 1"
FT /id="PRO_0000078218"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 82..754
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 655
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42892"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 106..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 114..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 169..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 628..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CONFLICT 8
FT /note="A -> P (in Ref. 1; CAA84547)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="A -> S (in Ref. 2; AAI33321)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..164
FT /note="AQV -> DQE (in Ref. 1; CAA84547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 85517 MW; 763D8E2664E3A540 CRC64;
MMSTYKRATL DEEDLVDSLS ESDVYPNHLQ VNFRGPRNGQ RCWAARTPVE KRLVVLVALL
AAALVACLAV LGIQYQTRTP SVCLSEACIS VTSSILSSMD PTVDPCQDFF TYACGGWIKA
NPVPDGHSRW GTFSNLWEHN QAIIKHLLEN STASVSEAER KAQVYYRACM NETRIEELKA
KPLMELIEKL GGWNITGPWD KDNFQDTLQV VTSHYHTSPF FSVYVSADSK NSNSNVIQVD
QSGLGLPSRD YYLNKTENEK VLTGYLNYMV QLGKLLGGGA EDTIRPQMQQ ILDFETALAN
ITIPQEKRRD EELIYHKVTA AELQTLAPAI NWLPFLNTIF YPVEINESEP IVIYDKEYLS
KVSTLINSTD KCLLNNYMIW NLVRKTSSFL DQRFQDADEK FMEVMYGTKK TCLPRWKFCV
SDTENTLGFA LGPMFVKATF AEDSKNIASE IILEIKKAFE ESLSTLKWMD EDTRKSAKEK
ADAIYNMIGY PNFIMDPKEL DKVFNDYTAV PDLYFENAMR FFNFSWRVTA DQLRKAPNRD
QWSMTPPMVN AYYSPTKNEI VFPAGILQAP FYTRSSPNAL NFGGIGVVVG HELTHAFDDQ
GREYDKDGNL RPWWKNSSVE AFKQQTACMV EQYGNYSVNG EPVNGRHTLG ENIADNGGLK
AAYRAYQNWV KKNGAEQTLP TLGLTNNQLF FLSFAQVWCS VRTPESSHEG LITDPHSPSR
FRVIGSISNS KEFSEHFHCP PGSPMNPHHK CEVW
//
