ECE1_CAVPO
ID ECE1_CAVPO Reviewed; 754 AA.
AC P97739;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Endothelin-converting enzyme 1;
DE Short=ECE-1;
DE EC=3.4.24.71;
GN Name=ECE1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8624482;
RA Shima H., Yamanouchi M., Omori K., Sugiura M., Kawashima K., Sato T.;
RT "Endothelin-1 production and endothelin converting enzyme expression by
RT guinea pig airway epithelial cells.";
RL Biochem. Mol. Biol. Int. 37:1001-1010(1995).
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. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC PPP1R16B (By similarity). {ECO:0000250|UniProtKB:P42891,
CC ECO:0000250|UniProtKB:P42893}.
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}.
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DR EMBL; S82653; AAB46734.1; -; mRNA.
DR AlphaFoldDB; P97739; -.
DR SMR; P97739; -.
DR STRING; 10141.ENSCPOP00000010492; -.
DR MEROPS; M13.002; -.
DR eggNOG; KOG3624; Eukaryota.
DR InParanoid; P97739; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR029734; ECE1.
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; PTHR11733; 1.
DR PANTHER; PTHR11733:SF130; PTHR11733:SF130; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..754
FT /note="Endothelin-converting enzyme 1"
FT /id="PRO_0000078219"
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"
SQ SEQUENCE 754 AA; 85772 MW; F0646C57FF2BA8A0 CRC64;
MMSTYKRATL DEEDLVDSLS EGEVYPNGLQ VNFRNFRSSQ RCWATRTQVE KRLIVLVALL
AAGLVACLTA LGIQYRTRTP PVCLSEACVS VTSSILNSMN PTVDPCQDFF SYACGGWIKA
NPVPDGHSRW GAFSNLWEHN QAIIKHLLEN STASVSEAER KAQVYYRACM NETRIEELRA
KPLMELIEKL GGWNITGPWA KDNFQDTLQV VTAHYRTSPF FSVYVSADSK NSNRNVIHVD
QSGLGLPSRD YYLNKTENEK VLNGYLNYMV QLGKLLGGGD ENAIRAQMQQ ILDFETALAN
ITIPQEKRRD EELIYHKVTA AELQTLAPAI NWLPFLNTIF YPVEINESEP IVVYDKEYLE
QVSTLINTTD KCLLNNYMIW NLVRKTSSFL DQRFQDADEK FMEVMYGTKK TCLPRWKFCV
SDTENNLGFG LGPMFVKATF AEDSKNIASE IILEIKKAFE ESLSTLKWMD EDTRKSAKEK
ADAIYNMIGY PNFIMDPKEL DKVFNDYTAV PDLYFENAMR FFNFSWRVTA EQLRKAPNRD
QWSMTPPMVN AYYSPTKNEI VFPAGILPAP FYTRSSPKAL NFGGIGVVVG HELTHAFDDQ
GREYDKDGNL RPWWKNSSVE AFKQQTECMV EQYSNYSVNG EPVNGRHTLG ENIADNGGLK
AAYRAYQNWV KKNGAEETLP TLGLTNNQLF FLGFAQVWCS VRTPESSHEG LITDPHSPSR
FRVIGSLSNS KEFSEHFQCP PGSPMNPRHK CEVW
