ECE1_MOUSE
ID ECE1_MOUSE Reviewed; 769 AA.
AC Q4PZA2; B1AXF9; Q4PZ99; Q4PZA1; Q6P9Q9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Endothelin-converting enzyme 1;
DE Short=ECE-1;
DE EC=3.4.24.71;
GN Name=Ece1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=16540265; DOI=10.1016/j.gene.2006.01.024;
RA Lindenau S., von Langsdorff C., Saxena A., Paul M., Orzechowski H.-D.;
RT "Genomic organisation of the mouse gene encoding endothelin-converting
RT enzyme-1 (ECE-1) and mRNA expression of ECE-1 isoforms in murine tissues.";
RL Gene 373:109-115(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-315; ASN-361 AND ASN-382.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-165; ASN-209 AND ASN-361.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts big endothelin-1 to endothelin-1. {ECO:0000250}.
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 {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B;
CC IsoId=Q4PZA2-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q4PZA2-2; Sequence=VSP_019399;
CC Name=C;
CC IsoId=Q4PZA2-3; Sequence=VSP_019400;
CC Name=D;
CC IsoId=Q4PZA2-4; Sequence=VSP_019401;
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; DQ022741; AAY81993.1; -; Genomic_DNA.
DR EMBL; DQ022723; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022725; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022727; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022726; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022728; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022730; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022732; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022734; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022736; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022740; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022739; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022738; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022737; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022735; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022733; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022731; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022729; AAY81993.1; JOINED; Genomic_DNA.
DR EMBL; DQ022741; AAY81995.1; -; Genomic_DNA.
DR EMBL; DQ022721; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022723; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022725; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022726; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022728; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022730; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022732; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022734; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022736; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022740; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022739; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022738; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022737; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022735; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022733; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022731; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022729; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022727; AAY81995.1; JOINED; Genomic_DNA.
DR EMBL; DQ022741; AAY81996.1; -; Genomic_DNA.
DR EMBL; DQ022722; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022723; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022725; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022726; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022728; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022730; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022732; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022734; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022736; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022740; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022739; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022738; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022737; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022735; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022733; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022731; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022729; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022727; AAY81996.1; JOINED; Genomic_DNA.
DR EMBL; DQ022741; AAY81997.1; -; Genomic_DNA.
DR EMBL; DQ022724; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022725; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022727; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022726; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022728; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022730; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022732; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022734; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022736; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022740; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022739; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022738; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022737; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022735; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022733; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022731; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; DQ022729; AAY81997.1; JOINED; Genomic_DNA.
DR EMBL; AK134088; BAE22007.1; -; mRNA.
DR EMBL; AL807764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060648; AAH60648.1; -; mRNA.
DR CCDS; CCDS18822.1; -. [Q4PZA2-3]
DR RefSeq; NP_955011.1; NM_199307.2. [Q4PZA2-3]
DR RefSeq; XP_006538828.1; XM_006538765.1.
DR RefSeq; XP_006538830.1; XM_006538767.3.
DR AlphaFoldDB; Q4PZA2; -.
DR SMR; Q4PZA2; -.
DR BioGRID; 231041; 3.
DR STRING; 10090.ENSMUSP00000099576; -.
DR MEROPS; M13.002; -.
DR GlyConnect; 2289; 3 N-Linked glycans (3 sites).
DR GlyGen; Q4PZA2; 10 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q4PZA2; -.
DR PhosphoSitePlus; Q4PZA2; -.
DR SwissPalm; Q4PZA2; -.
DR EPD; Q4PZA2; -.
DR jPOST; Q4PZA2; -.
DR MaxQB; Q4PZA2; -.
DR PaxDb; Q4PZA2; -.
DR PeptideAtlas; Q4PZA2; -.
DR PRIDE; Q4PZA2; -.
DR ProteomicsDB; 277623; -. [Q4PZA2-1]
DR ProteomicsDB; 277624; -. [Q4PZA2-2]
DR ProteomicsDB; 277625; -. [Q4PZA2-3]
DR ProteomicsDB; 277626; -. [Q4PZA2-4]
DR Antibodypedia; 772; 417 antibodies from 34 providers.
DR DNASU; 230857; -.
DR Ensembl; ENSMUST00000102518; ENSMUSP00000099576; ENSMUSG00000057530. [Q4PZA2-3]
DR GeneID; 230857; -.
DR KEGG; mmu:230857; -.
DR UCSC; uc008vju.2; mouse. [Q4PZA2-1]
DR UCSC; uc008vjv.1; mouse. [Q4PZA2-2]
DR CTD; 1889; -.
DR MGI; MGI:1101357; Ece1.
DR VEuPathDB; HostDB:ENSMUSG00000057530; -.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000156050; -.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; Q4PZA2; -.
DR OMA; DQRFFMN; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; Q4PZA2; -.
DR TreeFam; TF315192; -.
DR BRENDA; 3.4.24.71; 3474.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR BioGRID-ORCS; 230857; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ece1; mouse.
DR PRO; PR:Q4PZA2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q4PZA2; protein.
DR Bgee; ENSMUSG00000057530; Expressed in aortic valve and 265 other tissues.
DR ExpressionAtlas; Q4PZA2; baseline and differential.
DR Genevisible; Q4PZA2; MM.
DR GO; GO:0009986; C:cell surface; ISS:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0033093; C:Weibel-Palade body; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IMP:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISO:MGI.
DR GO; GO:0010815; P:bradykinin catabolic process; ISO:MGI.
DR GO; GO:0010816; P:calcitonin catabolic process; ISO:MGI.
DR GO; GO:0043583; P:ear development; ISO:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0034959; P:endothelin maturation; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0042447; P:hormone catabolic process; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0016486; P:peptide hormone processing; ISS:MGI.
DR GO; GO:0060037; P:pharyngeal system development; IMP:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:MGI.
DR GO; GO:0010814; P:substance P catabolic process; ISO:MGI.
DR GO; GO:0097492; P:sympathetic neuron axon guidance; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..769
FT /note="Endothelin-converting enzyme 1"
FT /id="PRO_0000240629"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..769
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 97..769
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 670
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 606
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 610
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 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42892"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 121..754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 129..714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 184..434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 643..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VAR_SEQ 1..43
FT /note="MRTVWSPLAAALAALGMSTYKRATLDEEDLVDSLSEGDVYPNG -> MPPQS
FT LGLQRGSFFLGKRGPGLMVSLPLLASS (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_019399"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019400"
FT VAR_SEQ 1..16
FT /note="MRTVWSPLAAALAALG -> METLRESVLHLALQ (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_019401"
SQ SEQUENCE 769 AA; 87073 MW; 58214938A0F2760A CRC64;
MRTVWSPLAA ALAALGMSTY KRATLDEEDL VDSLSEGDVY PNGLQVNFRS SRSGQRCWAA
RTSVEKRLVV LVTLLAAGLV ACLAALGIQY QTRTPPVCLT EACVSVTSSI LNSMDPTVDP
CQDFFSYACG GWIKANPVPD GHSRWGTFSN LWEHNQAVIK HLLENATASV SEAERKAQVY
YRACMNETRI EELRAKPLME LIEKLGGWNI TGPWAKDNFQ DTLQVVTAHY RTSPFFSVYV
SADSKNSNSN VIQVDQSGLG LPSRDYYLNK TENEKVLTGY LNYMVQLGKL LGGGDEDAIR
PQMQQILDFE TALANITIPQ EKRRDEELIY HKVTAAELQT LAPAINWLPF LNTIFYPVEI
NESEPIVVYD KEYLRQVSTL INNTDKCLLN NYMMWNLVRK TSSFLDQRFQ DADEKFMEVM
YGTKKTCIPR WKFCVSDTEN NLGFALGPMF VKATFAEDSK NIASEIIMEI KKAFEESLST
LKWMDEETRR SAKEKADAIY NMIGYPNFIM DPKELDKVFN DYTAVPDLYF ENAMRFFNFS
WRVTADQLRK APNRDQWSMT PPMVNAYYSP TKNEIVFPAG ILQAPFYTRS SPNALNFGGI
GVVVGHELTH AFDDQGREYD KDGNLRPWWK NSSVEAFKQQ TECMVQQYSN YSVNGEPVNG
RHTLGENIAD NGGLKAAYRA YQNWVKKNGA EQTLPTLGLT SNQLFFLGFA QVWCSVRTPE
SSHEGLITDP HSPSRFRVIG SLSNSKEFSE HFRCPPGSPM NPHHKCEVW
