P42892 (ECE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin-converting enzyme 1
Short name=ECE-1
EC=3.4.24.71

Gene names

Name:

ECE1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts big endothelin-1 to endothelin-1. Ref.11
Catalytic activity	Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.
Cofactor	Binds 1 zinc ion per subunit. Ref.19
Enzyme regulation	Inhibited by phosphoramidon.
Subunit structure	Homodimer; disulfide-linked. Ref.19
Subcellular location	Cell membrane; Single-pass type II membrane protein.
Tissue specificity	All isoforms are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Isoforms A, B and C are also expressed in placenta, lung, heart, adrenal gland and phaeochromocytoma; isoforms A and C in liver, testis and small intestine; isoform B, C and D in endothelial cells and umbilical vein smooth muscle cells; isoforms C and D in saphenous vein cells, and isoform C in kidney. Ref.10 Ref.11
Involvement in disease	Defects in ECE1 are a cause of Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD) [MIM:613870]. It is a form of Hirschsprung disease with skip-lesions defects, craniofacial abnormalities and other dysmorphic features, and autonomic dysfunction. Ref.20
Sequence similarities	Belongs to the peptidase M13 family.
Sequence caution	The sequence AAX35820.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA84548.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hirschsprung disease
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	bradykinin catabolic process Inferred from direct assay. Source: BHF-UCL calcitonin catabolic process Inferred from direct assay. Source: BHF-UCL ear development Inferred from mutant phenotype Ref.20. Source: BHF-UCL embryonic digit morphogenesis Inferred from mutant phenotype Ref.20. Source: BHF-UCL endothelin maturation Inferred from direct assay Ref.12. Source: BHF-UCL heart development Inferred from mutant phenotype Ref.20. Source: BHF-UCL positive regulation of receptor recycling Inferred from mutant phenotype. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of systemic arterial blood pressure by endothelin Inferred by curator Ref.12. Source: BHF-UCL regulation of vasoconstriction Inferred by curator Ref.12. Source: BHF-UCL substance P catabolic process Inferred from direct assay. Source: BHF-UCL
Cellular component	Weibel-Palade body Inferred from direct assay. Source: BHF-UCL early endosome Inferred from direct assay. Source: BHF-UCL external side of plasma membrane Inferred from direct assay. Source: BHF-UCL integral to membrane Inferred from direct assay Ref.12. Source: BHF-UCL intrinsic to endosome membrane Traceable author statement. Source: BHF-UCL membrane fraction Inferred from direct assay Ref.2. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay. Source: BHF-UCL plasma membrane Inferred from direct assay. Source: BHF-UCL
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from sequence or structural similarity. Source: BHF-UCL peptide hormone binding Inferred by curator Ref.2. Source: BHF-UCL protein homodimerization activity Inferred from physical interaction Ref.12. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: P42892-1)

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.

Isoform A (identifier: P42892-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MRGVWPPPVS...LSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS

Isoform C (identifier: P42892-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MRGVWPPPVSALLSALG → M

Isoform D (identifier: P42892-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MRGVWPPPVSALLSALG → MEALRESVLHLALQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 770

770

Endothelin-converting enzyme 1

PRO_0000078220

Regions

Topological domain

1 – 68

68

Cytoplasmic Potential

Transmembrane

69 – 89

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

90 – 770

681

Extracellular Potential

Sites

Active site

608

1

Active site

671

1

Proton donor By similarity

Metal binding

607

1

Zinc; catalytic

Metal binding

611

1

Zinc; catalytic

Metal binding

667

1

Zinc; catalytic

Amino acid modifications

Modified residue

25

1

Phosphothreonine Ref.18

Modified residue

34

1

Phosphoserine Ref.14

Glycosylation

166

1

N-linked (GlcNAc...) Ref.16 Ref.17

Glycosylation

187

1

N-linked (GlcNAc...) Potential

Glycosylation

210

1

N-linked (GlcNAc...) Ref.15 Ref.16 Ref.17

Glycosylation

270

1

N-linked (GlcNAc...) Ref.16

Glycosylation

316

1

N-linked (GlcNAc...) Ref.16

Glycosylation

362

1

N-linked (GlcNAc...) Ref.17

Glycosylation

383

1

N-linked (GlcNAc...) Ref.17

Glycosylation

539

1

N-linked (GlcNAc...) Potential

Glycosylation

632

1

N-linked (GlcNAc...) Potential

Glycosylation

651

1

N-linked (GlcNAc...) Potential

Disulfide bond

428

Interchain

Natural variations

Alternative sequence

1 – 44

44

MRGVW…AYPNG → MPLQGLGLQRNPFLQGKRGP GLTSSPPLLPPS in isoform A.

VSP_005502

Alternative sequence

1 – 17

17

MRGVW…LSALG → M in isoform C.

VSP_005504

Alternative sequence

1 – 17

17

MRGVW…LSALG → MEALRESVLHLALQ in isoform D.

VSP_005503

Natural variant

341

1

T → I. Ref.6
Corresponds to variant rs1076669 [ dbSNP | Ensembl ].

VAR_011972

Natural variant

630

1

W → R.
Corresponds to variant rs2229451 [ dbSNP | Ensembl ].

VAR_054007

Natural variant

754

1

R → C in HSCRCDAD. Ref.20
Corresponds to variant rs3026906 [ dbSNP | Ensembl ].

VAR_026747

Experimental info

Mutagenesis

428

1

C → S: Abolishes dimerization. Ref.19

Secondary structure

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770

Helix Strand Turn

Details...

Helix

102 – 114

13

Turn

121 – 123

3

Helix

125 – 129

5

Turn

134 – 136

3

Helix

149 – 164

16

Helix

173 – 186

14

Helix

189 – 194

6

Helix

197 – 205

9

Helix

220 – 229

10

Beta strand

235 – 244

10

Beta strand

247 – 256

10

Helix

266 – 269

4

Turn

270 – 273

4

Helix

282 – 287

6

Helix

297 – 317

21

Helix

321 – 324

4

Helix

327 – 330

4

Beta strand

332 – 335

4

Helix

336 – 342

7

Helix

348 – 355

8

Beta strand

366 – 370

5

Helix

372 – 384

13

Helix

387 – 402

16

Helix

403 – 405

3

Helix

408 – 418

11

Helix

434 – 442

9

Helix

450 – 455

6

Helix

458 – 479

22

Helix

487 – 499

13

Beta strand

501 – 503

3

Helix

508 – 511

4

Helix

513 – 520

8

Helix

530 – 546

17

Turn

547 – 550

4

Beta strand

568 – 570

3

Turn

571 – 574

4

Beta strand

575 – 577

3

Turn

585 – 587

3

Helix

594 – 597

4

Helix

608 – 611

4

Helix

632 – 649

18

Helix

668 – 671

4

Helix

676 – 688

13

Helix

702 – 707

6

Helix

711 – 714

4

Helix

720 – 724

5

Helix

735 – 739

5

Helix

743 – 745

3

Helix

747 – 753

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified October 1, 1996. Version 2. Checksum: DD88A59748B22F80	FASTA	770	87,164
	10 20 30 40 50 60 MRGVWPPPVS ALLSALGMST YKRATLDEED LVDSLSEGDA YPNGLQVNFH SPRSGQRCWA 70 80 90 100 110 120 ARTQVEKRLV VLVVLLAAGL VACLAALGIQ YQTRSPSVCL SEACVSVTSS ILSSMDPTVD 130 140 150 160 170 180 PCHDFFSYAC GGWIKANPVP DGHSRWGTFS NLWEHNQAII KHLLENSTAS VSEAERKAQV 190 200 210 220 230 240 YYRACMNETR IEELRAKPLM ELIERLGGWN ITGPWAKDNF QDTLQVVTAH YRTSPFFSVY 250 260 270 280 290 300 VSADSKNSNS NVIQVDQSGL GLPSRDYYLN KTENEKVLTG YLNYMVQLGK LLGGGDEEAI 310 320 330 340 350 360 RPQMQQILDF ETALANITIP QEKRRDEELI YHKVTAAELQ TLAPAINWLP FLNTIFYPVE 370 380 390 400 410 420 INESEPIVVY DKEYLEQIST LINTTDRCLL NNYMIWNLVR KTSSFLDQRF QDADEKFMEV 430 440 450 460 470 480 MYGTKKTCLP RWKFCVSDTE NNLGFALGPM FVKATFAEDS KSIATEIILE IKKAFEESLS 490 500 510 520 530 540 TLKWMDEETR KSAKEKADAI YNMIGYPNFI MDPKELDKVF NDYTAVPDLY FENAMRFFNF 550 560 570 580 590 600 SWRVTADQLR KAPNRDQWSM TPPMVNAYYS PTKNEIVFPA GILQAPFYTR SSPKALNFGG 610 620 630 640 650 660 IGVVVGHELT HAFDDQGREY DKDGNLRPWW KNSSVEAFKR QTECMVEQYS NYSVNGEPVN 670 680 690 700 710 720 GRHTLGENIA DNGGLKAAYR AYQNWVKKNG AEHSLPTLGL TNNQLFFLGF AQVWCSVRTP 730 740 750 760 770 ESSHEGLITD PHSPSRFRVI GSLSNSKEFS EHFRCPPGSP MNPPHKCEVW
	Isoform A [UniParc]. Checksum: 4768314E789DFF96	FASTA	758	85,808
	10 20 30 40 50 60 MPLQGLGLQR NPFLQGKRGP GLTSSPPLLP PSLQVNFHSP RSGQRCWAAR TQVEKRLVVL 70 80 90 100 110 120 VVLLAAGLVA CLAALGIQYQ TRSPSVCLSE ACVSVTSSIL SSMDPTVDPC HDFFSYACGG 130 140 150 160 170 180 WIKANPVPDG HSRWGTFSNL WEHNQAIIKH LLENSTASVS EAERKAQVYY RACMNETRIE 190 200 210 220 230 240 ELRAKPLMEL IERLGGWNIT GPWAKDNFQD TLQVVTAHYR TSPFFSVYVS ADSKNSNSNV 250 260 270 280 290 300 IQVDQSGLGL PSRDYYLNKT ENEKVLTGYL NYMVQLGKLL GGGDEEAIRP QMQQILDFET 310 320 330 340 350 360 ALANITIPQE KRRDEELIYH KVTAAELQTL APAINWLPFL NTIFYPVEIN ESEPIVVYDK 370 380 390 400 410 420 EYLEQISTLI NTTDRCLLNN YMIWNLVRKT SSFLDQRFQD ADEKFMEVMY GTKKTCLPRW 430 440 450 460 470 480 KFCVSDTENN LGFALGPMFV KATFAEDSKS IATEIILEIK KAFEESLSTL KWMDEETRKS 490 500 510 520 530 540 AKEKADAIYN MIGYPNFIMD PKELDKVFND YTAVPDLYFE NAMRFFNFSW RVTADQLRKA 550 560 570 580 590 600 PNRDQWSMTP PMVNAYYSPT KNEIVFPAGI LQAPFYTRSS PKALNFGGIG VVVGHELTHA 610 620 630 640 650 660 FDDQGREYDK DGNLRPWWKN SSVEAFKRQT ECMVEQYSNY SVNGEPVNGR HTLGENIADN 670 680 690 700 710 720 GGLKAAYRAY QNWVKKNGAE HSLPTLGLTN NQLFFLGFAQ VWCSVRTPES SHEGLITDPH 730 740 750 SPSRFRVIGS LSNSKEFSEH FRCPPGSPMN PPHKCEVW
	Isoform C [UniParc]. Checksum: A16E45032B03029D	FASTA	754	85,562
	10 20 30 40 50 60 MMSTYKRATL DEEDLVDSLS EGDAYPNGLQ VNFHSPRSGQ RCWAARTQVE KRLVVLVVLL 70 80 90 100 110 120 AAGLVACLAA LGIQYQTRSP SVCLSEACVS VTSSILSSMD PTVDPCHDFF SYACGGWIKA 130 140 150 160 170 180 NPVPDGHSRW GTFSNLWEHN QAIIKHLLEN STASVSEAER KAQVYYRACM NETRIEELRA 190 200 210 220 230 240 KPLMELIERL GGWNITGPWA KDNFQDTLQV VTAHYRTSPF FSVYVSADSK NSNSNVIQVD 250 260 270 280 290 300 QSGLGLPSRD YYLNKTENEK VLTGYLNYMV QLGKLLGGGD EEAIRPQMQQ ILDFETALAN 310 320 330 340 350 360 ITIPQEKRRD EELIYHKVTA AELQTLAPAI NWLPFLNTIF YPVEINESEP IVVYDKEYLE 370 380 390 400 410 420 QISTLINTTD RCLLNNYMIW NLVRKTSSFL DQRFQDADEK FMEVMYGTKK TCLPRWKFCV 430 440 450 460 470 480 SDTENNLGFA LGPMFVKATF AEDSKSIATE IILEIKKAFE ESLSTLKWMD EETRKSAKEK 490 500 510 520 530 540 ADAIYNMIGY PNFIMDPKEL DKVFNDYTAV PDLYFENAMR FFNFSWRVTA DQLRKAPNRD 550 560 570 580 590 600 QWSMTPPMVN AYYSPTKNEI VFPAGILQAP FYTRSSPKAL NFGGIGVVVG HELTHAFDDQ 610 620 630 640 650 660 GREYDKDGNL RPWWKNSSVE AFKRQTECMV EQYSNYSVNG EPVNGRHTLG ENIADNGGLK 670 680 690 700 710 720 AAYRAYQNWV KKNGAEHSLP TLGLTNNQLF FLGFAQVWCS VRTPESSHEG LITDPHSPSR 730 740 750 FRVIGSLSNS KEFSEHFRCP PGSPMNPPHK CEVW
	Isoform D [UniParc]. Checksum: 09B58AF5A63882F4	FASTA	767	87,022
	10 20 30 40 50 60 MEALRESVLH LALQMSTYKR ATLDEEDLVD SLSEGDAYPN GLQVNFHSPR SGQRCWAART 70 80 90 100 110 120 QVEKRLVVLV VLLAAGLVAC LAALGIQYQT RSPSVCLSEA CVSVTSSILS SMDPTVDPCH 130 140 150 160 170 180 DFFSYACGGW IKANPVPDGH SRWGTFSNLW EHNQAIIKHL LENSTASVSE AERKAQVYYR 190 200 210 220 230 240 ACMNETRIEE LRAKPLMELI ERLGGWNITG PWAKDNFQDT LQVVTAHYRT SPFFSVYVSA 250 260 270 280 290 300 DSKNSNSNVI QVDQSGLGLP SRDYYLNKTE NEKVLTGYLN YMVQLGKLLG GGDEEAIRPQ 310 320 330 340 350 360 MQQILDFETA LANITIPQEK RRDEELIYHK VTAAELQTLA PAINWLPFLN TIFYPVEINE 370 380 390 400 410 420 SEPIVVYDKE YLEQISTLIN TTDRCLLNNY MIWNLVRKTS SFLDQRFQDA DEKFMEVMYG 430 440 450 460 470 480 TKKTCLPRWK FCVSDTENNL GFALGPMFVK ATFAEDSKSI ATEIILEIKK AFEESLSTLK 490 500 510 520 530 540 WMDEETRKSA KEKADAIYNM IGYPNFIMDP KELDKVFNDY TAVPDLYFEN AMRFFNFSWR 550 560 570 580 590 600 VTADQLRKAP NRDQWSMTPP MVNAYYSPTK NEIVFPAGIL QAPFYTRSSP KALNFGGIGV 610 620 630 640 650 660 VVGHELTHAF DDQGREYDKD GNLRPWWKNS SVEAFKRQTE CMVEQYSNYS VNGEPVNGRH 670 680 690 700 710 720 TLGENIADNG GLKAAYRAYQ NWVKKNGAEH SLPTLGLTNN QLFFLGFAQV WCSVRTPESS 730 740 750 760 HEGLITDPHS PSRFRVIGSL SNSKEFSEHF RCPPGSPMNP PHKCEVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2." Yorimitsu K., Moroi K., Inagaki N., Saito T., Masuda Y., Masaki T., Seino S., Kimura S. Biochem. Biophys. Res. Commun. 208:721-727(1995) [PubMed: 7695628] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[2]	"Cloning and functional expression of human endothelin-converting enzyme cDNA." Shimada K., Matsushita Y., Wakabayashi K., Takahashi M., Matsubara A., Iijima Y., Tanzawa K. Biochem. Biophys. Res. Commun. 207:807-812(1995) [PubMed: 7864876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]	"Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)." Valdenaire O., Rohrbacher E., Mattei M.-G. J. Biol. Chem. 270:29794-29798(1995) [PubMed: 8530372] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B). Tissue: Placenta.
[4]	"Human endothelin-converting enzyme-1c." Takayanagi R. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). Tissue: Umbilical vein endothelial cell.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Tissue: Trachea.
[6]	NIEHS SNPs program Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-341.
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Tissue: Brain.
[10]	"A fourth isoform of endothelin-converting enzyme (ECE-1) is generated from an additional promoter." Valdenaire O., Lepailleur-Enouf D., Egidy G., Thouard A., Barret A., Vranckx R., Tougard C., Michel J.-B. Eur. J. Biochem. 264:341-349(1999) [PubMed: 10491078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-132 (ISOFORM D), TISSUE SPECIFICITY.
[11]	"Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations." Schweizer A., Valdenaire O., Nelboeck P., Deuschle U., Dumas Milne Edwards J.B., Stumpf J.G., Loeffler B.-M. Biochem. J. 328:871-877(1997) [PubMed: 9396733] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM C), FUNCTION, TISSUE SPECIFICITY. Tissue: Umbilical vein endothelial cell.
[12]	"Molecular characterization of human and bovine endothelin converting enzyme (ECE-1)." Schmidt M., Kroeger B., Jacob E., Seulberger H., Subkowski T., Otter R., Meyer T., Schmalzing G., Hillen H. FEBS Lett. 356:238-243(1994) [PubMed: 7805846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-770 (ISOFORM B). Tissue: Placenta.
[13]	"Characterization of the human endothelin converting enzyme-1 gene (ECE-1): genomic structure and chromosomal localization." Flowers M.A., Tai S.C., Baluyut C.A., Cheung A.H., Kau C.L., Wong G.K.T., Marsden P.A. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-770.
[14]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-270 AND ASN-316, MASS SPECTROMETRY. Tissue: Liver.
[17]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-362 AND ASN-383, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Structure of human endothelin-converting enzyme I complexed with phosphoramidon." Schulz H., Dale G.E., Karimi-Nejad Y., Oefner C. J. Mol. Biol. 385:178-187(2009) [PubMed: 18992253] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 101-770 OF MUTANT SER-428 IN COMPLEX WITH ZINC IONS AND PHOSPHORAMIDON, COFACTOR, SUBUNIT, MUTAGENESIS OF CYS-428.
[20]	"A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction." Hofstra R.M.W., Valdenaire O., Arch E., Osinga J., Kroes H., Loffler B.-M., Hamosh A., Meijers C., Buys C.H.C.M. Am. J. Hum. Genet. 64:304-308(1999) [PubMed: 9915973] [Abstract] Cited for: VARIANT HSCRCDAD CYS-754.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D49471 mRNA. Translation: BAA08442.1.
D43698 mRNA. Translation: BAA07800.1.
X91922 , X91923, X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63015.1.
X91923 , X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63016.1.
AY953519 Genomic DNA. Translation: AAX35820.1. Sequence problems.
AK290656 mRNA. Translation: BAF83345.1.
AK304167 mRNA. Translation: BAG65053.1.
AL031005 Genomic DNA. Translation: CAI20195.1.
AL031005, AL031728 Genomic DNA. Translation: CAI20192.1.
AL031005, AL031728 Genomic DNA. Translation: CAI20194.1.
AL031728 Genomic DNA. Translation: CAB52285.2.
AL031728, AL031005 Genomic DNA. Translation: CAI19064.1.
CH471134 Genomic DNA. Translation: EAW94959.1.
BC117256 mRNA. Translation: AAI17257.1.
BC126257 mRNA. Translation: AAI26258.1.
AJ130828 mRNA. Translation: CAB46443.1.
X98272 mRNA. Translation: CAA66922.1.
Z35307 mRNA. Translation: CAA84548.1. Different initiation.
AF018034 Genomic DNA. Translation: AAD21221.1.

IPI

IPI00002478.
IPI00216758.
IPI00216760.
IPI00216762.

PIR

JC2521.
JC4136.

RefSeq

NP_001106818.1. NM_001113347.1.
NP_001106819.1. NM_001113348.1.
NP_001106820.1. NM_001113349.1.
NP_001388.1. NM_001397.2.

UniGene

Hs.195080.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DWB	X-ray	2.38	A	101-770	[»]

ProteinModelPortal

P42892.

SMR

P42892. Positions 101-770.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42892. 1 interaction.

STRING

P42892.

Protein family/group databases

MEROPS

M13.002.

PTM databases

PhosphoSite

P42892.

Polymorphism databases

DMDM

1706563.

Proteomic databases

PRIDE

P42892.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374893; ENSP00000364028; ENSG00000117298.

GeneID

1889.

KEGG

hsa:1889.

UCSC

uc001bei.2. human.
uc001bej.2. human.
uc001bek.2. human.

Organism-specific databases

CTD

1889.

GeneCards

GC01M021543.

H-InvDB

HIX0023513.

HGNC

HGNC:3146. ECE1.

HPA

HPA001490.
HPA013616.

MIM

600423. gene.
613870. phenotype.

neXtProt

NX_P42892.

Orphanet

388. Hirschsprung disease.

PharmGKB

PA27594.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11506.

GeneTree

ENSGT00550000074200.

HOVERGEN

HBG005554.

InParanoid

P42892.

OMA

AIASKHW.

PhylomeDB

P42892.

Gene expression databases

ArrayExpress

P42892.

Bgee

P42892.

Genevestigator

P42892.

GermOnline

ENSG00000117298. Homo sapiens.

Family and domain databases

InterPro

IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]

Gene3D

G3DSA:3.40.390.10. G3DSA:3.40.390.10. 2 hits.

KO

K01415.

PANTHER

PTHR11733. Peptidase_M13. 1 hit.

Pfam

PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]

PRINTS

PR00786. NEPRILYSIN.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

7703.

SOURCE

Search...

Entry information

Entry name

ECE1_HUMAN

Accession

Primary (citable) accession number: P42892
Secondary accession number(s): A8K3P1 , B4E291, Q14217, Q17RN5, Q58GE7, Q5THM5, Q5THM7, Q5THM8, Q9UJQ6, Q9UPF4, Q9UPM4, Q9Y501

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.