O60344 (ECE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin-converting enzyme 2
Short name=ECE-2

Including the following 2 domains:

1. Methyltransferase-like region
   EC=2.1.1.-
2. Endothelin-converting enzyme 2 region
   EC=3.4.24.71

Gene names

Name:	ECE2
Synonyms:	KIAA0604
ORF Names:	UNQ403/PRO740

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	883 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Cytoplasmic granule membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Expressed in brain. Strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). Ref.10
Sequence similarities	In the N-terminal section; belongs to the methyltransferase superfamily. In the C-terminal section; belongs to the peptidase M13 family.
Biophysicochemical properties	Kinetic parameters: KM=0.4 µM for big ET-1 Ref.8 KM=1.4 µM for peptide E KM=27.4 µM for bradykinin KM=48.4 µM for dynorphin B pH dependence: Optimum pH is 5.0-5.5. Inactive at neutral pH.
Sequence caution	The sequence AAL30386.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA25530.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Methyltransferase Protease Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from sequence or structural similarity. Source: UniProtKB cardioblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB cell-cell signaling Traceable author statement Ref.1. Source: UniProtKB peptide hormone processing Inferred from direct assay Ref.1. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle membrane Inferred from direct assay Ref.1. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: O60344-1)

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 B (identifier: O60344-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: MASPGAGRAP...GVHTVDQVLS → MNVALQELGA...VEGGASPDAM

Isoform C (identifier: O60344-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MASPGAGRAP...VHTVDQVLSE → MNVALQELGAGSN

Isoform D (identifier: O60344-4)

The sequence of this isoform differs from the canonical sequence as follows:
     162-261: GFQKGTRQLL...LPDGRSRWNT → SRVLVPGGRF...HEDFLSAIQL
     262-883: Missing.

Isoform 2C (identifier: O60344-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MASPGAGRAP...VHTVDQVLSE → MNVALQELGA...SISGLCSRTM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 883

883

Endothelin-converting enzyme 2

PRO_0000078223

Regions

Topological domain

1 – 178

178

Cytoplasmic Potential

Transmembrane

179 – 199

21

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

Topological domain

200 – 883

684

Lumenal Potential

Region

1 – 160

160

Methyltransferase-like region

Region

88 – 89

2

S-adenosyl-L-homocysteine binding

Region

113 – 114

2

S-adenosyl-L-homocysteine binding

Region

200 – 883

684

Endothelin-converting enzyme 2 region

Sites

Active site

721

1

By similarity

Active site

784

1

Proton donor By similarity

Metal binding

720

1

Zinc; catalytic By similarity

Metal binding

724

1

Zinc; catalytic By similarity

Metal binding

780

1

Zinc; catalytic By similarity

Binding site

30

1

S-adenosyl-L-homocysteine

Binding site

41

1

S-adenosyl-L-homocysteine; via amide nitrogen

Binding site

66

1

S-adenosyl-L-homocysteine; via carbonyl oxygen

Binding site

130

1

S-adenosyl-L-homocysteine

Amino acid modifications

Modified residue

39

1

Phosphotyrosine Ref.9

Glycosylation

324

1

N-linked (GlcNAc...) Potential

Glycosylation

384

1

N-linked (GlcNAc...) Potential

Glycosylation

429

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 160

160

MASPG…QVLSE → MNVALQELGAGSNMVEYKRA TLRDEDAPETPVEGGASPDA MEVGKGASPFSPGPSPGMTP GTPRSSGLFWRVTCPHLRSI SGLCSRTM in isoform 2C.

VSP_039176

Alternative sequence

1 – 160

160

MASPG…QVLSE → MNVALQELGAGSN in isoform C.

VSP_005509

Alternative sequence

1 – 159

159

MASPG…DQVLS → MNVALQELGAGSNMVEYKRA TLRDEDAPETPVEGGASPDA M in isoform B.

VSP_005508

Alternative sequence

162 – 261

100

GFQKG…SRWNT → SRVLVPGGRFISMTSAAPHF RTRHYAQAYYGWSLRHATYG SGFHFHLYLMHKGGKLSVAQ LALGAQILSPPRPPTSPCFL QDSDHEDFLSAIQL in isoform D.

VSP_029333

Alternative sequence

262 – 883

622

Missing in isoform D.

VSP_029334

Natural variant

101

1

H → Y. Ref.6 Ref.7
Corresponds to variant rs7633387 [ dbSNP | Ensembl ].

VAR_047752

Natural variant

571

1

R → Q.
Corresponds to variant rs35875049 [ dbSNP | Ensembl ].

VAR_037085

Experimental info

Sequence conflict

467

1

F → S in AAI42951. Ref.7

Sequence conflict

783

1

A → T in AAQ89362. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

883

Helix Strand Turn

Details...

Helix

19 – 21

3

Helix

23 – 29

7

Turn

30 – 35

6

Helix

45 – 52

8

Helix

53 – 55

3

Beta strand

62 – 65

4

Helix

72 – 78

7

Beta strand

84 – 89

6

Helix

91 – 100

10

Turn

101 – 103

3

Beta strand

108 – 111

4

Beta strand

124 – 131

8

Helix

132 – 136

5

Turn

137 – 139

3

Helix

148 – 161

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 25, 2008. Version 4. Checksum: EE1C0F4AA4C6B225	FASTA	883	99,773
	10 20 30 40 50 60 MASPGAGRAP PELPERNCGY REVEYWDQRY QGAADSAPYD WFGDFSSFRA LLEPELRPED 70 80 90 100 110 120 RILVLGCGNS ALSYELFLGG FPNVTSVDYS SVVVAAMQAR HAHVPQLRWE TMDVRKLDFP 130 140 150 160 170 180 SASFDVVLEK GTLDALLAGE RDPWTVSSEG VHTVDQVLSE VGFQKGTRQL LGSRTQLELV 190 200 210 220 230 240 LAGASLLLAA LLLGCLVALG VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ 250 260 270 280 290 300 FSCGGWIRRN PLPDGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAEQ KTQRFYLSCL 310 320 330 340 350 360 QVERIEELGA QPLRDLIEKI GGWNITGPWD QDNFMEVLKA VAGTYRATPF FTVYISADSK 370 380 390 400 410 420 SSNSNVIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME ELGMLLGGRP TSTREQMQQV 430 440 450 460 470 480 LELEIQLANI TVPQDQRRDE EKIYHKMSIS ELQALAPSMD WLEFLSFLLS PLELSDSEPV 490 500 510 520 530 540 VVYGMDYLQQ VSELINRTEP SILNNYLIWN LVQKTTSSLD RRFESAQEKL LETLYGTKKS 550 560 570 580 590 600 CVPRWQTCIS NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRTAFEE ALGQLVWMDE 610 620 630 640 650 660 KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEISE DSFFQNMLNL YNFSAKVMAD 670 680 690 700 710 720 QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF YARNHPKALN FGGIGVVMGH 730 740 750 760 770 780 ELTHAFDDQG REYDKEGNLR PWWQNESLAA FRNHTACMEE QYNQYQVNGE RLNGRQTLGE 790 800 810 820 830 840 NIADNGGLKA AYNAYKAWLR KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL 850 860 870 880 VTDPHSPARF RVLGTLSNSR DFLRHFGCPV GSPMNPGQLC EVW
	Isoform B [UniParc]. Checksum: 89D1B831B5628694	FASTA	765	86,470
	10 20 30 40 50 60 MNVALQELGA GSNMVEYKRA TLRDEDAPET PVEGGASPDA MEVGFQKGTR QLLGSRTQLE 70 80 90 100 110 120 LVLAGASLLL AALLLGCLVA LGVQYHRDPS HSTCLTEACI RVAGKILESL DRGVSPCEDF 130 140 150 160 170 180 YQFSCGGWIR RNPLPDGRSR WNTFNSLWDQ NQAILKHLLE NTTFNSSSEA EQKTQRFYLS 190 200 210 220 230 240 CLQVERIEEL GAQPLRDLIE KIGGWNITGP WDQDNFMEVL KAVAGTYRAT PFFTVYISAD 250 260 270 280 290 300 SKSSNSNVIQ VDQSGLFLPS RDYYLNRTAN EKVLTAYLDY MEELGMLLGG RPTSTREQMQ 310 320 330 340 350 360 QVLELEIQLA NITVPQDQRR DEEKIYHKMS ISELQALAPS MDWLEFLSFL LSPLELSDSE 370 380 390 400 410 420 PVVVYGMDYL QQVSELINRT EPSILNNYLI WNLVQKTTSS LDRRFESAQE KLLETLYGTK 430 440 450 460 470 480 KSCVPRWQTC ISNTDDALGF ALGSLFVKAT FDRQSKEIAE GMISEIRTAF EEALGQLVWM 490 500 510 520 530 540 DEKTRQAAKE KADAIYDMIG FPDFILEPKE LDDVYDGYEI SEDSFFQNML NLYNFSAKVM 550 560 570 580 590 600 ADQLRKPPSR DQWSMTPQTV NAYYLPTKNE IVFPAGILQA PFYARNHPKA LNFGGIGVVM 610 620 630 640 650 660 GHELTHAFDD QGREYDKEGN LRPWWQNESL AAFRNHTACM EEQYNQYQVN GERLNGRQTL 670 680 690 700 710 720 GENIADNGGL KAAYNAYKAW LRKHGEEQQL PAVGLTNHQL FFVGFAQVWC SVRTPESSHE 730 740 750 760 GLVTDPHSPA RFRVLGTLSN SRDFLRHFGC PVGSPMNPGQ LCEVW
	Isoform C [UniParc]. Checksum: 77F14FE5AC80E187	FASTA	736	83,322
	10 20 30 40 50 60 MNVALQELGA GSNVGFQKGT RQLLGSRTQL ELVLAGASLL LAALLLGCLV ALGVQYHRDP 70 80 90 100 110 120 SHSTCLTEAC IRVAGKILES LDRGVSPCED FYQFSCGGWI RRNPLPDGRS RWNTFNSLWD 130 140 150 160 170 180 QNQAILKHLL ENTTFNSSSE AEQKTQRFYL SCLQVERIEE LGAQPLRDLI EKIGGWNITG 190 200 210 220 230 240 PWDQDNFMEV LKAVAGTYRA TPFFTVYISA DSKSSNSNVI QVDQSGLFLP SRDYYLNRTA 250 260 270 280 290 300 NEKVLTAYLD YMEELGMLLG GRPTSTREQM QQVLELEIQL ANITVPQDQR RDEEKIYHKM 310 320 330 340 350 360 SISELQALAP SMDWLEFLSF LLSPLELSDS EPVVVYGMDY LQQVSELINR TEPSILNNYL 370 380 390 400 410 420 IWNLVQKTTS SLDRRFESAQ EKLLETLYGT KKSCVPRWQT CISNTDDALG FALGSLFVKA 430 440 450 460 470 480 TFDRQSKEIA EGMISEIRTA FEEALGQLVW MDEKTRQAAK EKADAIYDMI GFPDFILEPK 490 500 510 520 530 540 ELDDVYDGYE ISEDSFFQNM LNLYNFSAKV MADQLRKPPS RDQWSMTPQT VNAYYLPTKN 550 560 570 580 590 600 EIVFPAGILQ APFYARNHPK ALNFGGIGVV MGHELTHAFD DQGREYDKEG NLRPWWQNES 610 620 630 640 650 660 LAAFRNHTAC MEEQYNQYQV NGERLNGRQT LGENIADNGG LKAAYNAYKA WLRKHGEEQQ 670 680 690 700 710 720 LPAVGLTNHQ LFFVGFAQVW CSVRTPESSH EGLVTDPHSP ARFRVLGTLS NSRDFLRHFG 730 CPVGSPMNPG QLCEVW
	Isoform D [UniParc]. Checksum: 39389C81C0798805	FASTA	255	28,306
	10 20 30 40 50 60 MASPGAGRAP PELPERNCGY REVEYWDQRY QGAADSAPYD WFGDFSSFRA LLEPELRPED 70 80 90 100 110 120 RILVLGCGNS ALSYELFLGG FPNVTSVDYS SVVVAAMQAR HAHVPQLRWE TMDVRKLDFP 130 140 150 160 170 180 SASFDVVLEK GTLDALLAGE RDPWTVSSEG VHTVDQVLSE VSRVLVPGGR FISMTSAAPH 190 200 210 220 230 240 FRTRHYAQAY YGWSLRHATY GSGFHFHLYL MHKGGKLSVA QLALGAQILS PPRPPTSPCF 250 LQDSDHEDFL SAIQL
	Isoform 2C [UniParc]. Checksum: 7379F7AFEA937FCE	FASTA	811	91,211
	10 20 30 40 50 60 MNVALQELGA GSNMVEYKRA TLRDEDAPET PVEGGASPDA MEVGKGASPF SPGPSPGMTP 70 80 90 100 110 120 GTPRSSGLFW RVTCPHLRSI SGLCSRTMVG FQKGTRQLLG SRTQLELVLA GASLLLAALL 130 140 150 160 170 180 LGCLVALGVQ YHRDPSHSTC LTEACIRVAG KILESLDRGV SPCEDFYQFS CGGWIRRNPL 190 200 210 220 230 240 PDGRSRWNTF NSLWDQNQAI LKHLLENTTF NSSSEAEQKT QRFYLSCLQV ERIEELGAQP 250 260 270 280 290 300 LRDLIEKIGG WNITGPWDQD NFMEVLKAVA GTYRATPFFT VYISADSKSS NSNVIQVDQS 310 320 330 340 350 360 GLFLPSRDYY LNRTANEKVL TAYLDYMEEL GMLLGGRPTS TREQMQQVLE LEIQLANITV 370 380 390 400 410 420 PQDQRRDEEK IYHKMSISEL QALAPSMDWL EFLSFLLSPL ELSDSEPVVV YGMDYLQQVS 430 440 450 460 470 480 ELINRTEPSI LNNYLIWNLV QKTTSSLDRR FESAQEKLLE TLYGTKKSCV PRWQTCISNT 490 500 510 520 530 540 DDALGFALGS LFVKATFDRQ SKEIAEGMIS EIRTAFEEAL GQLVWMDEKT RQAAKEKADA 550 560 570 580 590 600 IYDMIGFPDF ILEPKELDDV YDGYEISEDS FFQNMLNLYN FSAKVMADQL RKPPSRDQWS 610 620 630 640 650 660 MTPQTVNAYY LPTKNEIVFP AGILQAPFYA RNHPKALNFG GIGVVMGHEL THAFDDQGRE 670 680 690 700 710 720 YDKEGNLRPW WQNESLAAFR NHTACMEEQY NQYQVNGERL NGRQTLGENI ADNGGLKAAY 730 740 750 760 770 780 NAYKAWLRKH GEEQQLPAVG LTNHQLFFVG FAQVWCSVRT PESSHEGLVT DPHSPARFRV 790 800 810 LGTLSNSRDF LRHFGCPVGS PMNPGQLCEV W

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human endothelin converting enzyme-2 (ECE2): characterization of mRNA species and chromosomal localization." Lorenzo M.-N., Khan R.Y., Wang Y., Tai S.C., Chan G.C., Cheung A.H., Marsden P.A. Biochim. Biophys. Acta 1522:46-52(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), NUCLEOTIDE SEQUENCE [MRNA] OF 13-883 (ISOFORM A).
[2]	"Human endothelin-converting enzyme-2C (ECE-2C): a new ECE-2 variant." Funke-Kaiser H., Scheuch K., Behrouzi T., Synowitz M., Draheim N., Schwaneberg B., Thomas A., Zollmann F.S., Paul M., Orzechowski H.D. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C). Tissue: Thalamus.
[3]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Tissue: Brain.
[4]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-101.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D), VARIANT TYR-101. Tissue: Lung and Ovary.
[8]	"Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides." Mzhavia N., Pan H., Che F.-Y., Fricker L.D., Devi L.A. J. Biol. Chem. 278:14704-14711(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, MASS SPECTROMETRY.
[10]	"Alterations in immunological and neurological gene expression patterns in Alzheimer's disease tissues." Weeraratna A.T., Kalehua A., Deleon I., Bertak D., Maher G., Wade M.S., Lustig A., Becker K.G., Wood W. III, Walker D.G., Beach T.G., Taub D.D. Exp. Cell Res. 313:450-461(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"An intact SAM-dependent methyltransferase fold is encoded by the human endothelin-converting enzyme-2 gene." Tempel W., Wu H., Dombrovsky L., Zeng H., Loppnau P., Zhu H., Plotnikov A.N., Bochkarev A. Proteins 74:789-793(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 19-161 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF428263 mRNA. Translation: AAL30386.1. Different initiation.
AF428264 mRNA. Translation: AAL30387.1.
AF192531 mRNA. Translation: AAG28399.1.
AF521189 mRNA. Translation: AAM77664.1.
AB011176 mRNA. Translation: BAA25530.2. Different initiation.
AY359003 mRNA. Translation: AAQ89362.1.
AC061705 Genomic DNA. No translation available.
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78277.1.
BC005835 mRNA. Translation: AAH05835.1.
BC012449 mRNA. Translation: AAH12449.1.
BC069005 mRNA. Translation: AAH69005.1.
BC142950 mRNA. Translation: AAI42951.1.

IPI

IPI00218597.
IPI00219948.
IPI00396198.
IPI00413953.
IPI00472106.

RefSeq

NP_001032401.1. NM_001037324.2.
NP_001093590.1. NM_001100120.1.
NP_001093591.1. NM_001100121.1.
NP_055508.3. NM_014693.3.
NP_115707.2. NM_032331.3.

UniGene

Hs.146161.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PXX	X-ray	1.30	A	19-161	[»]

ProteinModelPortal

O60344.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60344. 2 interactions.

STRING

9606.ENSP00000384223.

Protein family/group databases

MEROPS

M13.003.

PTM databases

PhosphoSite

O60344.

Proteomic databases

PaxDb

O60344.

PRIDE

O60344.

Protocols and materials databases

DNASU

9718.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324557; ENSP00000314295; ENSG00000145194.
ENST00000357474; ENSP00000350066; ENSG00000145194.
ENST00000359140; ENSP00000352052; ENSG00000145194.
ENST00000402825; ENSP00000384223; ENSG00000145194.
ENST00000404464; ENSP00000385846; ENSG00000145194.

GeneID

9718.

KEGG

hsa:9718.

UCSC

uc003fnh.4. human.
uc003fni.4. human.
uc003fnk.4. human.
uc003fnl.4. human.
uc003fnm.4. human.

Organism-specific databases

CTD

9718.

GeneCards

GC03P183967.

H-InvDB

HIX0003914.

HGNC

HGNC:13275. ECE2.

HPA

HPA043346.

MIM

610145. gene.

neXtProt

NX_O60344.

PharmGKB

PA134886910.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3590.

HOVERGEN

HBG005554.

InParanoid

O60344.

KO

K01415.

OMA

AMRNRVA.

OrthoDB

EOG4P2Q1N.

Enzyme and pathway databases

SABIO-RK

O60344.

Gene expression databases

ArrayExpress

O60344.

Bgee

O60344.

CleanEx

HS_ECE2.

Genevestigator

O60344.

GermOnline

ENSG00000145194. Homo sapiens.

Family and domain databases

Gene3D

3.40.390.10. 2 hits.

InterPro

IPR024079. MetalloPept_cat_dom.
IPR013216. Methyltransf_11.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]

PANTHER

PTHR11733. PTHR11733. 1 hit.

Pfam

PF08241. Methyltransf_11. 1 hit.
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

BindingDB

O60344.

ChEMBL

CHEMBL5890.

EvolutionaryTrace

O60344.

GenomeRNAi

9718.

NextBio

36537.

SOURCE

Search...

Entry information

Entry name

ECE2_HUMAN

Accession

Primary (citable) accession number: O60344
Secondary accession number(s): A5PLK8 , Q6NTG7, Q6UW36, Q8NFD7, Q96NX3, Q96NX4, Q9BRZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 127 of the entry and version 4 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.