Endothelin-converting enzyme 2 - Bos taurus (Bovine)

Preferred order of sections

Names and origin

Protein names

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

Including the following 2 domains:

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

Gene names

Name:

ECE2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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.
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.
Enzyme regulation	Inhibited by phosphoramidon.
Subunit structure	Homodimer.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein. Cytoplasmic granule membrane; Single-pass type II membrane protein Ref.1.
Tissue specificity	Isoform 1 and isoform 2 are expressed in liver, kidney, adrenal gland, testis and endothelial cells. Isoform 3 and isoform 4 are expressed in brain and adrenal gland. Ref.1
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	pH dependence: Optimum pH is 5.5. Inactive at neutral pH.
Sequence caution	The sequence AAA82927.1 differs from that shown. Reason: Frameshift at position 78. The sequence AAO72360.1 differs from that shown. Reason: Frameshift at position 78. The sequence AAO72361.1 differs from that shown. Reason: Frameshift at position 78.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Methyltransferase Protease Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	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 embryo development Traceable author statement Ref.3. Source: UniProtKB peptide hormone processing Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of G-protein coupled receptor protein signaling pathway Traceable author statement Ref.3. Source: UniProtKB vasoconstriction Traceable author statement Ref.3. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle membrane Inferred from sequence or structural similarity. 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.3. Source: UniProtKB methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q10711-1) Also known as: ECE-2a-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 2 (identifier: Q10711-2) Also known as: ECE-2a-2; The sequence of this isoform differs from the canonical sequence as follows: 161-161: A → MVEYKRATLRDEDAPETPVEGGASPDAVEA

Isoform 3 (identifier: Q10711-3) Also known as: ECE-2b-1; The sequence of this isoform differs from the canonical sequence as follows: 1-160: MACLGPSAQV...VHTVDQVLNE → MRVALQELGGGGN

Isoform 4 (identifier: Q10711-4) Also known as: ECE-2b-2; The sequence of this isoform differs from the canonical sequence as follows: 1-160: MACLGPSAQV...VHTVDQVLNE → MRVALQELGGGGN 161-161: A → MVEYKRATLRDEDAPETPVEGGASPDAVEA

Isoform 5 (identifier: Q10711-5) The sequence of this isoform differs from the canonical sequence as follows: 161-255: AGFRKRTSRL...WIRRNPLPDG → VSRVLVPAGR...HEDFLSAIQL 256-883: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 883

883

Endothelin-converting enzyme 2

PRO_0000078222

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 By similarity

Region

113 – 114

2

S-adenosyl-L-homocysteine binding By similarity

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 By similarity

Binding site

41

1

S-adenosyl-L-homocysteine; via amide nitrogen By similarity

Binding site

66

1

S-adenosyl-L-homocysteine; via carbonyl oxygen By similarity

Binding site

130

1

S-adenosyl-L-homocysteine By similarity

Amino acid modifications

Modified residue

39

1

Phosphotyrosine By similarity

Glycosylation

283

1

N-linked (GlcNAc...) Potential

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

MACLG…QVLNE → MRVALQELGGGGN in isoform 3 and isoform 4.

VSP_029329

Alternative sequence

161 – 255

95

AGFRK…PLPDG → VSRVLVPAGRFISLTSAAPH FRTRHYAQAHYGWSLRHATY GNGFQFHFYLMQKGKELSVA QLAVGAQILSPPRPPTPSCF LQDSDHEDFLSAIQL in isoform 5.

VSP_029330

Alternative sequence

161

1

A → MVEYKRATLRDEDAPETPVE GGASPDAVEA in isoform 2 and isoform 4.

VSP_029331

Alternative sequence

256 – 883

628

Missing in isoform 5.

VSP_029332

Sequences

Sequence		Length	Mass (Da)
Isoform 1 (ECE-2a-1) [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 3079A02496E82BE8 Show »	FASTA	883	99,601
10 20 30 40 50 60 MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD LLEPELRPLD 70 80 90 100 110 120 RILVLGCGNS ALSYELFLGG FPDVTSVDYS SVVVAAMRAR YAHVPTLRWE TMDVRALGFP 130 140 150 160 170 180 SGSFDVVLEK GTLDALLTGE QDPWTVSSEG VHTVDQVLNE AGFRKRTSRL LGLHTQLELV 190 200 210 220 230 240 LAGVSLLLAA LLLGCLVALG VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ 250 260 270 280 290 300 FSCGGWIRRN PLPDGRSRWN NSNSLWDQNQ AILKHLLENT TFNSSSEAER KTQRFYLSCL 310 320 330 340 350 360 QVERIEELGA HALRDLIDKI GGWNVTGPWD QDNFMEVLKA VAGTYRATPF FTVYVSADSK 370 380 390 400 410 420 SSNSNIIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME ELGMLLGGQP TSTREQMRQV 430 440 450 460 470 480 LELEIQLANI TVPQDQRRDE EKIYHKMSIA ELQALAPSMD WLEFLSFLLS PLELGDSEPV 490 500 510 520 530 540 VVYGTDYLQQ VSELINRTEP SVLNNYLIWN LVQKTTSSLD HRFESAQEKL LETLYGTKKS 550 560 570 580 590 600 CTPRWQTCIS NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRVAFEE ALGHLVWMDE 610 620 630 640 650 660 KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEVSE DSFFQNMLNL YNFSAKVMAD 670 680 690 700 710 720 QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF YTCNHPQALN FGGIGVVMGH 730 740 750 760 770 780 ELTHAFDDQG REYDKEGNLR PWWQNESLAA FRNHTACIEE QYSQYQVNGE KLNGRQTLGE 790 800 810 820 830 840 NIADNGGLKA AYNAYKAWLR KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL 850 860 870 880 VTDPHSPARF RVLGTLSNSR DFLRHFGCPV GSPMNSGQLC EVW « Hide
Isoform 2 (ECE-2a-2) [UniParc]. Checksum: 6BA7F597283C189B Show »	FASTA	912	102,717
10 20 30 40 50 60 MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD LLEPELRPLD 70 80 90 100 110 120 RILVLGCGNS ALSYELFLGG FPDVTSVDYS SVVVAAMRAR YAHVPTLRWE TMDVRALGFP 130 140 150 160 170 180 SGSFDVVLEK GTLDALLTGE QDPWTVSSEG VHTVDQVLNE MVEYKRATLR DEDAPETPVE 190 200 210 220 230 240 GGASPDAVEA GFRKRTSRLL GLHTQLELVL AGVSLLLAAL LLGCLVALGV QYHRDPSHST 250 260 270 280 290 300 CLTEACIRVA GKILESLDRG VSPCEDFYQF SCGGWIRRNP LPDGRSRWNN SNSLWDQNQA 310 320 330 340 350 360 ILKHLLENTT FNSSSEAERK TQRFYLSCLQ VERIEELGAH ALRDLIDKIG GWNVTGPWDQ 370 380 390 400 410 420 DNFMEVLKAV AGTYRATPFF TVYVSADSKS SNSNIIQVDQ SGLFLPSRDY YLNRTANEKV 430 440 450 460 470 480 LTAYLDYMEE LGMLLGGQPT STREQMRQVL ELEIQLANIT VPQDQRRDEE KIYHKMSIAE 490 500 510 520 530 540 LQALAPSMDW LEFLSFLLSP LELGDSEPVV VYGTDYLQQV SELINRTEPS VLNNYLIWNL 550 560 570 580 590 600 VQKTTSSLDH RFESAQEKLL ETLYGTKKSC TPRWQTCISN TDDALGFALG SLFVKATFDR 610 620 630 640 650 660 QSKEIAEGMI SEIRVAFEEA LGHLVWMDEK TRQAAKEKAD AIYDMIGFPD FILEPKELDD 670 680 690 700 710 720 VYDGYEVSED SFFQNMLNLY NFSAKVMADQ LRKPPSRDQW SMTPQTVNAY YLPTKNEIVF 730 740 750 760 770 780 PAGILQAPFY TCNHPQALNF GGIGVVMGHE LTHAFDDQGR EYDKEGNLRP WWQNESLAAF 790 800 810 820 830 840 RNHTACIEEQ YSQYQVNGEK LNGRQTLGEN IADNGGLKAA YNAYKAWLRK HGEEQQLPAV 850 860 870 880 890 900 GLTNHQLFFV GFAQVWCSVR TPESSHEGLV TDPHSPARFR VLGTLSNSRD FLRHFGCPVG 910 SPMNSGQLCE VW « Hide
Isoform 3 (ECE-2b-1) [UniParc]. Checksum: 7ECD124469751D91 Show »	FASTA	736	83,129
10 20 30 40 50 60 MRVALQELGG GGNAGFRKRT SRLLGLHTQL ELVLAGVSLL LAALLLGCLV ALGVQYHRDP 70 80 90 100 110 120 SHSTCLTEAC IRVAGKILES LDRGVSPCED FYQFSCGGWI RRNPLPDGRS RWNNSNSLWD 130 140 150 160 170 180 QNQAILKHLL ENTTFNSSSE AERKTQRFYL SCLQVERIEE LGAHALRDLI DKIGGWNVTG 190 200 210 220 230 240 PWDQDNFMEV LKAVAGTYRA TPFFTVYVSA DSKSSNSNII QVDQSGLFLP SRDYYLNRTA 250 260 270 280 290 300 NEKVLTAYLD YMEELGMLLG GQPTSTREQM RQVLELEIQL ANITVPQDQR RDEEKIYHKM 310 320 330 340 350 360 SIAELQALAP SMDWLEFLSF LLSPLELGDS EPVVVYGTDY LQQVSELINR TEPSVLNNYL 370 380 390 400 410 420 IWNLVQKTTS SLDHRFESAQ EKLLETLYGT KKSCTPRWQT CISNTDDALG FALGSLFVKA 430 440 450 460 470 480 TFDRQSKEIA EGMISEIRVA FEEALGHLVW MDEKTRQAAK EKADAIYDMI GFPDFILEPK 490 500 510 520 530 540 ELDDVYDGYE VSEDSFFQNM LNLYNFSAKV MADQLRKPPS RDQWSMTPQT VNAYYLPTKN 550 560 570 580 590 600 EIVFPAGILQ APFYTCNHPQ ALNFGGIGVV MGHELTHAFD DQGREYDKEG NLRPWWQNES 610 620 630 640 650 660 LAAFRNHTAC IEEQYSQYQV NGEKLNGRQT LGENIADNGG LKAAYNAYKA WLRKHGEEQQ 670 680 690 700 710 720 LPAVGLTNHQ LFFVGFAQVW CSVRTPESSH EGLVTDPHSP ARFRVLGTLS NSRDFLRHFG 730 CPVGSPMNSG QLCEVW « Hide
Isoform 4 (ECE-2b-2) [UniParc]. Checksum: 12C3FE747881E1FF Show »	FASTA	765	86,244
10 20 30 40 50 60 MRVALQELGG GGNMVEYKRA TLRDEDAPET PVEGGASPDA VEAGFRKRTS RLLGLHTQLE 70 80 90 100 110 120 LVLAGVSLLL AALLLGCLVA LGVQYHRDPS HSTCLTEACI RVAGKILESL DRGVSPCEDF 130 140 150 160 170 180 YQFSCGGWIR RNPLPDGRSR WNNSNSLWDQ NQAILKHLLE NTTFNSSSEA ERKTQRFYLS 190 200 210 220 230 240 CLQVERIEEL GAHALRDLID KIGGWNVTGP WDQDNFMEVL KAVAGTYRAT PFFTVYVSAD 250 260 270 280 290 300 SKSSNSNIIQ VDQSGLFLPS RDYYLNRTAN EKVLTAYLDY MEELGMLLGG QPTSTREQMR 310 320 330 340 350 360 QVLELEIQLA NITVPQDQRR DEEKIYHKMS IAELQALAPS MDWLEFLSFL LSPLELGDSE 370 380 390 400 410 420 PVVVYGTDYL QQVSELINRT EPSVLNNYLI WNLVQKTTSS LDHRFESAQE KLLETLYGTK 430 440 450 460 470 480 KSCTPRWQTC ISNTDDALGF ALGSLFVKAT FDRQSKEIAE GMISEIRVAF EEALGHLVWM 490 500 510 520 530 540 DEKTRQAAKE KADAIYDMIG FPDFILEPKE LDDVYDGYEV SEDSFFQNML NLYNFSAKVM 550 560 570 580 590 600 ADQLRKPPSR DQWSMTPQTV NAYYLPTKNE IVFPAGILQA PFYTCNHPQA LNFGGIGVVM 610 620 630 640 650 660 GHELTHAFDD QGREYDKEGN LRPWWQNESL AAFRNHTACI EEQYSQYQVN GEKLNGRQTL 670 680 690 700 710 720 GENIADNGGL KAAYNAYKAW LRKHGEEQQL PAVGLTNHQL FFVGFAQVWC SVRTPESSHE 730 740 750 760 GLVTDPHSPA RFRVLGTLSN SRDFLRHFGC PVGSPMNSGQ LCEVW « Hide
Isoform 5 [UniParc]. Checksum: 2B7566ABDFED9C0F Show »	FASTA	255	28,396
10 20 30 40 50 60 MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD LLEPELRPLD 70 80 90 100 110 120 RILVLGCGNS ALSYELFLGG FPDVTSVDYS SVVVAAMRAR YAHVPTLRWE TMDVRALGFP 130 140 150 160 170 180 SGSFDVVLEK GTLDALLTGE QDPWTVSSEG VHTVDQVLNE VSRVLVPAGR FISLTSAAPH 190 200 210 220 230 240 FRTRHYAQAH YGWSLRHATY GNGFQFHFYL MQKGKELSVA QLAVGAQILS PPRPPTPSCF 250 LQDSDHEDFL SAIQL « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular isolation and characterization of novel four subisoforms of ECE-2." Ikeda S., Emoto N., Alimsardjono H., Yokoyama M., Matsuo M. Biochem. Biophys. Res. Commun. 293:421-426(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [MRNA] OF 59-883 (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Strain: Hereford. Tissue: Thymus.
[3]	"Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum." Emoto N., Yanagisawa M. J. Biol. Chem. 270:15262-15268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-883 (ISOFORM 1).

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF489573 mRNA. Translation: AAO72360.1. Frameshift. AF489574 mRNA. Translation: AAO72361.1. Frameshift. BC142117 mRNA. Translation: AAI42118.1. U27341 mRNA. Translation: AAA82927.1. Frameshift.
IPI	IPI00691881. IPI00696952. IPI00711229. IPI00854347. IPI01017646.
RefSeq	NP_776471.2. NM_174046.3. NP_808871.2. NM_177956.2.
UniGene	Bt.4840.
3D structure databases
ProteinModelPortal	Q10711.
SMR	Q10711. Positions 19-160.
ModBase	Search...
Protein family/group databases
MEROPS	M13.003.
Proteomic databases
PRIDE	Q10711.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281134.
KEGG	bta:281134.
Organism-specific databases
CTD	9718.
Phylogenomic databases
eggNOG	COG3590.
HOGENOM	HOG000245574.
HOVERGEN	HBG005554.
KO	K01415.
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
ChEMBL	CHEMBL3850.
NextBio	20805201.

Entry information

Entry name

ECE2_BOVIN

Accession

Primary (citable) accession number: Q10711
Secondary accession number(s): A5PJH8, Q547G8, Q865C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 13, 2007
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents