ECE2_BOVIN
ID ECE2_BOVIN Reviewed; 765 AA.
AC F1N476; Q865C2; Q865C3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Endothelin-converting enzyme 2 {ECO:0000250|UniProtKB:P0DPD6};
DE Short=ECE-2;
DE EC=3.4.24.71 {ECO:0000250|UniProtKB:P0DPD6};
GN Name=ECE2 {ECO:0000250|UniProtKB:P0DPD6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ECE2-1 AND ECE2-2), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=12054617; DOI=10.1016/s0006-291x(02)00252-8;
RA Ikeda S., Emoto N., Alimsardjono H., Yokoyama M., Matsuo M.;
RT "Molecular isolation and characterization of novel four subisoforms of ECE-
RT 2.";
RL Biochem. Biophys. Res. Commun. 293:421-426(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Converts big endothelin-1 to endothelin-1. Also involved in
CC the processing of various neuroendocrine peptides, including
CC neurotensin, angiotensin I, substance P, proenkephalin-derived
CC peptides, and prodynorphin-derived peptides (By similarity). May play a
CC role in amyloid-beta processing (By similarity).
CC {ECO:0000250|UniProtKB:B2RQR8, ECO:0000250|UniProtKB:P0DPD6}.
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 Evidence={ECO:0000250|UniProtKB:P0DPD6};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12054617}; Single-pass type II membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:12054617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=ECE2-1; Synonyms=ECE-2b-2 {ECO:0000303|PubMed:12054617};
CC IsoId=F1N476-1, Q10711-4;
CC Sequence=Displayed;
CC Name=ECE2-2; Synonyms=ECE-2b-1 {ECO:0000303|PubMed:12054617};
CC IsoId=F1N476-2, Q10711-3;
CC Sequence=VSP_059327;
CC Name=EEF1AKMT4-ECE2-1; Synonyms=ECE-2a-1;
CC IsoId=P0DPE2-1, Q10711-1;
CC Sequence=External;
CC Name=EEF1AKMT4-ECE2-2; Synonyms=ECE-2a-2;
CC IsoId=P0DPE2-2, Q10711-2;
CC Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform ECE2-1 and isoform ECE2-2 are expressed in
CC brain and adrenal gland. {ECO:0000269|PubMed:12054617}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AF489575; AAO72362.1; -; mRNA.
DR EMBL; AF489576; AAO72363.1; -; mRNA.
DR EMBL; DAAA02001884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_808872.2; NM_177957.3. [F1N476-2]
DR RefSeq; NP_808873.2; NM_177958.3. [F1N476-1]
DR AlphaFoldDB; F1N476; -.
DR SMR; F1N476; -.
DR MEROPS; M13.003; -.
DR Ensembl; ENSBTAT00000007435; ENSBTAP00000007435; ENSBTAG00000005658. [F1N476-1]
DR Ensembl; ENSBTAT00000064205; ENSBTAP00000053896; ENSBTAG00000005658. [F1N476-2]
DR GeneID; 281134; -.
DR CTD; 9718; -.
DR VEuPathDB; HostDB:ENSBTAG00000005658; -.
DR GeneTree; ENSGT00940000156921; -.
DR OMA; FGWAQVW; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000005658; Expressed in adenohypophysis and 96 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030658; C:transport vesicle membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
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 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 Alternative splicing; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..765
FT /note="Endothelin-converting enzyme 2"
FT /id="PRO_0000443295"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 82..765
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 93..765
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 666
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 602
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 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 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
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 94..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 117..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 125..710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 181..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 639..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VAR_SEQ 14..42
FT /note="Missing (in isoform ECE2-2)"
FT /id="VSP_059327"
FT CONFLICT 2
FT /note="S -> R (in Ref. 1; AAO72363/AAO72362)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="TF -> NS (in Ref. 1; AAO72363/AAO72362)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..194
FT /note="QP -> HA (in Ref. 1; AAO72363/AAO72362)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="A -> V (in Ref. 1; AAO72363/AAO72362)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="K -> Q (in Ref. 1; AAO72363/AAO72362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 86211 MW; 416F58103F2D6A72 CRC64;
MSVALQELGG GGNMVEYKRA TLRDEDAPET PVEGGASPDA VEAGFRKRTS RLLGLHTQLE
LVLAGVSLLL AALLLGCLVA LGVQYHRDPS HSTCLTEACI RVAGKILESL DRGVSPCEDF
YQFSCGGWIR RNPLPDGRSR WNTFNSLWDQ NQAILKHLLE NTTFNSSSEA ERKTQRFYLS
CLQVERIEEL GAQPLRDLID KIGGWNVTGP WDQDNFMEVL KAVAGTYRAT PFFTVYVSAD
SKSSNSNIIQ VDQSGLFLPS RDYYLNRTAN EKVLTAYLDY MEELGMLLGG QPTSTREQMR
QVLELEIQLA NITVPQDQRR DEEKIYHKMS IAELQALAPS MDWLEFLSFL LSPLELGDSE
PVVVYGTDYL QQVSELINRT EPSVLNNYLI WNLVQKTTSS LDHRFESAQE KLLETLYGTK
KSCTPRWQTC ISNTDDALGF ALGSLFVKAT FDRQSKEIAE GMISEIRAAF EEALGHLVWM
DEKTRQAAKE KADAIYDMIG FPDFILEPKE LDDVYDGYEV SEDSFFQNML NLYNFSAKVM
ADQLRKPPSR DQWSMTPQTV NAYYLPTKNE IVFPAGILQA PFYTCNHPKA LNFGGIGVVM
GHELTHAFDD QGREYDKEGN LRPWWQNESL AAFRNHTACI EEQYSQYQVN GEKLNGRQTL
GENIADNGGL KAAYNAYKAW LRKHGEEQQL PAVGLTNHQL FFVGFAQVWC SVRTPESSHE
GLVTDPHSPA RFRVLGTLSN SRDFLRHFGC PVGSPMNSGQ LCEVW
