EFCE2_BOVIN
ID EFCE2_BOVIN Reviewed; 883 AA.
AC P0DPE2; A5PJH8; G8JKW4; Q10711; Q547G8; Q865C4;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=EEF1AKMT4-ECE2 readthrough transcript protein {ECO:0000250|UniProtKB:P0DPD8};
DE EC=3.4.24.71 {ECO:0000269|PubMed:7797512};
DE Includes:
DE RecName: Full=Methyltransferase-like region {ECO:0000305};
DE EC=2.1.1.-;
DE Includes:
DE RecName: Full=Endothelin-converting enzyme 2 region {ECO:0000305};
DE EC=3.4.24.71;
GN Name=EEF1AKMT4-ECE2 {ECO:0000250|UniProtKB:P0DPD8};
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-883 (ISOFORMS EEF1AKMT4-ECE2-1 AND
RP EEF1AKMT4-ECE2-2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-883 (ISOFORM EEF1AKMT4-ECE2-1), ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=7797512; DOI=10.1074/jbc.270.25.15262;
RA Emoto N., Yanagisawa M.;
RT "Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-
RT sensitive metalloprotease with acidic pH optimum.";
RL J. Biol. Chem. 270:15262-15268(1995).
CC -!- FUNCTION: Converts big endothelin-1 to endothelin-1 (PubMed:7797512).
CC May also have methyltransferase activity (Probable).
CC {ECO:0000269|PubMed:7797512, ECO:0000305}.
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:0000269|PubMed:7797512};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P42892};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoramidon.
CC {ECO:0000269|PubMed:7797512}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Inactive at neutral pH.
CC {ECO:0000269|PubMed:7797512};
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=5;
CC Name=EEF1AKMT4-ECE2-1; Synonyms=ECE-2a-1 {ECO:0000303|PubMed:12054617};
CC IsoId=P0DPE2-1, Q10711-1;
CC Sequence=Displayed;
CC Name=EEF1AKMT4-ECE2-2; Synonyms=ECE-2a-2 {ECO:0000303|PubMed:12054617};
CC IsoId=P0DPE2-2, Q10711-2;
CC Sequence=VSP_029331;
CC Name=EEF1AKMT4-1;
CC IsoId=P0DPE1-1, Q10711-5;
CC Sequence=External;
CC Name=ECE2-1; Synonyms=ECE-2b-2;
CC IsoId=F1N476-1, Q10711-4;
CC Sequence=External;
CC Name=ECE2-2; Synonyms=ECE-2b-1;
CC IsoId=F1N476-2, Q10711-3;
CC Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform EEF1AKMT4-ECE2-1 and isoform EEF1AKMT4-
CC ECE2-2 are expressed in liver, kidney, adrenal gland, testis and
CC endothelial cells. {ECO:0000269|PubMed:12054617}.
CC -!- MISCELLANEOUS: [Isoform EEF1AKMT4-ECE2-1]: Based on a naturally
CC occurring readthrough transcript which produces an EEF1AKMT4-ECE2
CC fusion protein. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform EEF1AKMT4-ECE2-2]: Based on a naturally
CC occurring readthrough transcript which produces an EEF1AKMT4-ECE2
CC fusion protein. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M13
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA82927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA82927.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO72360.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO72360.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO72361.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO72361.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DAAA02001884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF489573; AAO72360.1; ALT_SEQ; mRNA.
DR EMBL; AF489574; AAO72361.1; ALT_SEQ; mRNA.
DR EMBL; U27341; AAA82927.1; ALT_SEQ; mRNA.
DR RefSeq; NP_776471.3; NM_174046.4. [P0DPE2-1]
DR RefSeq; NP_808871.3; NM_177956.3. [P0DPE2-2]
DR AlphaFoldDB; P0DPE2; -.
DR SMR; P0DPE2; -.
DR STRING; 9913.ENSBTAP00000042778; -.
DR GeneID; 281134; -.
DR CTD; 9718; -.
DR OrthoDB; 282463at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; ISS:ARUK-UCL.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:ARUK-UCL.
DR GO; GO:0007507; P:heart development; ISS:ARUK-UCL.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR041698; Methyltransf_25.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Methyltransferase; Multifunctional enzyme; Phosphoprotein; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..883
FT /note="EEF1AKMT4-ECE2 readthrough transcript protein"
FT /id="PRO_0000443305"
FT TOPO_DOM 1..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..883
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 211..883
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 1..160
FT /note="Methyltransferase-like region"
FT /evidence="ECO:0000305"
FT ACT_SITE 721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 784
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 720
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 724
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 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 39
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DPD8"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 212..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 235..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 243..828
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 299..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 757..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VAR_SEQ 161
FT /note="A -> MVEYKRATLRDEDAPETPVEGGASPDAVEA (in isoform
FT EEF1AKMT4-ECE2-2)"
FT /evidence="ECO:0000303|PubMed:12054617"
FT /id="VSP_029331"
FT CONFLICT 76
FT /note="I -> L (in Ref. 2; AAO72360/AAO72361 and 3;
FT AAA82927)"
FT CONFLICT 261..262
FT /note="TF -> NS (in Ref. 2; AAO72360/AAO72361 and 3;
FT AAA82927)"
FT CONFLICT 311..312
FT /note="QP -> HA (in Ref. 2; AAO72360/AAO72361 and 3;
FT AAA82927)"
FT CONFLICT 586
FT /note="A -> V (in Ref. 2; AAO72360/AAO72361 and 3;
FT AAA82927)"
FT CONFLICT 707
FT /note="K -> Q (in Ref. 2; AAO72360/AAO72361 and 3;
FT AAA82927)"
SQ SEQUENCE 883 AA; 99637 MW; 711168454AC8F0A7 CRC64;
MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD LLEPELRPLD
RILVLGCGNS ALSYEIFLGG FPDVTSVDYS SVVVAAMRAR YAHVPTLRWE TMDVRALGFP
SGSFDVVLEK GTLDALLTGE QDPWTVSSEG VHTVDQVLNE AGFRKRTSRL LGLHTQLELV
LAGVSLLLAA LLLGCLVALG VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ
FSCGGWIRRN PLPDGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAER KTQRFYLSCL
QVERIEELGA QPLRDLIDKI GGWNVTGPWD QDNFMEVLKA VAGTYRATPF FTVYVSADSK
SSNSNIIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME ELGMLLGGQP TSTREQMRQV
LELEIQLANI TVPQDQRRDE EKIYHKMSIA ELQALAPSMD WLEFLSFLLS PLELGDSEPV
VVYGTDYLQQ VSELINRTEP SVLNNYLIWN LVQKTTSSLD HRFESAQEKL LETLYGTKKS
CTPRWQTCIS NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRAAFEE ALGHLVWMDE
KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEVSE DSFFQNMLNL YNFSAKVMAD
QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF YTCNHPKALN FGGIGVVMGH
ELTHAFDDQG REYDKEGNLR PWWQNESLAA FRNHTACIEE QYSQYQVNGE KLNGRQTLGE
NIADNGGLKA AYNAYKAWLR KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL
VTDPHSPARF RVLGTLSNSR DFLRHFGCPV GSPMNSGQLC EVW
