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EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)]

 EFCE2_MOUSE             Reviewed;         881 AA.
P0DPD9; E9QKA6; Q14BY3; Q80Z59; Q80Z60; Q9D8Q9; Q9D928;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
28-FEB-2018, sequence version 1.
18-JUL-2018, entry version 6.
RecName: Full=EEF1AKMT4-ECE2 readthrough transcript protein {ECO:0000250|UniProtKB:P0DPD8};
EC=3.4.24.71 {ECO:0000250|UniProtKB:P0DPE2};
Includes:
RecName: Full=Methyltransferase-like region {ECO:0000305};
EC=2.1.1.-;
Includes:
RecName: Full=Endothelin-converting enzyme 2 region {ECO:0000305};
EC=3.4.24.71;
Name=Eef1akmt4-Ece2 {ECO:0000250|UniProtKB:P0DPD8};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-881 (ISOFORMS EEF1AKMT4-ECE2-1 AND
EEF1AKMT4-ECE2-2).
PubMed=12054617; DOI=10.1016/S0006-291X(02)00252-8;
Ikeda S., Emoto N., Alimsardjono H., Yokoyama M., Matsuo M.;
"Molecular isolation and characterization of novel four subisoforms of
ECE-2.";
Biochem. Biophys. Res. Commun. 293:421-426(2002).
[3]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=10811845; DOI=10.1172/JCI7447;
Yanagisawa H., Hammer R.E., Richardson J.A., Emoto N., Williams S.C.,
Takeda S., Clouthier D.E., Yanagisawa M.;
"Disruption of ECE-1 and ECE-2 reveals a role for endothelin-
converting enzyme-2 in murine cardiac development.";
J. Clin. Invest. 105:1373-1382(2000).
[4]
FUNCTION.
PubMed=12464614; DOI=10.1074/jbc.C200642200;
Eckman E.A., Watson M., Marlow L., Sambamurti K., Eckman C.B.;
"Alzheimer's disease beta-amyloid peptide is increased in mice
deficient in endothelin-converting enzyme.";
J. Biol. Chem. 278:2081-2084(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 (ISOFORM
EEF1AKMT4-ECE2-2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Converts big endothelin-1 to endothelin-1. May also have
methyltransferase activity (By similarity). May play a role in
amyloid-beta processing (PubMed:12464614).
{ECO:0000250|UniProtKB:P0DPE2, ECO:0000269|PubMed:12464614}.
-!- CATALYTIC ACTIVITY: Hydrolysis of the 21-Trp-|-Val-22 bond in big
endothelin to form endothelin 1. {ECO:0000250|UniProtKB:P0DPE2}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P42892};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42892};
-!- ENZYME REGULATION: Inhibited by phosphoramidon.
{ECO:0000250|UniProtKB:P0DPE2}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:P0DPE2}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle,
secretory vesicle membrane {ECO:0000250|UniProtKB:P0DPE2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Eef1akmt4-Ece2-1; Synonyms=ECE-2a-1
{ECO:0000303|PubMed:12054617};
IsoId=P0DPD9-1, Q80Z60-1;
Sequence=Displayed;
Note=Based on a naturally occurring readthrough transcript which
produces an Eef1akmt4-Ece2 fusion protein. {ECO:0000305};
Name=Eef1akmt4-Ece2-2; Synonyms=ECE-2a-2
{ECO:0000303|PubMed:12054617};
IsoId=P0DPD9-2, Q80Z60-2;
Sequence=VSP_029335;
Note=Based on a naturally occurring readthrough transcript which
produces an Eef1akmt4-Ece2 fusion protein. Contains a
phosphoserine at position 174. {ECO:0000244|PubMed:21183079,
ECO:0000305};
Name=Eef1akmt4-1;
IsoId=P0DPE0-1, Q80Z60-3;
Sequence=External;
Name=Ece2-1;
IsoId=B2RQR8-1; Sequence=External;
Name=Ece2-2;
IsoId=B2RQR8-2; Sequence=External;
-!- TISSUE SPECIFICITY: Expressed at high levels in central nervous
system. Expressed in adrenal glands, ovary and uterus, and at low
levels in heart. {ECO:0000269|PubMed:10811845}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in mesenchyme and parts of
neural tube at E10.5. At E13.5, expressed in anterior part of
neural tube, dorsal root ganglia, bilateral sympathetic trunk and
heart. {ECO:0000269|PubMed:10811845}.
-!- DISRUPTION PHENOTYPE: Eef1akmt4-Ece2 and Ece2 double mutant mice
are fertile and healthy, and do not display any abnormality in
terms of growth or aging. {ECO:0000269|PubMed:10811845}.
-!- SIMILARITY: In the N-terminal section; belongs to the
methyltransferase superfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the peptidase
M13 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAO72356.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAO72357.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF489569; AAO72356.1; ALT_INIT; mRNA.
EMBL; AF489570; AAO72357.1; ALT_INIT; mRNA.
RefSeq; NP_808809.1; NM_177940.1. [P0DPD9-1]
RefSeq; NP_808810.1; NM_177941.1. [P0DPD9-2]
UniGene; Mm.263319; -.
SMR; P0DPD9; -.
STRING; 10090.ENSMUSP00000113475; -.
MEROPS; M13.003; -.
PaxDb; E9QKA6; -.
Ensembl; ENSMUST00000079600; ENSMUSP00000078550; ENSMUSG00000115293. [P0DPD9-1]
Ensembl; ENSMUST00000120394; ENSMUSP00000113475; ENSMUSG00000115293. [P0DPD9-2]
GeneID; 110599584; -.
KEGG; mmu:110599584; -.
CTD; 110599583; -.
MGI; MGI:1101356; Eef1akmt4-Ece2.
eggNOG; KOG2352; Eukaryota.
eggNOG; KOG3624; Eukaryota.
eggNOG; COG3590; LUCA.
GeneTree; ENSGT00760000119162; -.
HOGENOM; HOG000245574; -.
HOVERGEN; HBG005554; -.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
PRO; PR:P0DPD9; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022842; -.
CleanEx; MM_ECE2; -.
Genevisible; E9QKA6; MM.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005802; C:trans-Golgi network; ISS:MGI.
GO; GO:0030658; C:transport vesicle membrane; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0016486; P:peptide hormone processing; ISS:MGI.
CDD; cd08662; M13; 1.
Gene3D; 3.40.390.10; -; 3.
InterPro; IPR029733; ECE1/ECE2.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR000718; Peptidase_M13.
InterPro; IPR018497; Peptidase_M13_C.
InterPro; IPR008753; Peptidase_M13_N.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR11733; PTHR11733; 1.
PANTHER; PTHR11733:SF130; PTHR11733:SF130; 1.
Pfam; PF01431; Peptidase_M13; 1.
Pfam; PF05649; Peptidase_M13_N; 1.
PRINTS; PR00786; NEPRILYSIN.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Methyltransferase; Multifunctional enzyme;
Phosphoprotein; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 881 EEF1AKMT4-ECE2 readthrough transcript
protein.
/FTId=PRO_0000310760.
TOPO_DOM 1 178 Cytoplasmic. {ECO:0000305}.
TRANSMEM 179 199 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 200 881 Lumenal. {ECO:0000305}.
REGION 1 160 Methyltransferase-like region.
{ECO:0000305}.
REGION 88 89 S-adenosyl-L-homocysteine binding.
{ECO:0000250|UniProtKB:P0DPD7}.
REGION 113 114 S-adenosyl-L-homocysteine binding.
{ECO:0000250|UniProtKB:P0DPD7}.
REGION 200 881 Endothelin-converting enzyme 2 region.
{ECO:0000305}.
ACT_SITE 719 719 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 782 782 Proton donor.
{ECO:0000250|UniProtKB:P42892,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 718 718 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 722 722 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 778 778 Zinc; catalytic.
{ECO:0000250|UniProtKB:P42892}.
BINDING 26 26 S-adenosyl-L-homocysteine.
{ECO:0000250|UniProtKB:P0DPD7}.
BINDING 30 30 S-adenosyl-L-homocysteine.
{ECO:0000250|UniProtKB:P0DPD7}.
BINDING 41 41 S-adenosyl-L-homocysteine; via amide
nitrogen. {ECO:0000250|UniProtKB:P0DPD7}.
BINDING 66 66 S-adenosyl-L-homocysteine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P0DPD7}.
BINDING 130 130 S-adenosyl-L-homocysteine.
{ECO:0000250|UniProtKB:P0DPD7}.
MOD_RES 39 39 Phosphotyrosine.
{ECO:0000250|UniProtKB:P0DPD8}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 650 650 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 751 751 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 159 159 S -> SEMVEYKRAKLRDEESPEITVEGRATRDSL (in
isoform Eef1akmt4-Ece2-2).
{ECO:0000303|PubMed:12054617}.
/FTId=VSP_029335.
CONFLICT 359 365 SSNSNII -> RSYSNIT (in Ref. 2; AAO72356/
AAO72357). {ECO:0000305}.
CONFLICT 483 484 TE -> MS (in Ref. 2; AAO72356/AAO72357).
{ECO:0000305}.
CONFLICT 632 632 D -> Y (in Ref. 2; AAO72356/AAO72357).
{ECO:0000305}.
CONFLICT 696 696 A -> P (in Ref. 2; AAO72356/AAO72357).
{ECO:0000305}.
CONFLICT 717 717 G -> D (in Ref. 2; AAO72356/AAO72357).
{ECO:0000305}.
SEQUENCE 881 AA; 99480 MW; 43F512214E293D89 CRC64;
MASPRTPVSP PELPEKNFQY RQVQYWDQRY KDAADSGPYE WFGDFASFRA LLEPELCPED
RILVLGCGNS ALSYELFLGG FPNVTSVDYS PVVVAAMQVR YAHVPSLRWE TMDVRALDFP
SGSFDVVLEK GTLDAMLAGE PDPWNVSSEG VHTVDQVLSE VGFQKRTRQL FGSHTQLELV
LAGLILVLAA LLLGCLVALW VHRDPAHSTC VTEACIRVAG KILESLDRGV SPCQDFYQFS
CGGWIRRNPL PNGRSRWNTF NSLWDQNQAI LKHLLENTTF NSSSEAERKT RSFYLSCLQS
ERIEKLGAKP LRDLIDKIGG WNITGPWDED SFMDVLKAVA GTYRATPFFT VYVSADSKSS
NSNIIQVDQS GLFLPSRDYY LNRTANEKVL TAYLDYMVEL GVLLGGQPTS TREQMQQVLE
LEIQLANITV PQDQRRDEEK IYHKMSISEL QALAPAVDWL EFLSFLLSPL ELGDSEPVVV
YGTEYLQQVS ELINRTEPSI LNNYLIWNLV QKTTSSLDQR FETAQEKLLE TLYGTKKSCT
PRWQTCISNT DDALGFALGS LFVKATFDRQ SKEIAEGMIN EIRSAFEETL GDLVWMDEKT
RLAAKEKADA IYDMIGFPDF ILEPKELDDV YDGYEVSEDS FFQNMLNLYN FSAKVMADQL
RKPPSRDQWS MTPQTVNAYY LPTKNEIVFP AGILQAPFYA HNHPKALNFG GIGVVMGHEL
THAFDDQGRE YDKEGNLRPW WQNESLTAFQ NHTACMEEQY SQYQVNGERL NGLQTLGENI
ADNGGLKAAY NAYKAWLRKH GEEQPLPAVG LTNHQLFFVG FAQVWCSVRT PESSHEGLVT
DPHSPARFRV LGTLSNSRDF LRHFGCPVGS PMNPGQLCEV W


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