EFCE2_HUMAN
ID EFCE2_HUMAN Reviewed; 883 AA.
AC P0DPD8; A5PLK8; O60344; Q6NTG7; Q6UW36; Q8NFD7; Q96NX3; Q96NX4; Q9BRZ8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=EEF1AKMT4-ECE2 readthrough transcript protein {ECO:0000305};
DE EC=3.4.24.71 {ECO:0000250|UniProtKB:P0DPE2};
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:0000312|HGNC:HGNC:53615};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-883 (ISOFORM EEF1AKMT4-ECE2-1), AND
RP ALTERNATIVE SPLICING.
RX PubMed=11718899; DOI=10.1016/s0167-4781(01)00283-4;
RA Lorenzo M.-N., Khan R.Y., Wang Y., Tai S.C., Chan G.C., Cheung A.H.,
RA Marsden P.A.;
RT "Human endothelin converting enzyme-2 (ECE2): characterization of mRNA
RT species and chromosomal localization.";
RL Biochim. Biophys. Acta 1522:46-52(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
CC -!- FUNCTION: Converts big endothelin-1 to endothelin-1. May also have
CC methyltransferase activity (By similarity). May play a role in amyloid-
CC beta processing (By similarity). {ECO:0000250|UniProtKB:P0DPD9,
CC ECO:0000250|UniProtKB:P0DPE2}.
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:P0DPE2};
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:0000250|UniProtKB:P0DPE2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P0DPE2}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P0DPE2}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:P0DPE2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=EEF1AKMT4-ECE2-1; Synonyms=ECE-2A {ECO:0000303|PubMed:11718899};
CC IsoId=P0DPD8-1, O60344-1;
CC Sequence=Displayed;
CC Name=ECE2-1; Synonyms=ECE2-2C;
CC IsoId=P0DPD6-4, O60344-5;
CC Sequence=External;
CC Name=ECE2-2; Synonyms=ECE-2B;
CC IsoId=P0DPD6-2, O60344-2;
CC Sequence=External;
CC Name=ECE2-3;
CC IsoId=P0DPD6-3, O60344-3;
CC Sequence=External;
CC Name=EEF1AKMT4-1;
CC IsoId=P0DPD7-4, O60344-4;
CC Sequence=External;
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 -!- 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=AAL30386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC061705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF428263; AAL30386.1; ALT_INIT; mRNA.
DR CCDS; CCDS3256.2; -.
DR RefSeq; NP_001032401.1; NM_001037324.2.
DR RefSeq; NP_001093590.1; NM_001100120.1.
DR RefSeq; NP_001093591.1; NM_001100121.1.
DR RefSeq; NP_055508.3; NM_014693.3. [P0DPD8-1]
DR AlphaFoldDB; P0DPD8; -.
DR SMR; P0DPD8; -.
DR STRING; 9606.ENSP00000384223; -.
DR BindingDB; P0DPD8; -.
DR GlyGen; P0DPD8; 10 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P0DPD8; -.
DR PhosphoSitePlus; P0DPD8; -.
DR jPOST; P0DPD8; -.
DR MassIVE; P0DPD8; -.
DR MaxQB; P0DPD8; -.
DR PeptideAtlas; P0DPD8; -.
DR PRIDE; P0DPD8; -.
DR Antibodypedia; 81501; 15 antibodies from 1 providers.
DR DNASU; 9718; -.
DR Ensembl; ENST00000402825.7; ENSP00000384223.3; ENSG00000284917.1. [P0DPD8-1]
DR GeneID; 110599583; -.
DR GeneID; 9718; -.
DR KEGG; hsa:110599583; -.
DR KEGG; hsa:9718; -.
DR CTD; 110599583; -.
DR CTD; 9718; -.
DR DisGeNET; 110599583; -.
DR DisGeNET; 9718; -.
DR GeneCards; EEF1AKMT4-ECE2; -.
DR HGNC; HGNC:53615; EEF1AKMT4-ECE2.
DR HPA; ENSG00000284917; Not detected.
DR MIM; 610145; gene.
DR neXtProt; NX_P0DPD8; -.
DR VEuPathDB; HostDB:ENSG00000284917; -.
DR GeneTree; ENSGT00940000156921; -.
DR OMA; FGWAQVW; -.
DR OrthoDB; 282463at2759; -.
DR PathwayCommons; P0DPD8; -.
DR SignaLink; P0DPD8; -.
DR ChiTaRS; EEF1AKMT4-ECE2; human.
DR Pharos; P0DPD8; Tdark.
DR PRO; PR:P0DPD8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000284917; Expressed in prefrontal cortex and 27 other tissues.
DR GO; GO:0000139; C:Golgi membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
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: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; Transferase; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..883
FT /note="EEF1AKMT4-ECE2 readthrough transcript protein"
FT /id="PRO_0000078223"
FT TOPO_DOM 1..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
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:0007744|PubMed:15592455"
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"
SQ SEQUENCE 883 AA; 99773 MW; EE1C0F4AA4C6B225 CRC64;
MASPGAGRAP PELPERNCGY REVEYWDQRY QGAADSAPYD WFGDFSSFRA LLEPELRPED
RILVLGCGNS ALSYELFLGG FPNVTSVDYS SVVVAAMQAR HAHVPQLRWE TMDVRKLDFP
SASFDVVLEK GTLDALLAGE RDPWTVSSEG VHTVDQVLSE VGFQKGTRQL LGSRTQLELV
LAGASLLLAA LLLGCLVALG VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ
FSCGGWIRRN PLPDGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAEQ KTQRFYLSCL
QVERIEELGA QPLRDLIEKI GGWNITGPWD QDNFMEVLKA VAGTYRATPF FTVYISADSK
SSNSNVIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME ELGMLLGGRP TSTREQMQQV
LELEIQLANI TVPQDQRRDE EKIYHKMSIS ELQALAPSMD WLEFLSFLLS PLELSDSEPV
VVYGMDYLQQ VSELINRTEP SILNNYLIWN LVQKTTSSLD RRFESAQEKL LETLYGTKKS
CVPRWQTCIS NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRTAFEE ALGQLVWMDE
KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEISE DSFFQNMLNL YNFSAKVMAD
QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF YARNHPKALN FGGIGVVMGH
ELTHAFDDQG REYDKEGNLR PWWQNESLAA FRNHTACMEE QYNQYQVNGE RLNGRQTLGE
NIADNGGLKA AYNAYKAWLR KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL
VTDPHSPARF RVLGTLSNSR DFLRHFGCPV GSPMNPGQLC EVW
