ECEL1_MOUSE
ID ECEL1_MOUSE Reviewed; 775 AA.
AC Q9JMI0; Q6PFG4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Endothelin-converting enzyme-like 1;
DE EC=3.4.24.-;
DE AltName: Full=Damage-induced neuronal endopeptidase;
DE AltName: Full=Xce protein;
GN Name=Ecel1; Synonyms=Dine, Xce;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10759559; DOI=10.1073/pnas.070509897;
RA Kiryu-Seo S., Sasaki M., Yokohama H., Nakagomi S., Hirayama T., Aoki S.,
RA Wada K., Kiyama H.;
RT "Damage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase
RT expressed in response to neuronal damage and activates superoxide
RT scavengers.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4345-4350(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10400672; DOI=10.1074/jbc.274.29.20450;
RA Schweizer A., Valdenaire O., Koster A., Lang Y., Schmitt G., Lenz B.,
RA Bluethmann H., Rohrer J.;
RT "Neonatal lethality in mice deficient in XCE, a novel member of the
RT endothelin-converting enzyme and neutral endopeptidase family.";
RL J. Biol. Chem. 274:20450-20456(1999).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=23261301; DOI=10.1016/j.ajhg.2012.11.014;
RG University of Washington Center for Mendelian Genomics;
RA McMillin M.J., Below J.E., Shively K.M., Beck A.E., Gildersleeve H.I.,
RA Pinner J., Gogola G.R., Hecht J.T., Grange D.K., Harris D.J., Earl D.L.,
RA Jagadeesh S., Mehta S.G., Robertson S.P., Swanson J.M., Faustman E.M.,
RA Mefford H.C., Shendure J., Nickerson D.A., Bamshad M.J.;
RT "Mutations in ECEL1 cause distal arthrogryposis type 5D.";
RL Am. J. Hum. Genet. 92:150-156(2013).
CC -!- FUNCTION: May contribute to the degradation of peptide hormones and be
CC involved in the inactivation of neuronal peptides.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: According to a report, mice die of respiratory
CC failure shortly after birth (PubMed:10400672). According to a second
CC report, mice exhibit perturbed terminal branching of motor neurons to
CC the endplate of skeletal muscles, resulting in poor formation of the
CC neuromuscular junction (PubMed:23261301). {ECO:0000269|PubMed:10400672,
CC ECO:0000269|PubMed:23261301}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AB026294; BAA95005.1; -; mRNA.
DR EMBL; CH466520; EDL40189.1; -; Genomic_DNA.
DR EMBL; BC057569; AAH57569.1; -; mRNA.
DR CCDS; CCDS15128.1; -.
DR RefSeq; NP_001264854.1; NM_001277925.1.
DR RefSeq; NP_067281.2; NM_021306.3.
DR RefSeq; XP_017170387.1; XM_017314898.1.
DR RefSeq; XP_017170391.1; XM_017314902.1.
DR RefSeq; XP_017170392.1; XM_017314903.1.
DR AlphaFoldDB; Q9JMI0; -.
DR SMR; Q9JMI0; -.
DR BioGRID; 199364; 3.
DR IntAct; Q9JMI0; 1.
DR STRING; 10090.ENSMUSP00000125557; -.
DR MEROPS; M13.007; -.
DR GlyGen; Q9JMI0; 3 sites.
DR iPTMnet; Q9JMI0; -.
DR PhosphoSitePlus; Q9JMI0; -.
DR MaxQB; Q9JMI0; -.
DR PaxDb; Q9JMI0; -.
DR PRIDE; Q9JMI0; -.
DR ProteomicsDB; 275429; -.
DR Antibodypedia; 47689; 53 antibodies from 13 providers.
DR DNASU; 13599; -.
DR Ensembl; ENSMUST00000027463; ENSMUSP00000027463; ENSMUSG00000026247.
DR Ensembl; ENSMUST00000160810; ENSMUSP00000125557; ENSMUSG00000026247.
DR Ensembl; ENSMUST00000161002; ENSMUSP00000125096; ENSMUSG00000026247.
DR GeneID; 13599; -.
DR KEGG; mmu:13599; -.
DR UCSC; uc007bwc.2; mouse.
DR CTD; 9427; -.
DR MGI; MGI:1343461; Ecel1.
DR VEuPathDB; HostDB:ENSMUSG00000026247; -.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000157673; -.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; Q9JMI0; -.
DR OMA; MHKVSDL; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; Q9JMI0; -.
DR TreeFam; TF315192; -.
DR BioGRID-ORCS; 13599; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9JMI0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JMI0; protein.
DR Bgee; ENSMUSG00000026247; Expressed in facial nucleus and 87 other tissues.
DR Genevisible; Q9JMI0; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0003016; P:respiratory system process; IMP:UniProtKB.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR029736; ECEL1.
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 PANTHER; PTHR11733:SF195; PTHR11733:SF195; 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 Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..775
FT /note="Endothelin-converting enzyme-like 1"
FT /id="PRO_0000078225"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..775
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 99..775
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 676
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 612
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 616
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 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 132..720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 188..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 649..772
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CONFLICT 562
FT /note="S -> T (in Ref. 1; BAA95005)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="F -> Y (in Ref. 1; BAA95005)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="T -> A (in Ref. 1; BAA95005)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="H -> R (in Ref. 1; BAA95005)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="R -> H (in Ref. 1; BAA95005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 87993 MW; 37ACB98A53E5B48B CRC64;
MEAPYSMTAH YDEFQEVKYV SRCGTGGARG TSLPPGFPRG SGRSASGSRS GLPRWNRREV
CLLSGLVFAA GLCAILAAML ALKYLGPGAA GGGGACPEGC PERKAFARAA RFLSANLDAS
IDPCQDFYSF ACGGWLRRHA IPDDKLTYGT IAAIGEQNEE RLRRLLARPT GGPGGAAQRK
VRAFFRSCLD MREIERLGPR PMLEVIEDCG GWDLGGAADR PGAARWDLNR LLYKAQGVYS
AAALFSLTVS LDDRNSSRYV IRIDQDGLTL PERTLYLAQD EESEKILAAY RVFMQRLLRL
LGADAVEQKA QEILQLEQRL ANISVSEYDD LRRDVSSAYN KVTLGQLQKI IPHLQWKWLL
DQIFQEDFSE EEEVVLLATD YMQQVSQLIR STPRRILHNY LVWRVVVVLS EHLSSPFREA
LHELAKEMEG NDKPQELARV CLGQANRHFG MALGALFVHE HFSAASKAKV QQLVEDIKYI
LGQRLEELDW MDAQTKAAAR AKLQYMMVMV GYPDFLLKPE AVDKEYEFEV HEKTYFKNIL
NSIRFSIQLS VKKIRQEVDK SSWLLPPQAL NAYYLPNKNQ MVFPAGILQP TLYDPDFPQS
LNYGGIGTII GHELTHGYDD WGGQYDRSGN LLHWWTETSY SHFLRKAECI VRLYDNFTVY
NQRVNGKHTL GENIADMGGL KLAYYAYQKW VREHGPEHPL HRLKYTHNQL FFIAFAQNWC
IKRRSQSIYL QVLTDKHAPE HYRVLGSVSQ FEEFGRAFHC PKDSPMNPVH KCSVW
