ECEL1_RAT
ID ECEL1_RAT Reviewed; 775 AA.
AC Q9JHL3; Q9Z192;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; 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 [MRNA] OF 431-632.
RX PubMed=9931490; DOI=10.1016/s0169-328x(98)00321-0;
RA Valdenaire O., Richards J.G., Faull R.L.M., Schweizer A.;
RT "XCE, a new member of the endothelin-converting enzyme and neutral
RT endopeptidase family, is preferentially expressed in the CNS.";
RL Brain Res. Mol. Brain Res. 64:211-221(1999).
CC -!- FUNCTION: May contribute to the degradation of peptide hormones and be
CC involved in the inactivation of neuronal peptides. Cleaves the
CC synthetic substrate Z-Gly-Gly-Leu-pNA and releases pNA. May protect
CC against C2-ceramide-induced apoptosis.
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; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in the CNS, in particular in
CC neurons of the caudate putamen, diagonal band, the paraventricular
CC nucleus of the thalamus, part of the hypothalamus, in cranial motor
CC nuclei, inferior olive, and substantia gelatinosa of the spinal tract
CC trigeminal nucleus. Not detected in cerebral cortex, hippocampus and
CC cerebellum.
CC -!- INDUCTION: By mechanical damage to nerve cells.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AB026293; BAA95004.1; -; mRNA.
DR EMBL; AB023896; BAA95006.1; -; mRNA.
DR EMBL; Y16188; CAA76114.1; -; mRNA.
DR RefSeq; NP_068544.1; NM_021776.1.
DR AlphaFoldDB; Q9JHL3; -.
DR SMR; Q9JHL3; -.
DR STRING; 10116.ENSRNOP00000026388; -.
DR MEROPS; M13.007; -.
DR GlyGen; Q9JHL3; 3 sites.
DR PaxDb; Q9JHL3; -.
DR GeneID; 60417; -.
DR KEGG; rno:60417; -.
DR UCSC; RGD:61806; rat.
DR CTD; 9427; -.
DR RGD; 61806; Ecel1.
DR eggNOG; KOG3624; Eukaryota.
DR InParanoid; Q9JHL3; -.
DR PhylomeDB; Q9JHL3; -.
DR PRO; PR:Q9JHL3; -.
DR Proteomes; UP000002494; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0003016; P:respiratory system process; ISS: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_0000078226"
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 23..51
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 536
FT /note="L -> F (in Ref. 2; CAA76114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 87944 MW; 0823091F98A41556 CRC64;
MEAPYSMTAH YDEFQEVKYE SRCGTGGARG TSLPPGFPRS SGRSASGARS GLPRWNRREV
CLLSGLVFAA GLCAILAAML ALKYLGPGAA GTGGACPEGC PERKAFARAA RFLSANLDAS
IDPCQDFYSF ACGGWLRRHA IPDDKLTYGT IAAIGEQNEE RLRRLLARPT GGPGGAAQRK
VRAFFRSCLD MREIERLGPR PMLEVIEDCG GWDLGGAADR PGAARWDLNR LLYKAQGVYS
AAALFSLTVS LDDRNSSRYV IRIDQDGLTL PERTLYLAQD EGSEKVLAAY KVFMERLLRL
LGADAVEQKA QEILQLEQRL ANISVSEYDD LRRDVSSVYN KVTLGQLQKI TPHLQWKWLL
DQIFQEDFSE EEEVVLLATD YMQQVSQLIR STPRRILHNY LVWRVVVVLS EHLSPPFREA
LHELAKEMEG NDKPQELARV CLGQANRHFG MALGALFVHE HFSAASKAKV QQLVEDIKYI
LGQRLEELDW MDAQTKAAAR AKLQYMMVMV GYPDFLLKPE AVDKEYEFEV HEKTYLKNIL
NSIRFSIQLS VKKIRQEVDK STWLLPPQAL NAYYLPNKNQ MVFPAGILQP TLYDPDFPQS
LNYGGIGTII GHELTHGYDD WGGQYDRSGN LLHWWTEASY SRFLHKAECI VRLYDNFTVY
NQRVNGKHTL GENIADMGGL KLAYYAYQKW VREHGPEHPL HRLKYTHNQL FFIAFAQNWC
IKRRSQSIYL QVLTDKHAPE HYRVLGSVSQ FEEFGRAFHC PKDSPMNPVH KCSVW
