ECE_LOCMI
ID ECE_LOCMI Reviewed; 727 AA.
AC Q8IS64;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Endothelin-converting enzyme homolog {ECO:0000305|PubMed:12752656, ECO:0000312|EMBL:AAN73018.1};
DE Short=ECE {ECO:0000303|PubMed:12752656};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:P42892};
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004 {ECO:0000312|EMBL:AAN73018.1};
RN [1] {ECO:0000312|EMBL:AAN73018.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000303|PubMed:12752656};
RX PubMed=12752656; DOI=10.1046/j.1365-2583.2003.00406.x;
RA Macours N., Poels J., Hens K., Luciani N., De Loof A., Huybrechts R.;
RT "An endothelin-converting enzyme homologue in the locust, Locusta
RT migratoria: functional activity, molecular cloning and tissue
RT distribution.";
RL Insect Mol. Biol. 12:233-240(2003).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P42892};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P42892};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and midgut, and to a
CC lesser extent in fat body, ovaries, testes and haemocytes.
CC {ECO:0000269|PubMed:12752656}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AY149919; AAN73018.1; -; mRNA.
DR AlphaFoldDB; Q8IS64; -.
DR SMR; Q8IS64; -.
DR MEROPS; M13.A14; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
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 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 Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..727
FT /note="Endothelin-converting enzyme homolog"
FT /id="PRO_0000439041"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 66..727
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 46..727
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 628
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 564
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 568
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 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 47..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 70..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 78..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 134..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 601..724
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ SEQUENCE 727 AA; 83112 MW; B929AA73AA16228C CRC64;
MSFNFSRYSG AYTTTFSFLL LALLIVSAVL LSRPYAPALL HAEEAYCVSM SCVTAAASVL
SLMDATADPC SDFYQYACGG WVRANPIPDT KSMWGTFVKL EQQNQLVIKN VLEQPMSEFK
SEAERKAKLY YMSCLDVNDT IETLGPKPML DLLVKIGGWN ITGNFSIKNW SLQKSLETLQ
NRYNMGGLFT WAVGEDDRDS KKHIIQIDQG GLTLPTRDNY LNETMDDKVL SAYLEYMTKI
GVLLGGEEKN VRTQMKAVIE FETELAKIMS PQEDRRDEEK LYNNMELDKV QGRPPFINWH
AFFSNAMENI TRKISKKEKV VVYAPEYLEK LNDIIRNYTN TTDGKIILNN YLVWQTVRSM
TSYLSKAFRD AYKGLRKALV GSEGGEKPWR YCVTDTNNVI GFAIGAMFVR EAFHGNSKPA
AENMINQIRT AFKSNLKNLK WMDAETRRAA EKKADAISDM IGFPDYILNP EELDKKYKDL
EIKEDEYFEN NLRVNKYNLK SNLEKLDQPV NKTRWGMTPP TVNAYYTPTK NQIVFPAGIL
QAPFYDIGHP KSMNYGAMGV VMGHELTHAF DDQGREYDQN GNLHKWWNNQ TIEAFKKRTQ
CVVDQYSNYT VDNKHVNGKQ TLGENIADNG GLKAAYHAYL EWEQRNPREL PLPGLNFSHK
QLFFLSFAQV WCSASTDEAI KLQLEKDPHA PPKFRVIGPL SNLQEFSTEF RCPLGSKMNP
VHKCEVW
