ID Q58EB5_DANRE Unreviewed; 619 AA. AC Q58EB5; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 25-MAY-2022, entry version 78. DE RecName: Full=Glutamyl aminopeptidase {ECO:0000256|ARBA:ARBA00019328}; DE EC=3.4.11.7 {ECO:0000256|ARBA:ARBA00012567}; DE AltName: Full=Aminopeptidase A {ECO:0000256|ARBA:ARBA00029704}; DE Flags: Fragment; GN Name=enpep {ECO:0000313|EMBL:AAH91994.1, GN ECO:0000313|ZFIN:ZDB-GENE-050309-218}; GN Synonyms=im:7152184 {ECO:0000313|ZFIN:ZDB-GENE-050309-218}, GN si:ch211-146m5.2 {ECO:0000313|ZFIN:ZDB-GENE-050309-218}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH91994.1}; RN [1] {ECO:0000313|EMBL:AAH91994.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Singapore local strain {ECO:0000313|EMBL:AAH91994.1}; RC TISSUE=Embryo {ECO:0000313|EMBL:AAH91994.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Regulates central hypertension through its calcium-modulated CC preference to cleave N-terminal acidic residues from peptides such as CC angiotensin II. {ECO:0000256|ARBA:ARBA00002507}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal glutamate (and to a lesser extent CC aspartate) from a peptide.; EC=3.4.11.7; CC Evidence={ECO:0000256|ARBA:ARBA00001703}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR633508-4}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR633508-4}; CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. CC -!- SIMILARITY: Belongs to the peptidase M1 family. CC {ECO:0000256|ARBA:ARBA00010136}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC091994; AAH91994.1; -; mRNA. DR MEROPS; M01.003; -. DR ZFIN; ZDB-GENE-050309-218; enpep. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0070006; F:metalloaminopeptidase activity; IBA:GO_Central. DR GO; GO:0042277; F:peptide binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd09601; M1_APN-Q_like; 1. DR Gene3D; 1.10.390.10; -; 1. DR InterPro; IPR033508; Aminopeptidase_A. DR InterPro; IPR024571; ERAP1-like_C_dom. DR InterPro; IPR034016; M1_APN-typ. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_dom. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR PANTHER; PTHR11533:SF242; PTHR11533:SF242; 1. DR Pfam; PF11838; ERAP1_C; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. PE 2: Evidence at transcript level; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR633508-4}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR633508-4}. FT DOMAIN 3..197 FT /note="Peptidase_M1" FT /evidence="ECO:0000259|Pfam:PF01433" FT DOMAIN 278..597 FT /note="ERAP1_C" FT /evidence="ECO:0000259|Pfam:PF11838" FT ACT_SITE 53 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR633508-1" FT METAL 52 FT /note="Zinc; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR633508-4" FT METAL 56 FT /note="Zinc; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR633508-4" FT METAL 75 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR633508-4" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAH91994.1" SQ SEQUENCE 619 AA; 71325 MW; F0FF5C54C3527562 CRC64; GIQKLDKIAI PDFGTGAMEN WGLITYRETN LLFDEKESSS VNKQRVASVI AHELVHQWFG NIVTMDWWDD LWLNEGFASF FEYIGVEEAE HDWGMRDVML INDVYPVMVD DALLSSHPII VDVSSPAEIT SVFDAISYNK GASILRMLED LLGRDTFRDG CRRYLKTYLF QNAKTSDFWK ALADESGLPV ADIMDTWTKQ MGYPVLSLTN TDTEAKLTQT RFLLDPNADP SQPTTPLGYK WTIPVKWKAL DSTNNSFIFE KGQTEAVISG YSHATNGLIK VNKDHMGFYR VNHHDQMWSD IAEQLLMDHQ VYDATDRSSY IDDIFALGRA DMVDYGNAFN LTRYLADETE YIVWDRVSAS ISYVREMLAD DTVLYPLFQK LFRGHVQKIS RELGWKDEGN QTQRLLREIV LGIACQMGDQ EALDQASDIF NKWIKGTIGS VPVNLRLLVY RYGMMNSGTE ESWEIMFQKY LSATLAQEKD KLLYGLASVK NIHLLHRLLE ATKNESIIRS QDVFTLVQYV SRSSDGKIMA WDWMTLNWDY LVNRYTINDR NLGRLPARIT TTYSSNLQLW KMEHFFALHP NAGAGEMPRK QALETVKNNI EWVDRNKDEI RFWLENNVS //