ID A0A2R9ALQ2_PANPA Unreviewed; 904 AA.
AC A0A2R9ALQ2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ENPEP {ECO:0000313|Ensembl:ENSPPAP00000018078.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000018078.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000018078.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000018078.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AJFE02105156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02105157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02105158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9ALQ2; -.
DR Ensembl; ENSPPAT00000040806.1; ENSPPAP00000018078.1; ENSPPAG00000031975.1.
DR GeneTree; ENSGT00940000156946; -.
DR OMA; NVWSQFV; -.
DR Proteomes; UP000240080; Chromosome 4.
DR Bgee; ENSPPAG00000031975; Expressed in adult mammalian kidney and 4 other cell types or tissues.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
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; GLUTAMYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 46..233
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 268..485
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 563..880
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 834
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT SITE 426
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 904 AA; 103912 MW; B6B51B8C750DE2BE CRC64;
MWCPSLDAVS SHSPSGPPAP DQDICPGSED ESGQWKNFRL PDFVNPVHYD LHVKPLLEED
TYTGTVSISI NLSAPTRYLW LHLRETRITR LPELKKPSGD QVQVRRCFEY KKQEYVVVEA
EEELTPSSGD GLYLLTMEFA GWLNGSLVGF YRTTYTENGQ VKSIAATDHE PTDARKSFPC
FDEPNKKATY TISITHPKEY GALSNMPVAK EESVDDKWTQ TTFEKSVPMS TYLVCFAVHQ
FDSVKRISNS GKPLTIYVQP EQKHTAEYAA NITKSVFDYF EEYFAMNYSL PKLDKIAIPD
FGTGAMENWG LITYRETNLL YDPKESASSN QQRVATVVAH ELVHQWFGNI VTMDWWEDLW
LNEGFASFFE FLGVNHAETD WQMRDQMLLE DVLPVQEDDS LMSSHPIIVT VTTPDEITSV
FDGISYSKGS SILRMLEDWI KPENFQKGCQ IYLEKYQFKN AKTSDFWAAL EEASRLPVKE
VMDTWTRQMG YPVLNVNGVK NITQKRFLLD PRANPSQPPS HLGYTWNIPV KWTEDNITSS
VLFNRSEKEG ITLNSSNPSG NAFLKINPDH IGFYRVNYEV ATWDSIATAL SLNHKTFSSA
DRASLIDDAF ALARAQLLDY KVALNLTKYL KREENFLPWQ RAISAVTYII SMFEDDKELY
PMIEEYFQGQ VKPIADSLGW NDAGDHVTKL LRSSVLGFAC KMGDREALNN ASSLFEQWLN
GTVSLPVNLR LLVYRYGMQN SGNEISWNYT LEQYQKTSLA QEKEKLLYGL ASVKNVTLLS
RYLDLLKDTN LIKTQDVFTV IRYISYNSYG KNMAWNWIQL NWDYLVNRYT LNNRNLGRIV
TIAEPFNTEL QLWQMESFFA KYPQAGAGEK PREQVLETVK NNIEWLKQHR NTIREWFFNL
LESG
//
