ID   A0A2K6NIE4_RHIRO        Unreviewed;       548 AA.
AC   A0A2K6NIE4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Endoplasmic reticulum aminopeptidase 1 {ECO:0000313|Ensembl:ENSRROP00000004041.1};
GN   Name=ERAP1 {ECO:0000313|Ensembl:ENSRROP00000004041.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000004041.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000004041.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
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   AlphaFoldDB; A0A2K6NIE4; -.
DR   Ensembl; ENSRROT00000018114.1; ENSRROP00000004041.1; ENSRROG00000016179.1.
DR   GeneTree; ENSGT00940000159086; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 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; 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:SF156; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..548
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014349026"
FT   DOMAIN          60..246
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          281..484
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            438
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   548 AA;  61352 MW;  55790C387AE701FA CRC64;
     MVFPSLKWSL PTMSFLPSLL LALLTVSTPS WCQSSEASPK GSNGMPFPWN KIRLPEYVIP
     VHYDLLIHAN LTTLTFWGTT EVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL
     QVLEHPPQEQ IALLAPEPLL VGLLYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST
     QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV
     KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL DFYEDYFNIP
     YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSP ASSKLGITMI VAHELAHQWF
     GNLVTMEWWS DLWLNEGFAK FMEFVSVSVT HPELKVEDYF FGKCFDAMEV DALNSSHPVS
     TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD
     SMASICPTDG VKGMDGFCSG SQHSSSFSVP VACSIDVHHQ QIRHGPSIFA KNKNRCAHPP
     RRGGMDQI
//