ID M3W374_FELCA Unreviewed; 961 AA.
AC M3W374;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ERAP1 {ECO:0000313|Ensembl:ENSFCAP00000004594.6,
GN ECO:0000313|VGNC:VGNC:61926};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000004594.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000004594.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004594.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000004594.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004594.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000004594.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004594.6};
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 ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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; AANG04001174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3W374; -.
DR MEROPS; M01.018; -.
DR Ensembl; ENSFCAT00000004966.6; ENSFCAP00000004594.6; ENSFCAG00000004966.6.
DR VGNC; VGNC:61926; ERAP1.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000159086; -.
DR HOGENOM; CLU_003705_2_1_1; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000004966; Expressed in liver and 11 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF156; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; 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|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
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:UP000011712};
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:PIRSR634016-3}.
FT DOMAIN 80..266
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 301..508
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 617..936
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 458
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 961 AA; 109547 MW; 039B0AB2A66EBDFD CRC64;
MCLERCELEL GLQGSVSKKM ISLSVKWPLG TMPLLLSSLL ILLTVSTPSW CQSSDTSSPK
ASNGSPFPWD KIRLPEHISP VHYDLMIHAN LTTLTFEGTT QIEITASQPT TTIILHSHHL
QISKATLRKR VGERLTAEPL RVLEYPLHEQ IALLAPEPLV VGLLYTVVID YAGTLSEHLN
GFYKSTYRTK EGEVRVLAST HFEPTAARMA FPCFDEPSFK ANFSVKIRRE PRHLSISNMP
LVKSVTIAEG LIEDHFDVTV KMSTYLVAFI ISDFKSVSKM TKSGIKVSIY AVPDKIHQAD
YALDAAVTLL EFYEDYFSIP YPLPKQDLAA IPDFESGAME NWGLTTYRES VLLFDSEKSS
ASNKLGITLT VSHELAHQWF GNLVTMEWWN DLWLNEGFAK FMEFVSVTVT HPELKVEDYF
FGKCFDVMEV DALNSSHPVS TAVENPAQIR EMFDEVSYEK GACILNMLRD YLSADAFKSG
IVQYLQKYSY KNTKNEDLWN SMASICPADD TQRMDGFCSR GAHSSSSSHW RQEGLDVKTM
MNTWTLQKGF PLITITVRGR NVHMKQEHYR KGPDDASETG YLWHVPLTFI TSKSDSVQRF
LLKTKTDVLI LPEEVEWIKF NVGMNGYYIV HYEDDGWNSL SGLLRGAHTT ISSNDRASLI
NNAFQLVSNG KLSIEKALDL TLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMKEVENQFK
AFLIRLLRDL IDNQTWTDEG SVSQRMLRSE LLLLACMCKY QPCVQRAEAY FREWKEAGGN
LSLPSDVTLA VFAVGVQNPE GWDFLYSKYQ SSLSSTEKNE IEFALSISQN EGKLQWLLDE
SFKGDKIKIQ EFPHILRAVG RNPVGYPLAW QFLRENWDKL IQKFELGSSS LTNMVIGTTN
QFSTRARLEE VKGFFSSLKE NSSQLRCVQQ TIETIEENIR WMDKNFDKIR VWLQSEKLAL
L
//
