ID H2QDA2_PANTR Unreviewed; 813 AA.
AC H2QDA2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=NPEPPS {ECO:0000313|Ensembl:ENSPTRP00000015864.4,
GN ECO:0000313|VGNC:VGNC:14185};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000015864.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000015864.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000015864.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AACZ04040227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04059956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QDA2; -.
DR MEROPS; M01.010; -.
DR Ensembl; ENSPTRT00000017137.4; ENSPTRP00000015864.4; ENSPTRG00000009330.4.
DR VGNC; VGNC:14185; NPEPPS.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000155246; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; H2QDA2; -.
DR OMA; HDMAGFY; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000009330; Expressed in cerebellar cortex and 20 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; 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 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 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR PRINTS; PR00756; ALADIPTASE.
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 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:UP000002277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 179..391
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 472..785
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 813 AA; 90969 MW; 1C059E788281E6BC CRC64;
MGWRPGRGAP HFPEGVAGQR RPPPPGRGGW PGGGCPPPPS GTGRLKQFSC LCLPSSWDYR
RRPLRPANFC IFNFALENVA VLLSSCQSSQ NCEVIFFLIP EIHATGFNYQ NEDEKVTLSF
PSTLQTGKRH SFLVGLQAGA TPPSRIKSFL KRFVATFGPP AFPSAEVGLR KAGFPPPVAA
KTLPFYKDYF NVPYPLPKID LIAIADFAAG AMENWGLVTY RETALLIDPK NSCSSSRQWV
ALVVGHELAH QWFGNLVTME WWTHLWLNEG FASWIEYLCV DHCFPEYDIW TQFVSADYTR
AQELDALDNS HPIEVSVGHP SEVDEIFDAI SYSKGASVIR MLHDYIGDKD FKKGMNMYLT
KFQQKNAATE DLWESLENAS GKPIAAVMNT WTKQMGFPLI YVEAEQVEDD RLLRLSQKKF
CAGGSYVGED CPQWMVPITI STSEDPNQAK LKILMDKPEM NVVLKNVKPD QWVKLNLGTV
GFYRTQYSSA MLESLLPGIR DLSLPPVDRL GLQNDLFSLA RAGIISTVEV LKVMEAFVNE
PNYTVWSDLS CNLGILSTLL SHTDFYEEIQ EFVKDVFSPI GERLGWDPKP GEGHLDALLR
GLVLGKLGKA GHKATLEEAR RRFKDHVEGK QILSADLRSP VYLTVLKHGD GTTLDIMLKL
HKQADMQEEK NRIERVLGAT LLPDLIQKVL TFALSEEVRP QDTVSVIGGV AGGSKHGRKA
AWKFIKDNWE ELYNRYQGGF LISRLIKLSV EGFAVDKMAG EVKAFFESHP APSAERTIQQ
CCENILLNAA WLKRDAESIH QYLLQRKASP PTV
//
