PEPL1_PONAB
ID PEPL1_PONAB Reviewed; 523 AA.
AC Q5R7G6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable aminopeptidase NPEPL1;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase-like 1;
GN Name=NPEPL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably catalyzes the removal of unsubstituted N-terminal
CC amino acids from various peptides. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR860151; CAH92294.1; ALT_INIT; Transcribed_RNA.
DR AlphaFoldDB; Q5R7G6; -.
DR SMR; Q5R7G6; -.
DR STRING; 9601.ENSPPYP00000012484; -.
DR MEROPS; M17.006; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_3_1_1; -.
DR InParanoid; Q5R7G6; -.
DR OrthoDB; 562530at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..523
FT /note="Probable aminopeptidase NPEPL1"
FT /id="PRO_0000165830"
FT ACT_SITE 272
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /evidence="ECO:0000255"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 523 AA; 55847 MW; 1B00DFB02D169C0C CRC64;
MANVGLQFQA SAGDSDPQSR PLLLLGQLHH LHRVPWSHVR GKLQPRVTEE LWQAALSTLN
PNPTDSCPLY LNYATVAALP CRVSRHNSPS AAHFITRLVR TCLPPGAHRC IVMVCEQPEV
FASACALARA FPLFTHRSGA SRRLEKKTVT VEFFLVGQDN GPVEVSTLQC LANATDGVRL
AARIVDTPCN EMNTDTFLEE INKVGKELGI IPTIIRDEEL KTRGFGGIYG VGKAALHPPA
LAVLSHTPDG ATQTIAWVGK GIVYDTGGLS IKGKTTMPGM KRDCGGAAAV LGAFRAAIKQ
GFKDNLHAVF CLAENSVGPN ATRPDDIHLL YSGKTVEINN TDAEGRLVLA DGVSYACKDL
GADIILDMAT LTGAQGIATG KYHAAVLTNS AEWEAACVKA GRKCGDLVHP LVYCPELHFS
EFTSAVADMK NSVADRDNSP SSCAGLFIAS HIGFDWPGVW VHLDIAAPVH AGERATGFGV
ALLLALFGRA SEDPLLNLVS PLGCEVDVEE GDVGRDSKRR RLV