NALDL_MOUSE
ID NALDL_MOUSE Reviewed; 745 AA.
AC Q7M758;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Aminopeptidase NAALADL1 {ECO:0000305};
DE EC=3.4.11.- {ECO:0000250|UniProtKB:Q9UQQ1};
DE AltName: Full=N-acetylated-alpha-linked acidic dipeptidase-like protein;
DE Short=NAALADase L;
GN Name=Naaladl1; Synonyms=Gm964, Naaladasel;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J;
RA Pearman C., Haakenson W.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
CC -!- FUNCTION: Aminopeptidase with broad substrate specificity. Has lower
CC activity with substrates that have Asp or Glu in the P2' position, or
CC Pro in the P3' position. Lacks activity with substrates that have both
CC Pro in the P3' position and Asp or Glu in the P2' position. Lacks
CC carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity.
CC {ECO:0000250|UniProtKB:Q9UQQ1}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UQQ1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UQQ1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UQQ1}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O54697}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O54697}. Note=Ileal brush border membrane.
CC {ECO:0000250|UniProtKB:O54697}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O54697}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; AC131114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000129; CAD67582.1; -; mRNA.
DR CCDS; CCDS29494.1; -.
DR RefSeq; NP_001009546.1; NM_001009546.1.
DR AlphaFoldDB; Q7M758; -.
DR SMR; Q7M758; -.
DR IntAct; Q7M758; 1.
DR STRING; 10090.ENSMUSP00000044231; -.
DR MEROPS; M28.011; -.
DR GlyGen; Q7M758; 10 sites.
DR iPTMnet; Q7M758; -.
DR PhosphoSitePlus; Q7M758; -.
DR MaxQB; Q7M758; -.
DR PaxDb; Q7M758; -.
DR PeptideAtlas; Q7M758; -.
DR PRIDE; Q7M758; -.
DR ProteomicsDB; 287434; -.
DR Antibodypedia; 58724; 151 antibodies from 16 providers.
DR DNASU; 381204; -.
DR Ensembl; ENSMUST00000044451; ENSMUSP00000044231; ENSMUSG00000054999.
DR GeneID; 381204; -.
DR KEGG; mmu:381204; -.
DR UCSC; uc008ghk.1; mouse.
DR CTD; 10004; -.
DR MGI; MGI:2685810; Naaladl1.
DR VEuPathDB; HostDB:ENSMUSG00000054999; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR HOGENOM; CLU_005688_3_2_1; -.
DR InParanoid; Q7M758; -.
DR OMA; IEFVSWD; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q7M758; -.
DR TreeFam; TF312981; -.
DR BioGRID-ORCS; 381204; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q7M758; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q7M758; protein.
DR Bgee; ENSMUSG00000054999; Expressed in ileum and 47 other tissues.
DR Genevisible; Q7M758; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..745
FT /note="Aminopeptidase NAALADL1"
FT /id="PRO_0000174124"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 421
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 301..318
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ1"
SQ SEQUENCE 745 AA; 80513 MW; 5DC21DFEAD6D34CE CRC64;
MHWVKILGVA LGAAALLGLG IILGHFAIPK ATSPLTSSTS DSQDLDLAIL DSVMGQLDAS
RIRENLRELS KEPHVATSPR DEALVQLLLG RWKDTATGLD SAKTYEYRVL LSFPNAEQPN
SVEVVGPNGT TFHSFQPFEK NLTGEQAGPN VLQPYAAYAP PGTPKGLLVY ANQGSEEDFK
ELETQGINLE GTIALTRYGG VGRGAKAINA AKHGVVGVLV YTDPGDINDG KSLPNETFPN
SWRLPPSGVE RGSYYEYFGD PLTPYLPAHP SSFRLDPHNT SGFPPIPTQP IGFEDARDLL
CNLTGTSAPA FWQGALGCEY KLGPGFEPNG SFPAGSEVKV SVHNRLELRT SSNVLGIIQG
AVEPDRYVIY GNHRDSWVHG AVDPSSGTAV LLEISRVLGT LLKKGTWRPR RSIIFASWGA
EEFGLIGSTE FTEEFLSKLQ ERTVAYINVD ISVFSNATLR AQGTPPVQSV IFSATKEISA
PGSSGLSIYD NWIRYTNRTS PVYGLVPSLG TLGAGSDYAA FVHFLGITSM DLAYTYDRSK
TSARIYPTYH TAFDTFDYVE KFLDPGFSSH QAVARTAGSV LLRLSDSLFL PLNVSDYSET
LQSFLQAAQE ALGTQLEKQN ISLGPLVTAV ANFKAAAASL GEHILTLQKS SPDPLQVRMV
NDQLMLLERA FLNPRAFPEE RHYSHVLWAP NTASVDTFPG LANAYAKAQE INSGSEAWAE
VQRQLSIVVT ALEGAAATLV PVADL
