NALDL_RAT
ID NALDL_RAT Reviewed; 745 AA.
AC O54697;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Aminopeptidase NAALADL1 {ECO:0000305};
DE EC=3.4.11.- {ECO:0000250|UniProtKB:Q9UQQ1};
DE AltName: Full=100 kDa ileum brush border membrane protein {ECO:0000303|PubMed:9388249};
DE Short=I100 {ECO:0000303|PubMed:9388249};
DE AltName: Full=Ileal dipeptidylpeptidase;
DE AltName: Full=N-acetylated-alpha-linked acidic dipeptidase-like protein;
DE Short=NAALADase L;
GN Name=Naaladl1; Synonyms=Naaladl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-17, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Ileum;
RX PubMed=9388249; DOI=10.1074/jbc.272.49.31006;
RA Shneider B.L., Thevananther S., Moyer M.S., Walters H.C., Rinaldo P.,
RA Devarajan P., Sun A.Q., Dawson P.A., Ananthanarayanan M.;
RT "Cloning and characterization of a novel peptidase from rat and human
RT ileum.";
RL J. Biol. Chem. 272:31006-31015(1997).
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:0000269|PubMed:9388249}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9388249}. Note=Ileal brush border membrane.
CC {ECO:0000269|PubMed:9388249}.
CC -!- TISSUE SPECIFICITY: Detected on apical villi on the brush border
CC membrane of ileum enterocytes (at protein level) (PubMed:9388249).
CC Mainly expressed in the distal small intestine (PubMed:9388249).
CC {ECO:0000269|PubMed:9388249}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9388249}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; AF009921; AAB87644.1; -; mRNA.
DR RefSeq; NP_113947.1; NM_031759.1.
DR AlphaFoldDB; O54697; -.
DR SMR; O54697; -.
DR STRING; 10116.ENSRNOP00000051719; -.
DR MEROPS; M28.011; -.
DR GlyGen; O54697; 10 sites.
DR iPTMnet; O54697; -.
DR PhosphoSitePlus; O54697; -.
DR PaxDb; O54697; -.
DR PRIDE; O54697; -.
DR Ensembl; ENSRNOT00000054835; ENSRNOP00000051719; ENSRNOG00000021000.
DR GeneID; 83568; -.
DR KEGG; rno:83568; -.
DR UCSC; RGD:620987; rat.
DR CTD; 10004; -.
DR RGD; 620987; Naaladl1.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR HOGENOM; CLU_005688_3_2_1; -.
DR InParanoid; O54697; -.
DR OMA; IEFVSWD; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; O54697; -.
DR PRO; PR:O54697; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021000; Expressed in jejunum and 13 other tissues.
DR Genevisible; O54697; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA: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 1: Evidence at protein level;
KW Aminopeptidase; Calcium; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..745
FT /note="Aminopeptidase NAALADL1"
FT /id="PRO_0000174125"
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 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
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; 80641 MW; A59C2EFD23BE36B5 CRC64;
MHWAKILGVG IGAAALLGLG IILGHFAIPK ATEPLASSVS DSQDLDLAIL DSVMGQLDAS
RIRENLRELS KEPHVATSAR DEALVQLLLG RWKDSASGLD TAKTYEYTVL LSFPSTEQPN
SVEVVGPNGT VFHSFQPFEK NLTGEQAEPN VLQPYAAYAP PGTPKGPLVY ANRGSEDDFK
KLEAEGINLK GTIALTRYGS VGRGAKAINA ARHGVVGVLV YTDPGDINDG KSLPNETFPN
SWGLPPSGVE RGSYYEYFGD PLTPYLPAHP VSFRLDPHNI SGFPPIPTQP IGFEDAKNLL
CNLNGTSAPD SWQGALGCEY KLGPGFEPNG NFPAGSEVKV SVYNRLELRN SSNVLGIIQG
AVEPDRYVIY GNHRDSWVHG AVDPSSGTAV LLEISRVLGT LLKKGTWRPR RSIIFASWGA
EEFGLIGSTE FTEEFLSKLQ ERTVTYINVD ISVFSNATLR AQGTPPVQSV IFSATKEISA
PGSSGLSIYD NWIRYTNRSS PVYGLVPSMG TLGAGSDYAS FIHFLGITSM DLAYTYDRSK
TSARIYPTYH TAFDTFDYVE KFLDPGFSSH QAVARTAGSV LLRLSDSLFL PLNVSDYSET
LQSFLQAAQE NLGALLESHN ISLGPLVTAV EKFKAAAAAL NQHILTLQKS SPDPLQVRMV
NDQLMLLERA FLNPRAFPEE RYYSHVLWAP NTASVATFPG LANAYARAQE INSGAEAWAE
VERQLSIAVM ALEGAAATLQ PVTDL
