MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=N-acetylated-alpha-linked acidic dipeptidase-like protein; Short=NAALADase L; EC=3.4.17.21; AltName: Full=100 kDa ileum brush border membrane protein; Short=I100; AltName: Full=Ileal dipeptidylpeptidase; |
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| MyHits synonyms | NALDL_RAT , O54697 , A59C2EFD23BE36B5 |
 Legends: 1, ACT_SITE Nucleophile; for NAALADase activity. {ECO:0000250}; 2, ACT_SITE Charge relay system. {ECO:0000255}; 3, Zinc 1. {ECO:0000255}; 4, Zinc 1. {ECO:0000250}; 5, Zinc 2. {ECO:0000250}; 6, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 7, TOPO_DOM Cytoplasmic. {ECO:0000255}; 8, TRANSMEM Helical; Signal-anchor for type II membrane protein. {ECO:0000255}; 9, COMPBIAS Poly-Ala; 10, ipfam:TFR_dimer [T].
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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 10-MAY-2017, entry version 123.
DE RecName: Full=N-acetylated-alpha-linked acidic dipeptidase-like protein;
DE Short=NAALADase L;
DE EC=3.4.17.21;
DE AltName: Full=100 kDa ileum brush border membrane protein;
DE Short=I100;
DE AltName: Full=Ileal dipeptidylpeptidase;
GN Name=Naaladl1; Synonyms=Naaladl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 4-17.
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: Has no NAAG hydrolyzing activity (By similarity).
CC Exhibits a dipeptidyl-peptidase IV type activity. In vitro,
CC cleaves Gly-Pro-AMC. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Release of an unsubstituted, C-terminal
CC glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-
CC glutamates.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
CC membrane protein. Note=Ileal brush border membrane.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the distal small
CC intestine.
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 UniGene; Rn.10856; -.
DR ProteinModelPortal; O54697; -.
DR SMR; O54697; -.
DR STRING; 10116.ENSRNOP00000051719; -.
DR MEROPS; M28.011; -.
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 eggNOG; COG2234; LUCA.
DR GeneTree; ENSGT00550000074421; -.
DR HOGENOM; HOG000211921; -.
DR HOVERGEN; HBG051639; -.
DR InParanoid; O54697; -.
DR KO; K01301; -.
DR OMA; TSMDLAY; -.
DR OrthoDB; EOG091G02ZM; -.
DR PhylomeDB; O54697; -.
DR PRO; PR:O54697; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021000; -.
DR Genevisible; O54697; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR007365; TFR-like_dimer_dom.
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 Carboxypeptidase; Cell membrane; Complete proteome; Dipeptidase;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Multifunctional enzyme; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1 745 N-acetylated-alpha-linked acidic
FT dipeptidase-like protein.
FT /FTId=PRO_0000174125.
FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 7 28 Helical; Signal-anchor for type II
FT membrane protein. {ECO:0000255}.
FT TOPO_DOM 29 745 Extracellular. {ECO:0000255}.
FT REGION 268 584 NAALADase.
FT COMPBIAS 635 639 Poly-Ala.
FT ACT_SITE 421 421 Nucleophile; for NAALADase activity.
FT {ECO:0000250}.
FT ACT_SITE 622 622 Charge relay system. {ECO:0000255}.
FT ACT_SITE 662 662 Charge relay system. {ECO:0000255}.
FT ACT_SITE 685 685 Charge relay system. {ECO:0000255}.
FT METAL 373 373 Zinc 1. {ECO:0000255}.
FT METAL 383 383 Zinc 1. {ECO:0000250}.
FT METAL 383 383 Zinc 2. {ECO:0000250}.
FT METAL 422 422 Zinc 2. {ECO:0000250}.
FT METAL 450 450 Zinc 1. {ECO:0000250}.
FT METAL 550 550 Zinc 2. {ECO:0000250}.
FT CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 456 456 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 497 497 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 621 739 ipfam:TFR_dimer [T]
FT MYHIT 165 251 ipfam:PA [T]
FT MYHIT 353 560 ipfam:Peptidase_M28 [T]
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
//
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