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Protein

N-acetylated-alpha-linked acidic dipeptidase 2

Gene

Naalad2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N-acetylaspartylglutamate.1 Publication

Catalytic activityi

Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. Required for NAALADase activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei200 – 2001SubstrateBy similarity
Binding sitei247 – 2471SubstrateBy similarity
Metal bindingi259 – 2591CalciumBy similarity
Metal bindingi262 – 2621Calcium; via carbonyl oxygenBy similarity
Metal bindingi367 – 3671Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi377 – 3771Zinc 1; catalyticBy similarity
Metal bindingi377 – 3771Zinc 2By similarity
Active sitei414 – 4141Nucleophile; for NAALADase activityBy similarity
Binding sitei414 – 4141SubstrateBy similarity
Metal bindingi415 – 4151Zinc 2By similarity
Metal bindingi423 – 4231CalciumBy similarity
Metal bindingi426 – 4261CalciumBy similarity
Metal bindingi443 – 4431Zinc 1; catalyticBy similarity
Binding sitei542 – 5421SubstrateBy similarity
Metal bindingi543 – 5431Zinc 2; via tele nitrogenBy similarity
Active sitei618 – 6181Charge relay systemSequence analysis
Active sitei656 – 6561Charge relay systemSequence analysis
Active sitei679 – 6791Charge relay systemSequence analysis

GO - Molecular functioni

  • carboxypeptidase activity Source: MGI
  • dipeptidase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: UniProtKB-KW
  • N-formylglutamate deformylase activity Source: MGI
  • peptidase activity Source: MGI

GO - Biological processi

  • neurotransmitter catabolic process Source: MGI
  • proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.21. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).

Protein family/group databases

MEROPSiM28.012.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylated-alpha-linked acidic dipeptidase 2 (EC:3.4.17.21)
Alternative name(s):
Glutamate carboxypeptidase III
Short name:
GCPIII
N-acetylaspartylglutamate peptidase II
Short name:
NAAG-peptidase II
N-acetylated-alpha-linked acidic dipeptidase II
Short name:
NAALADase II
Gene namesi
Name:Naalad2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1919810. Naalad2.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type II membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 3124Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini32 – 740709ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740N-acetylated-alpha-linked acidic dipeptidase 2PRO_0000174122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)By similarity
Glycosylationi143 – 1431N-linked (GlcNAc...)By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...)By similarity
Glycosylationi314 – 3141N-linked (GlcNAc...)1 Publication
Glycosylationi318 – 3181N-linked (GlcNAc...); atypical1 Publication
Glycosylationi449 – 4491N-linked (GlcNAc...)1 Publication
Glycosylationi603 – 6031N-linked (GlcNAc...)1 Publication
Glycosylationi628 – 6281N-linked (GlcNAc...)By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9CZR2.
PaxDbiQ9CZR2.
PRIDEiQ9CZR2.

PTM databases

PhosphoSiteiQ9CZR2.
SwissPalmiQ9CZR2.

Expressioni

Tissue specificityi

Expressed ovary, testes and lung, but not brain.1 Publication

Gene expression databases

BgeeiQ9CZR2.
CleanExiMM_NAALAD2.
ExpressionAtlasiQ9CZR2. baseline and differential.
GenevisibleiQ9CZR2. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9CZR2. 1 interaction.
MINTiMINT-4103897.
STRINGi10090.ENSMUSP00000128674.

Structurei

3D structure databases

ProteinModelPortaliQ9CZR2.
SMRiQ9CZR2. Positions 46-739.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 577314NAALADaseAdd
BLAST
Regioni507 – 5082Substrate bindingBy similarity
Regioni524 – 5263Substrate bindingBy similarity
Regioni542 – 5432Substrate bindingBy similarity
Regioni689 – 6902Substrate bindingBy similarity

Domaini

The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal.

Sequence similaritiesi

Belongs to the peptidase M28 family. M28B subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00550000074421.
HOVERGENiHBG051639.
InParanoidiQ9CZR2.
KOiK01301.
OrthoDBiEOG7QK0BC.
PhylomeDBiQ9CZR2.
TreeFamiTF312981.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR003137. PA_domain.
IPR007484. Peptidase_M28.
IPR007365. TFR-like_dimer_dom.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF47672. SSF47672. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CZR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARPRHLRGL GMCITAVLAS FIAGFTVGWF IKPLKETTTS AGYHQSIQQK
60 70 80 90 100
LLSEMKAENI RSFLRSFTKL PHLAGTEQNL LLAKKIQTQW KKFGLDSANL
110 120 130 140 150
VHYDVLLSYP NETNANYVSI VDEHGVEIFK TSYLEPPPDG YENVTNIIPP
160 170 180 190 200
YNAFSASGMP EGELVYVNYA RTEDFFKLER EMNINCTGKI VIARYGKIFR
210 220 230 240 250
GNKVKNAMLA GAMGIILYSD PADYFAPDVQ PYPKGWNLPG AAAQRGNVLN
260 270 280 290 300
LNGAGDPLTP GYPAKEYTFR LPVEEAVGIP NIPVHPIGYN DAERLLRNLG
310 320 330 340 350
GAAPPDKSWK GSLNVSYNIG PGFTGSEYSR NIRMHVNNIN KITRIYNVIG
360 370 380 390 400
TIRGSTEPDR YVILGGHRDS WVFGGIDPTT GTAVLQEIAR SFGKLVNGGW
410 420 430 440 450
RPRRTIIFAS WDAEEFGLLG STEWAEENAK LLQERSIAYI NSDSAIEGNY
460 470 480 490 500
TLRVDCTPLL NQLVYKVARE ISSPDDGFES KSLYESWLEK DPSPENKECP
510 520 530 540 550
RINKLGSGSD FEAYFQRLGI ASGRARYTKN KKTDKYSSYP VYHTIYETFE
560 570 580 590 600
LVQNFYDPTF KKQLSVAQLR GALVYELADS VVIPFNIQDY AKALKNYAAS
610 620 630 640 650
IFNISKKHDQ QLRNHAVSFD PLFSAVKNFS EAASDFHRRL TQVDLNNPIA
660 670 680 690 700
VRIMNDQQML LERAFIDPLG LPGRKFYRHI IFAPSSHNKY AGESFPGIYD
710 720 730 740
AMFDIENKAD PSLAWAEVKK HISIAAFTIQ AAAGTLTNVL
Length:740
Mass (Da):82,801
Last modified:May 24, 2005 - v2
Checksum:iB5EDAD7F7900E6C5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti484 – 4874YESW → MKAG in BAB28132 (PubMed:16141072).Curated
Sequence conflicti499 – 4991C → L in BAB28132 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY243507 mRNA. Translation: AAO89235.1.
AK012270 mRNA. Translation: BAB28132.1.
CCDSiCCDS52728.1.
RefSeqiNP_082555.2. NM_028279.3.
UniGeneiMm.474510.

Genome annotation databases

EnsembliENSMUST00000166825; ENSMUSP00000128674; ENSMUSG00000043943.
GeneIDi72560.
KEGGimmu:72560.
UCSCiuc009ogn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY243507 mRNA. Translation: AAO89235.1.
AK012270 mRNA. Translation: BAB28132.1.
CCDSiCCDS52728.1.
RefSeqiNP_082555.2. NM_028279.3.
UniGeneiMm.474510.

3D structure databases

ProteinModelPortaliQ9CZR2.
SMRiQ9CZR2. Positions 46-739.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CZR2. 1 interaction.
MINTiMINT-4103897.
STRINGi10090.ENSMUSP00000128674.

Protein family/group databases

MEROPSiM28.012.

PTM databases

PhosphoSiteiQ9CZR2.
SwissPalmiQ9CZR2.

Proteomic databases

MaxQBiQ9CZR2.
PaxDbiQ9CZR2.
PRIDEiQ9CZR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000166825; ENSMUSP00000128674; ENSMUSG00000043943.
GeneIDi72560.
KEGGimmu:72560.
UCSCiuc009ogn.1. mouse.

Organism-specific databases

CTDi10003.
MGIiMGI:1919810. Naalad2.

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00550000074421.
HOVERGENiHBG051639.
InParanoidiQ9CZR2.
KOiK01301.
OrthoDBiEOG7QK0BC.
PhylomeDBiQ9CZR2.
TreeFamiTF312981.

Enzyme and pathway databases

BRENDAi3.4.17.21. 3474.
ReactomeiR-MMU-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

PROiQ9CZR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZR2.
CleanExiMM_NAALAD2.
ExpressionAtlasiQ9CZR2. baseline and differential.
GenevisibleiQ9CZR2. MM.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR003137. PA_domain.
IPR007484. Peptidase_M28.
IPR007365. TFR-like_dimer_dom.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view]
SUPFAMiSSF47672. SSF47672. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cloning and characterization of a second brain enzyme with NAAG peptidase activity."
    Bzdega T., Crowe S.L., Ramadan E.R., Sciarretta K.H., Olszewski R.T., Ojeifo O.A., Rafalski V.A., Wroblewska B., Neale J.H.
    J. Neurochem. 89:627-635(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 484-740.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314; ASN-318; ASN-449 AND ASN-603.
    Tissue: Myoblast.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Lung and Testis.

Entry informationi

Entry nameiNALD2_MOUSE
AccessioniPrimary (citable) accession number: Q9CZR2
Secondary accession number(s): Q80YF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 24, 2005
Last modified: June 8, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.