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O35409

- FOLH1_MOUSE

UniProt

O35409 - FOLH1_MOUSE

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Protein
Glutamate carboxypeptidase 2
Gene
Folh1, Mopsm, Naalad1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides By similarity. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate.
Also exhibits a dipeptidyl-peptidase IV type activity By similarity. In vitro, cleaves Gly-Pro-AMC By similarity.

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit. Required for NAALADase activity.

Enzyme regulationi

The NAALADase and folate hydrolase activities are inhibited by quisqualic acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei212 – 2121Substrate By similarity
Binding sitei259 – 2591Substrate By similarity
Metal bindingi271 – 2711Calcium By similarity
Metal bindingi274 – 2741Calcium; via carbonyl oxygen By similarity
Metal bindingi379 – 3791Zinc 1 By similarity
Metal bindingi389 – 3891Zinc 1 By similarity
Metal bindingi389 – 3891Zinc 2 By similarity
Active sitei426 – 4261Nucleophile; for NAALADase activity By similarity
Metal bindingi427 – 4271Zinc 2 By similarity
Metal bindingi435 – 4351Calcium By similarity
Metal bindingi438 – 4381Calcium By similarity
Metal bindingi455 – 4551Zinc 1 By similarity
Binding sitei521 – 5211Substrate By similarity
Binding sitei554 – 5541Substrate By similarity
Metal bindingi555 – 5551Zinc 2 By similarity
Active sitei630 – 6301Charge relay system Reviewed prediction
Active sitei668 – 6681Charge relay system Reviewed prediction
Active sitei691 – 6911Charge relay system Reviewed prediction

GO - Molecular functioni

  1. carboxypeptidase activity Source: MGI
  2. dipeptidase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. metallopeptidase activity Source: UniProtKB-KW
  5. peptidase activity Source: MGI

GO - Biological processi

  1. folic acid-containing compound metabolic process Source: MGI
  2. proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM28.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate carboxypeptidase 2 (EC:3.4.17.21)
Alternative name(s):
Folate hydrolase 1
Folylpoly-gamma-glutamate carboxypeptidase
Short name:
FGCP
Glutamate carboxypeptidase II
Short name:
GCPII
Membrane glutamate carboxypeptidase
Short name:
mGCP
N-acetylated-alpha-linked acidic dipeptidase I
Short name:
NAALADase I
Prostate-specific membrane antigen homolog
Pteroylpoly-gamma-glutamate carboxypeptidase
Gene namesi
Name:Folh1
Synonyms:Mopsm, Naalad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1858193. Folh1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei23 – 4422Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini45 – 752708Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. integral component of membrane Source: MGI
  3. integral component of plasma membrane Source: MGI
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Glutamate carboxypeptidase 2
PRO_0000174118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi123 – 1231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi155 – 1551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi338 – 3381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi461 – 4611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi478 – 4781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi615 – 6151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi640 – 6401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi722 – 7221N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO35409.
PaxDbiO35409.
PRIDEiO35409.

PTM databases

PhosphoSiteiO35409.

Expressioni

Tissue specificityi

Expressed predominantly in the hippocampal region of the brain and in kidney. Lower levels in the ovary, testis and mandibular gland.

Gene expression databases

ArrayExpressiO35409.
BgeeiO35409.
CleanExiMM_FOLH1.
GenevestigatoriO35409.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiO35409. 1 interaction.
MINTiMINT-4996170.

Structurei

3D structure databases

ProteinModelPortaliO35409.
SMRiO35409. Positions 61-752.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 589314NAALADase
Add
BLAST
Regioni536 – 5383Substrate binding By similarity
Regioni701 – 7022Substrate binding By similarity

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG74799.
GeneTreeiENSGT00550000074421.
HOGENOMiHOG000211921.
HOVERGENiHBG051639.
InParanoidiQ0VDM5.
KOiK14592.
OMAiYAYRLDK.
TreeFamiTF312981.

Family and domain databases

Gene3Di1.20.930.40. 1 hit.
InterProiIPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
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.

O35409-1 [UniParc]FASTAAdd to Basket

« Hide

MWNALQDRDS AEVLGHRQRW LRVGTLVLAL TGTFLIGFLF GWFIKPSNEA    50
TGNVSHSGMK KEFLHELKAE NIKKFLYNFT RTPHLAGTQN NFELAKQIHD 100
QWKEFGLDLV ELSHYDVLLS YPNKTHPNYI SIINEDGNEI FKTSLSEQPP 150
PGYENISDVV PPYSAFSPQG TPEGDLVYVN YARTEDFFKL EREMKISCSG 200
KIVIARYGKV FRGNMVKNAQ LAGAKGMILY SDPADYFVPA VKSYPDGWNL 250
PGGGVQRGNV LNLNGAGDPL TPGYPANEHA YRHELTNAVG LPSIPVHPIG 300
YDDAQKLLEH MGGPAPPDSS WKGGLKVPYN VGPGFAGNFS TQKVKMHIHS 350
YTKVTRIYNV IGTLKGALEP DRYVILGGHR DAWVFGGIDP QSGAAVVHEI 400
VRSFGTLKKK GRRPRRTILF ASWDAEEFGL LGSTEWAEEH SRLLQERGVA 450
YINADSSIEG NYTLRVDCTP LMYSLVYNLT KELQSPDEGF EGKSLYDSWK 500
EKSPSPEFIG MPRISKLGSG NDFEVFFQRL GIASGRARYT KNWKTNKVSS 550
YPLYHSVYET YELVVKFYDP TFKYHLTVAQ VRGAMVFELA NSIVLPFDCQ 600
SYAVALKKYA DTIYNISMKH PQEMKAYMIS FDSLFSAVNN FTDVASKFNQ 650
RLQELDKSNP ILLRIMNDQL MYLERAFIDP LGLPGRPFYR HIIYAPSSHN 700
KYAGESFPGI YDALFDISSK VNASKAWNEV KRQISIATFT VQAAAETLRE 750
VA 752
Length:752
Mass (Da):84,574
Last modified:July 27, 2011 - v2
Checksum:iF96041949214E8F3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411F → S in BAB22457. 1 Publication
Sequence conflicti178 – 1781Y → F in AAB81971. 1 Publication
Sequence conflicti219 – 2191A → V in AAB81971. 1 Publication
Sequence conflicti240 – 2401A → G in AAB81971. 1 Publication
Sequence conflicti287 – 2871N → E in AAB81971. 1 Publication
Sequence conflicti583 – 5831G → R in AAB81971. 1 Publication
Sequence conflicti625 – 6251K → E in AAB81971. 1 Publication
Sequence conflicti728 – 7281N → S in AAB81971. 1 Publication
Sequence conflicti749 – 7491R → M in AAB81971. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026380 mRNA. Translation: AAB81971.1.
AK002920 mRNA. Translation: BAB22457.1.
BC119605 mRNA. Translation: AAI19606.1.
CCDSiCCDS21436.1.
RefSeqiNP_001153178.1. NM_001159706.1.
NP_058050.3. NM_016770.3.
UniGeneiMm.269137.

Genome annotation databases

EnsembliENSMUST00000001824; ENSMUSP00000001824; ENSMUSG00000001773.
GeneIDi53320.
KEGGimmu:53320.
UCSCiuc009ifh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026380 mRNA. Translation: AAB81971.1 .
AK002920 mRNA. Translation: BAB22457.1 .
BC119605 mRNA. Translation: AAI19606.1 .
CCDSi CCDS21436.1.
RefSeqi NP_001153178.1. NM_001159706.1.
NP_058050.3. NM_016770.3.
UniGenei Mm.269137.

3D structure databases

ProteinModelPortali O35409.
SMRi O35409. Positions 61-752.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35409. 1 interaction.
MINTi MINT-4996170.

Protein family/group databases

MEROPSi M28.010.

PTM databases

PhosphoSitei O35409.

Proteomic databases

MaxQBi O35409.
PaxDbi O35409.
PRIDEi O35409.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001824 ; ENSMUSP00000001824 ; ENSMUSG00000001773 .
GeneIDi 53320.
KEGGi mmu:53320.
UCSCi uc009ifh.2. mouse.

Organism-specific databases

CTDi 2346.
MGIi MGI:1858193. Folh1.

Phylogenomic databases

eggNOGi NOG74799.
GeneTreei ENSGT00550000074421.
HOGENOMi HOG000211921.
HOVERGENi HBG051639.
InParanoidi Q0VDM5.
KOi K14592.
OMAi YAYRLDK.
TreeFami TF312981.

Miscellaneous databases

NextBioi 310121.
PROi O35409.
SOURCEi Search...

Gene expression databases

ArrayExpressi O35409.
Bgeei O35409.
CleanExi MM_FOLH1.
Genevestigatori O35409.

Family and domain databases

Gene3Di 1.20.930.40. 1 hit.
InterProi IPR007484. Peptidase_M28.
IPR003137. Protease-assoc_domain.
IPR007365. TFR-like_dimer_dom.
[Graphical view ]
Pfami PF02225. PA. 1 hit.
PF04389. Peptidase_M28. 1 hit.
PF04253. TFR_dimer. 1 hit.
[Graphical view ]
SUPFAMi SSF47672. SSF47672. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, genomic localization, and enzymatic activities of the mouse homolog of prostate-specific membrane antigen/NAALADase/ folate hydrolase."
    Bacich D.J., Pinto J.T., Tong W.P., Heston W.D.W.
    Mamm. Genome 12:117-123(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
    Tissue: Brain.
  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].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiFOLH1_MOUSE
AccessioniPrimary (citable) accession number: O35409
Secondary accession number(s): Q0VDM5, Q9DCC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

There are amino acid differences between the sequence shown in fig.1 (1 Publication) and the sequence deposited in the database (AF026380). The sequence from fig.1 shows only 3 conflicts between 1 Publication and 1 Publication. These are at AA positions 141, 240 and 287.

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

External Data

Dasty 3

Similar proteinsi