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O35409

- FOLH1_MOUSE

UniProt

O35409 - FOLH1_MOUSE

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Protein

Glutamate carboxypeptidase 2

Gene

Folh1

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.By similarity
Also exhibits a dipeptidyl-peptidase IV type activity. 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 – 2121SubstrateBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Metal bindingi271 – 2711CalciumBy similarity
Metal bindingi274 – 2741Calcium; via carbonyl oxygenBy similarity
Metal bindingi379 – 3791Zinc 1By similarity
Metal bindingi389 – 3891Zinc 1By similarity
Metal bindingi389 – 3891Zinc 2By similarity
Active sitei426 – 4261Nucleophile; for NAALADase activityBy similarity
Metal bindingi427 – 4271Zinc 2By similarity
Metal bindingi435 – 4351CalciumBy similarity
Metal bindingi438 – 4381CalciumBy similarity
Metal bindingi455 – 4551Zinc 1By similarity
Binding sitei521 – 5211SubstrateBy similarity
Binding sitei554 – 5541SubstrateBy similarity
Metal bindingi555 – 5551Zinc 2By similarity
Active sitei630 – 6301Charge relay systemSequence Analysis
Active sitei668 – 6681Charge relay systemSequence Analysis
Active sitei691 – 6911Charge relay systemSequence Analysis

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

GO - Cellular componenti

  1. integral component of membrane Source: MGI
  2. integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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

BgeeiO35409.
CleanExiMM_FOLH1.
ExpressionAtlasiO35409. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini45 – 752708ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4422Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 589314NAALADaseAdd
BLAST
Regioni536 – 5383Substrate bindingBy similarity
Regioni701 – 7022Substrate 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

eggNOGiNOG74799.
GeneTreeiENSGT00550000074421.
HOGENOMiHOG000211921.
HOVERGENiHBG051639.
InParanoidiO35409.
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

        10         20         30         40         50
MWNALQDRDS AEVLGHRQRW LRVGTLVLAL TGTFLIGFLF GWFIKPSNEA
60 70 80 90 100
TGNVSHSGMK KEFLHELKAE NIKKFLYNFT RTPHLAGTQN NFELAKQIHD
110 120 130 140 150
QWKEFGLDLV ELSHYDVLLS YPNKTHPNYI SIINEDGNEI FKTSLSEQPP
160 170 180 190 200
PGYENISDVV PPYSAFSPQG TPEGDLVYVN YARTEDFFKL EREMKISCSG
210 220 230 240 250
KIVIARYGKV FRGNMVKNAQ LAGAKGMILY SDPADYFVPA VKSYPDGWNL
260 270 280 290 300
PGGGVQRGNV LNLNGAGDPL TPGYPANEHA YRHELTNAVG LPSIPVHPIG
310 320 330 340 350
YDDAQKLLEH MGGPAPPDSS WKGGLKVPYN VGPGFAGNFS TQKVKMHIHS
360 370 380 390 400
YTKVTRIYNV IGTLKGALEP DRYVILGGHR DAWVFGGIDP QSGAAVVHEI
410 420 430 440 450
VRSFGTLKKK GRRPRRTILF ASWDAEEFGL LGSTEWAEEH SRLLQERGVA
460 470 480 490 500
YINADSSIEG NYTLRVDCTP LMYSLVYNLT KELQSPDEGF EGKSLYDSWK
510 520 530 540 550
EKSPSPEFIG MPRISKLGSG NDFEVFFQRL GIASGRARYT KNWKTNKVSS
560 570 580 590 600
YPLYHSVYET YELVVKFYDP TFKYHLTVAQ VRGAMVFELA NSIVLPFDCQ
610 620 630 640 650
SYAVALKKYA DTIYNISMKH PQEMKAYMIS FDSLFSAVNN FTDVASKFNQ
660 670 680 690 700
RLQELDKSNP ILLRIMNDQL MYLERAFIDP LGLPGRPFYR HIIYAPSSHN
710 720 730 740 750
KYAGESFPGI YDALFDISSK VNASKAWNEV KRQISIATFT VQAAAETLRE

VA
Length:752
Mass (Da):84,574
Last modified:July 27, 2011 - v2
Checksum:iF96041949214E8F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411F → S in BAB22457. (PubMed:16141072)Curated
Sequence conflicti178 – 1781Y → F in AAB81971. (PubMed:11210180)Curated
Sequence conflicti219 – 2191A → V in AAB81971. (PubMed:11210180)Curated
Sequence conflicti240 – 2401A → G in AAB81971. (PubMed:11210180)Curated
Sequence conflicti287 – 2871N → E in AAB81971. (PubMed:11210180)Curated
Sequence conflicti583 – 5831G → R in AAB81971. (PubMed:11210180)Curated
Sequence conflicti625 – 6251K → E in AAB81971. (PubMed:11210180)Curated
Sequence conflicti728 – 7281N → S in AAB81971. (PubMed:11210180)Curated
Sequence conflicti749 – 7491R → M in AAB81971. (PubMed:11210180)Curated

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 O35409.
KOi K14592.
OMAi YAYRLDK.
TreeFami TF312981.

Miscellaneous databases

NextBioi 310121.
PROi O35409.
SOURCEi Search...

Gene expression databases

Bgeei O35409.
CleanExi MM_FOLH1.
ExpressionAtlasi O35409. baseline and differential.
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: October 29, 2014
This is version 122 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 (PubMed:11210180) and the sequence deposited in the database (AF026380). The sequence from fig.1 shows only 3 conflicts between PubMed:11210180 and PubMed:16141072. These are at AA positions 141, 240 and 287.1 Publication

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