Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O35409

- FOLH1_MOUSE

UniProt

O35409 - FOLH1_MOUSE

Protein

Glutamate carboxypeptidase 2

Gene

Folh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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. cytoplasm Source: Ensembl
    2. integral component of membrane Source: MGI
    3. integral component of plasma membrane Source: MGI
    4. nucleus Source: Ensembl

    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

    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.
    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.
    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

    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 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

    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 1, 2014
    This is version 121 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