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Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen homolog) (Pteroylpoly-gamma-glutamate carboxypeptidase)

 FOLH1_RAT               Reviewed;         752 AA.
P70627; Q547B6;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
10-MAY-2017, entry version 125.
RecName: Full=Glutamate carboxypeptidase 2;
EC=3.4.17.21;
AltName: Full=Folate hydrolase 1;
AltName: Full=Folylpoly-gamma-glutamate carboxypeptidase;
Short=FGCP;
AltName: Full=Glutamate carboxypeptidase II;
Short=GCPII;
AltName: Full=Membrane glutamate carboxypeptidase;
Short=mGCP;
AltName: Full=N-acetylated-alpha-linked acidic dipeptidase I;
Short=NAALADase I;
AltName: Full=Prostate-specific membrane antigen homolog;
AltName: Full=Pteroylpoly-gamma-glutamate carboxypeptidase;
Name=Folh1; Synonyms=Naalad1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=9375657;
Bzdega T., Turi T., Wroblewska B., She D., Chung H.S., Kim H.,
Neale J.H.;
"Molecular cloning of a peptidase against N-acetylaspartylglutamate
from a rat hippocampal cDNA library.";
J. Neurochem. 69:2270-2277(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9501243; DOI=10.1073/pnas.95.6.3215;
Luthi-Carter R., Berger U.V., Barczak A.K., Enna M., Coyle J.T.;
"Isolation and expression of a rat brain cDNA encoding glutamate
carboxypeptidase II.";
Proc. Natl. Acad. Sci. U.S.A. 95:3215-3220(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
PubMed=15019832; DOI=10.1016/j.abb.2004.01.011;
Park S.Y., Ha B.G., Choi G.H., Lee W.;
"N-Acetylated alpha-linked acidic dipeptidase expressed in rat
adipocytes is localized in the insulin-responsive glucose transporter
(GLUT4) intracellular compartments and involved in the insulin-
stimulated GLUT4 recruitment.";
Arch. Biochem. Biophys. 424:11-22(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 284-752.
TISSUE=Brain;
PubMed=8570628; DOI=10.1073/pnas.93.2.749;
Carter R.E., Feldman A.R., Coyle J.T.;
"Prostate-specific membrane antigen is a hydrolase with substrate and
pharmacologic characteristics of a neuropeptidase.";
Proc. Natl. Acad. Sci. U.S.A. 93:749-753(1996).
[5]
ALTERNATIVE SPLICING.
Bzdega T., She D., Turi T., Wroblewska B., Neale J.H.;
"Molecular cloning of alternatively spliced variants of the peptidase
against N-acetylaspartylglutamate (NAAG) from human and rat nervous
systems.";
Abstr. - Soc. Neurosci. 24:579-579(1998).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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. {ECO:0000250}.
-!- FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity.
In vitro, cleaves Gly-Pro-AMC. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of an unsubstituted, C-terminal
glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-
glutamates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase
activity.;
-!- ENZYME REGULATION: The NAALADase activity is inhibited by beta-
NAAG, quisqualic acid and 2-(phosphonomethyl)glutaric acid (PMG).
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q04609}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=P70627-1; Sequence=Displayed;
Name=2; Synonyms=Short form;
IsoId=P70627-2; Sequence=Not described;
Note=Probably inactive.;
Name=3; Synonyms=Long form;
IsoId=P70627-3; Sequence=Not described;
-!- TISSUE SPECIFICITY: Widely expressed throughout brain regions with
highest levels in the hippocampus, dentate gyrus, priform cortex,
choroid plexus of ventricles, pineal gland, anterior lobe of the
pituitary gland and supraoptic nucleus. High levels also found in
the cerebral cortex, substantia nigra, pontine nucleus and the
granule cell layer of cerebellum. Highly expressed in astrocytes
and non-myelinating Schwann cells. Also expressed in kidney,
localizing to the proximal brush border of the renal tube.
-!- DOMAIN: The NAALADase activity is found in the central region, the
dipeptidyl peptidase IV type activity in the C-terminal.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U75973; AAC53423.1; -; mRNA.
EMBL; AF040256; AAC40067.1; -; mRNA.
EMBL; AF513486; AAM47015.1; -; mRNA.
EMBL; AF039707; AAB96759.1; -; mRNA.
RefSeq; NP_476533.1; NM_057185.2. [P70627-1]
UniGene; Rn.89278; -.
ProteinModelPortal; P70627; -.
SMR; P70627; -.
STRING; 10116.ENSRNOP00000018592; -.
BindingDB; P70627; -.
ChEMBL; CHEMBL5098; -.
MEROPS; M28.010; -.
iPTMnet; P70627; -.
PhosphoSitePlus; P70627; -.
UniCarbKB; P70627; -.
PaxDb; P70627; -.
PRIDE; P70627; -.
GeneID; 85309; -.
KEGG; rno:85309; -.
UCSC; RGD:70963; rat. [P70627-1]
CTD; 2346; -.
RGD; 70963; Folh1.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
HOGENOM; HOG000211921; -.
HOVERGEN; HBG051639; -.
InParanoid; P70627; -.
KO; K14592; -.
PhylomeDB; P70627; -.
BRENDA; 3.4.17.21; 5301.
PRO; PR:P70627; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0006508; P:proteolysis; IDA:RGD.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR007365; TFR-like_dimer_dom.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Carboxypeptidase; Cell membrane;
Complete proteome; Dipeptidase; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Multifunctional enzyme;
Phosphoprotein; Protease; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 752 Glutamate carboxypeptidase 2.
/FTId=PRO_0000174120.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 44 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 45 752 Extracellular. {ECO:0000255}.
REGION 276 589 NAALADase.
REGION 519 520 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
REGION 536 538 Substrate binding.
{ECO:0000250|UniProtKB:Q04609}.
REGION 554 555 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
REGION 701 702 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
ACT_SITE 426 426 Nucleophile; for NAALADase activity.
{ECO:0000250}.
ACT_SITE 630 630 Charge relay system. {ECO:0000255}.
ACT_SITE 668 668 Charge relay system. {ECO:0000255}.
ACT_SITE 691 691 Charge relay system. {ECO:0000255}.
METAL 271 271 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 274 274 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q04609}.
METAL 379 379 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 389 389 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 389 389 Zinc 2. {ECO:0000250|UniProtKB:Q04609}.
METAL 427 427 Zinc 2. {ECO:0000250|UniProtKB:Q04609}.
METAL 435 435 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 438 438 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 455 455 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 555 555 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q04609}.
BINDING 212 212 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 259 259 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 426 426 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 521 521 Substrate.
{ECO:0000250|UniProtKB:Q04609}.
BINDING 554 554 Substrate.
{ECO:0000250|UniProtKB:Q04609}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 640 640 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
SEQUENCE 752 AA; 84540 MW; 5C0915A3B9C71E41 CRC64;
MWNAQQDSDS AEALGRRQRW FCAGTLVLAF TGTFIIGFLF GWFIKPSNDS TSSVSYPGMK
KAFLQELKAE NIKKFLYNFT RTPHLAGTQH NFELAKQIHA QWKEFGLDLV ELSDYDVLLS
YPNKTHPNYI SIINEDGNEI FKTSLAELSP PGYENISDVV PPYSAFSPQG TPEGDLVYVN
YARTEDFFKL ERVMKINCSG KIVIARYGQV FRGNKVKNAQ LAGAKGIILY SDPADYFVPG
VKSYPDGWNL PGGGVQRGNV LNLNGAGDPL TPGYPANEYA YRHEFTEAVG LPSIPVHPIG
YDDAQKLLEH MGGSAPPDSS WKGGLKVPYN VGPGFAGNFS KQKVKLHIHS YNKVTRIYNV
IGTLKGAVEP DRYVILGGHR DAWVFGGIDP QSGAAVVHEI VRTFGTLKKK GWRPRRTILF
ASWDAEEFGL LGSTEWAEEH SRLLQERGVA YINADSSIEG NYTLRVDCTP LMHSLVYNLT
KELPSPDEGF EGKSLYDSWK EKSPSTEFIG MPRISKLGSG NDFEVFFQRL GIASGRARYT
KNWKNNKVSS YPLYHSVYET YELVEKFYDP TFKYHLTVAQ VRGAMVFELA NSIVLPFDCQ
SYAVALKKHA ETIYNISMNH PQEMKAYMIS FDSLFSAVNN FTDVASKFNQ RLQDLDKSNP
ILLRILNDQL MYLERAFIDP LGLPGRPFYR HIIYAPSSHN KYAGESFPGI YDALFDINNK
VDTSKAWREV KRQISIAAFT VQAAAETLRE VD


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