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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_PIG               Reviewed;         751 AA.
O77564;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
16-JAN-2019, entry version 111.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 200-210 AND
471-483.
TISSUE=Jejunal mucosa;
PubMed=9685395; DOI=10.1074/jbc.273.32.20417;
Halsted C.H., Ling E.-H., Luthi-Carter R., Villanueva J.A.,
Gardner J.M., Coyle J.T.;
"Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum.
Molecular characterization and relation to glutamate carboxypeptidase
II.";
J. Biol. Chem. 273:20417-20424(1998).
[2]
ERRATUM.
Halsted C.H., Ling E.-H., Luthi-Carter R., Villanueva J.A.,
Gardner J.M., Coyle J.T.;
J. Biol. Chem. 275:30746-30746(2000).
[3]
CHARACTERIZATION.
PubMed=2867095;
Chandler C.J., Wang T.T., Halsted C.H.;
"Pteroylpolyglutamate hydrolase from human jejunal brush borders.
Purification and characterization.";
J. Biol. Chem. 261:928-933(1986).
-!- 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:
Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
EC=3.4.17.21;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase
activity.;
-!- ACTIVITY REGULATION: The NAALADase activity is inhibited by
quisqualic acid, beta-NAAG and 2-(phosphonomethyl) pentanedioic
acid (PMPA). Ethanol ingestion decreases the folate hydrolase
activity by 50%.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0.;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:Q04609}.
-!- TISSUE SPECIFICITY: High expression in the duodenum and in the
jejunum brush-border membrane. Weak expression in kidney.
-!- 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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EMBL; AF050502; AAC39269.1; -; mRNA.
RefSeq; NP_999549.1; NM_214384.1.
UniGene; Ssc.14488; -.
ProteinModelPortal; O77564; -.
SMR; O77564; -.
STRING; 9823.ENSSSCP00000027466; -.
MEROPS; M28.010; -.
PaxDb; O77564; -.
PeptideAtlas; O77564; -.
PRIDE; O77564; -.
GeneID; 397677; -.
KEGG; ssc:397677; -.
CTD; 219595; -.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
HOVERGEN; HBG051639; -.
InParanoid; O77564; -.
KO; K14592; -.
OrthoDB; 804230at2759; -.
Proteomes; UP000008227; 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.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR039373; Peptidase_M28B.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
PANTHER; PTHR10404; PTHR10404; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Calcium; Carboxypeptidase; Cell membrane; Complete proteome;
Dipeptidase; Direct protein sequencing; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Multifunctional enzyme;
Phosphoprotein; Protease; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 751 Glutamate carboxypeptidase 2.
/FTId=PRO_0000174119.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 43 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 44 750 Extracellular. {ECO:0000255}.
REGION 275 588 NAALADase.
REGION 518 519 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
REGION 535 537 Substrate binding.
{ECO:0000250|UniProtKB:Q04609}.
REGION 553 554 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
REGION 700 701 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
COMPBIAS 147 150 Poly-Pro.
ACT_SITE 425 425 Nucleophile; for NAALADase activity.
{ECO:0000250}.
ACT_SITE 629 629 Charge relay system. {ECO:0000255}.
ACT_SITE 667 667 Charge relay system. {ECO:0000255}.
ACT_SITE 690 690 Charge relay system. {ECO:0000255}.
METAL 270 270 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 273 273 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q04609}.
METAL 378 378 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 388 388 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 388 388 Zinc 2. {ECO:0000250|UniProtKB:Q04609}.
METAL 426 426 Zinc 2. {ECO:0000250|UniProtKB:Q04609}.
METAL 434 434 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 437 437 Calcium. {ECO:0000250|UniProtKB:Q04609}.
METAL 454 454 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
METAL 554 554 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q04609}.
BINDING 211 211 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 258 258 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 425 425 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Q0}.
BINDING 520 520 Substrate.
{ECO:0000250|UniProtKB:Q04609}.
BINDING 553 553 Substrate.
{ECO:0000250|UniProtKB:Q04609}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P70627}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 639 639 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q04609}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 751 AA; 84524 MW; AF77B35236328CCA CRC64;
MWNPLHETDS TSVAWRRPRW LCAGALVLAA GLFVLGFLFG WFIKSPNEAA NISPQHNVKK
AFLDELKAEN IKTFLYNFTR IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY
PNKTRPNYIS IIDEDGNEIF NTSLFEPPPP GYENVSDVVP PFSAFSPQGM PEGDLVYVNY
ARTEDFFKLE RDMKINCSGK ILIARYGKIF RGNKVKNAQL AGAKGIILYS DPADYFAPGV
QSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RLQIAEAVGL PRIPVHPIGY
SDAQKLLEKM GGSAPPDDSW KGSLHVPYNV GPGFTGNFST QKVKMHIHSD NKVKRIYNVI
GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGKLKKEG WRPRRTVLFA
SWDAEEYGLF GSTEWAEENS RILQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK
ELQSPDEGFE GKSLFESWNE KSPSPEFSGL PRISKLGSGN DFEVFFQRLG IASGRARYTK
DWVTNKFSSY PLYHSVYETY ELVEKFYDPT FKYHLAVAQV RGGIVFELAN SVVRPFDCRD
YAVVLRNYAD KLYNISMNHP QEMKAYSVSF DSLFSAVKNF TEIASNFSER VQDLDKNNPI
LLRIMNDQLM FLERAFIVPL GLPDRAFYRH VIYAPSSHNK YMGESFPGIY DALFDIENKV
DPSKAWGEVK RQISIAAFTV QAAAGTLREV A


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