FOH1B_HUMAN
ID FOH1B_HUMAN Reviewed; 442 AA.
AC Q9HBA9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative N-acetylated-alpha-linked acidic dipeptidase;
DE Short=NAALADase;
DE EC=3.4.-.-;
DE AltName: Full=Cell growth-inhibiting gene 26 protein;
DE AltName: Full=Prostate-specific membrane antigen-like protein;
DE AltName: Full=Putative folate hydrolase 1B;
GN Name=FOLH1B; Synonyms=PSMAL; ORFNames=GIG26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=14716746; DOI=10.1002/pros.10319;
RA O'Keefe D.S., Bacich D.J., Heston W.D.W.;
RT "Comparative analysis of prostate-specific membrane antigen (PSMA) versus a
RT prostate-specific membrane antigen-like gene.";
RL Prostate 58:200-210(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human cell growth inhibition gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-
CC acidic dipeptidase (NAALADase) activity. {ECO:0000250}.
CC -!- FUNCTION: Exhibits a dipeptidyl-peptidase IV type activity.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14716746}.
CC -!- TISSUE SPECIFICITY: Kidney and liver. Not expressed in the prostate.
CC {ECO:0000269|PubMed:14716746}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; AF261715; AAG29102.1; -; mRNA.
DR EMBL; AY544126; AAT11157.1; -; mRNA.
DR RefSeq; NP_710163.1; NM_153696.2.
DR AlphaFoldDB; Q9HBA9; -.
DR SMR; Q9HBA9; -.
DR BioGRID; 128556; 11.
DR MEROPS; M28.010; -.
DR GlyGen; Q9HBA9; 5 sites.
DR iPTMnet; Q9HBA9; -.
DR PhosphoSitePlus; Q9HBA9; -.
DR BioMuta; HGNC:13636; -.
DR DMDM; 74718738; -.
DR MassIVE; Q9HBA9; -.
DR MaxQB; Q9HBA9; -.
DR PeptideAtlas; Q9HBA9; -.
DR PRIDE; Q9HBA9; -.
DR ProteomicsDB; 81517; -.
DR DNASU; 219595; -.
DR GeneID; 219595; -.
DR KEGG; hsa:219595; -.
DR CTD; 219595; -.
DR DisGeNET; 219595; -.
DR GeneCards; FOLH1B; -.
DR HGNC; HGNC:13636; FOLH1B.
DR MIM; 609020; gene.
DR neXtProt; NX_Q9HBA9; -.
DR PharmGKB; PA165543408; -.
DR InParanoid; Q9HBA9; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q9HBA9; -.
DR PathwayCommons; Q9HBA9; -.
DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
DR SignaLink; Q9HBA9; -.
DR BioGRID-ORCS; 219595; 4 hits in 118 CRISPR screens.
DR ChiTaRS; FOLH1B; human.
DR GenomeRNAi; 219595; -.
DR Pharos; Q9HBA9; Tbio.
DR PRO; PR:Q9HBA9; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9HBA9; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:BHF-UCL.
DR GO; GO:0035609; P:C-terminal protein deglutamylation; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dipeptidase; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Multifunctional enzyme; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..442
FT /note="Putative N-acetylated-alpha-linked acidic
FT dipeptidase"
FT /id="PRO_0000256137"
FT ACT_SITE 116
FT /note="For NAALADase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 226..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 391..392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Q0"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT VARIANT 151
FT /note="N -> K (in dbSNP:rs10830339)"
FT /id="VAR_059782"
SQ SEQUENCE 442 AA; 50045 MW; 26CD6E082AC1E8D3 CRC64;
MGGSAPPDSS WRGSLKVSYN VGPGFTGNFS TQKVKMHIHS TNEVTRIYNV IGTLRGAVEP
DRYVILGGHR DSWVFGGIDP QSGAAVVHET VRSFGTLKKE GWRPRRTILF ASWDAEEFGL
LGSTEWAEDN SRLLQERGVA YINADSSIEG NYTLRVDCTP LMYSLVYNLT KELKSPDEGF
EGKSLYESWT KKSPSPEFSG MPRISKLGSG NDFEVFFQRL GIASGRARYT KNWETNKFSG
YPLYHSVYET YELVEKFYDP MFKYHLTVAQ VRGGMVFELA NSIVLPFDCR DYAVVLRKYA
DKIYNISMKH PQEMKTYSLS FDSLFSAVKN FTEIASKFSE RLQDFDKSNP ILLRMMNDQL
MFLERAFIDP LGLPDRPFYR HVIYAPSSHN KYAGESFPGI YDALFDIESK VDPSKAWGDV
KRQISVAAFT VQAAAETLSE VA
