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Database: UniProt
Entry: Q9BZG2
LinkDB: Q9BZG2
Original site: Q9BZG2 
ID   PPAT_HUMAN              Reviewed;         426 AA.
AC   Q9BZG2; C0H3P7; Q9BZG3; Q9BZG4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   01-OCT-2014, entry version 88.
DE   RecName: Full=Testicular acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=ACPT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), INDUCTION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=11414767; DOI=10.1006/geno.2001.6556;
RA   Yousef G.M., Diamandis M., Jung K., Diamandis E.P.;
RT   "Molecular cloning of a novel human acid phosphatase gene (ACPT) that
RT   is highly expressed in the testis.";
RL   Genomics 74:385-395(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Testis;
RX   PubMed=15219672; DOI=10.1016/j.neuroscience.2004.04.060;
RA   Fleisig H., El-Din El-Husseini A., Vincent S.R.;
RT   "Regulation of ErbB4 phosphorylation and cleavage by a novel histidine
RT   acid phosphatase.";
RL   Neuroscience 127:91-100(2004).
CC   -!- FUNCTION: Dephosphorylates receptor tyrosine-protein kinase erbB-4
CC       and inhibits the ligand-induced proteolytic cleavage.
CC       {ECO:0000269|PubMed:15219672}.
CC   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15219672}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9BZG2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Variant 3;
CC         IsoId=Q9BZG2-2; Sequence=VSP_021494;
CC       Name=3; Synonyms=Truncated variant 1, Truncated variant 2;
CC         IsoId=Q9BZG2-3; Sequence=VSP_021493, VSP_021495;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in the testis. Also expressed
CC       in the brain where they are enriched at the postsynaptic sites.
CC       Expressed at lower levels in the trachea, prostate, bone marrow,
CC       spinal cord, colon, fetal brain, heart, thymus, fetal liver,
CC       spleen, leukocytes, ovary, small intestine, pancreas and skeletal
CC       muscle. Expression is significantly lower in testicular cancer
CC       tissues than in normal testicular tissues. Isoform 3 is expressed
CC       in the testis, trachea, prostate and bone marrow.
CC       {ECO:0000269|PubMed:11414767}.
CC   -!- INDUCTION: Up-regulated by mibolerone (a synthetic androgen) and
CC       dihydrotestosterone (DHT) and is down-regulated by estrogen and
CC       progestin. {ECO:0000269|PubMed:11414767}.
CC   -!- PTM: Glycosylated. {ECO:0000305|PubMed:15219672}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AF321918; AAK09393.1; -; Genomic_DNA.
DR   EMBL; AF321918; AAK09394.1; -; Genomic_DNA.
DR   EMBL; AF321918; AAK09395.1; -; Genomic_DNA.
DR   EMBL; AF321918; AAK09396.1; -; Genomic_DNA.
DR   CCDS; CCDS12802.1; -. [Q9BZG2-1]
DR   RefSeq; NP_149059.1; NM_033068.2. [Q9BZG2-1]
DR   UniGene; Hs.293394; -.
DR   ProteinModelPortal; Q9BZG2; -.
DR   SMR; Q9BZG2; 32-378.
DR   STRING; 9606.ENSP00000270593; -.
DR   PhosphoSite; Q9BZG2; -.
DR   DMDM; 74717749; -.
DR   PaxDb; Q9BZG2; -.
DR   PRIDE; Q9BZG2; -.
DR   DNASU; 93650; -.
DR   Ensembl; ENST00000270593; ENSP00000270593; ENSG00000142513. [Q9BZG2-1]
DR   GeneID; 93650; -.
DR   KEGG; hsa:93650; -.
DR   UCSC; uc002pta.1; human. [Q9BZG2-1]
DR   CTD; 93650; -.
DR   GeneCards; GC19P051293; -.
DR   HGNC; HGNC:14376; ACPT.
DR   MIM; 606362; gene.
DR   neXtProt; NX_Q9BZG2; -.
DR   PharmGKB; PA24450; -.
DR   eggNOG; NOG85977; -.
DR   HOGENOM; HOG000231439; -.
DR   HOVERGEN; HBG002203; -.
DR   InParanoid; Q9BZG2; -.
DR   KO; K14410; -.
DR   OMA; ISLFYRN; -.
DR   OrthoDB; EOG7GXPBJ; -.
DR   PhylomeDB; Q9BZG2; -.
DR   TreeFam; TF312893; -.
DR   GenomeRNAi; 93650; -.
DR   NextBio; 78184; -.
DR   PRO; PR:Q9BZG2; -.
DR   Bgee; Q9BZG2; -.
DR   CleanEx; HS_ACPT; -.
DR   Genevestigator; Q9BZG2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR000560; His_Pase_superF_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    426       Testicular acid phosphatase.
FT                                /FTId=PRO_0000259643.
FT   TOPO_DOM     27    393       Extracellular. {ECO:0000255}.
FT   TRANSMEM    394    414       Helical. {ECO:0000255}.
FT   TOPO_DOM    415    426       Cytoplasmic. {ECO:0000255}.
FT   ACT_SITE     41     41       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    289    289       Proton donor. {ECO:0000250}.
FT   CARBOHYD    191    191       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    159    378       {ECO:0000250}.
FT   DISULFID    214    312       {ECO:0000250}.
FT   DISULFID    353    357       {ECO:0000250}.
FT   VAR_SEQ      39     92       FRHGDRAPLASYPMDPHKEVASTLWPRGLGQLTTEGVRQQL
FT                                ELGRFLRSRYEAF -> RRPHPGLPLAPPGLALTSPVPRYS
FT                                AMATGPRWPPTPWTHTRRWPPPCGHEAWAS (in
FT                                isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_021493.
FT   VAR_SEQ      91    183       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_021494.
FT   VAR_SEQ      93    426       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_021495.
SQ   SEQUENCE   426 AA;  46090 MW;  BE930398041DB061 CRC64;
     MAGLGFWGHP AGPLLLLLLL VLPPRALPEG PLVFVALVFR HGDRAPLASY PMDPHKEVAS
     TLWPRGLGQL TTEGVRQQLE LGRFLRSRYE AFLSPEYRRE EVYIRSTDFD RTLESAQANL
     AGLFPEAAPG SPEARWRPIP VHTVPVAEDK LLRFPMRSCP RYHELLREAT EAAEYQEALE
     GWTGFLSRLE NFTGLSLVGE PLRRAWKVLD TLMCQQAHGL PLPAWASPDV LRTLAQISAL
     DIGAHVGPPR AAEKAQLTGG ILLNAILANF SRVQRLGLPL KMVMYSAHDS TLLALQGALG
     LYDGHTPPYA ACLGFEFRKH LGNPAKDGGN VTVSLFYRND SAHLPLPLSL PGCPAPCPLG
     RFYQLTAPAR PPAHGVSCHG PYEAAIPPAP VVPLLAGAVA VLVALSLGLG LLAWRPGCLR
     ALGGPV
//
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