LOCUS       NP_149059                426 aa            linear   PRI 28-APR-2025
DEFINITION  testicular acid phosphatase precursor [Homo sapiens].
ACCESSION   NP_149059
VERSION     NP_149059.1
DBSOURCE    REFSEQ: accession NM_033068.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Liang,T., Wang,S.K., Smith,C., Zhang,H., Hu,Y., Seymen,F.,
            Koruyucu,M., Kasimoglu,Y., Kim,J.W., Zhang,C., Saunders,T.L.,
            Simmer,J.P. and Hu,J.C.
  TITLE     Enamel defects in Acp4R110C/R110C mice and human ACP4 mutations
  JOURNAL   Sci Rep 12 (1), 16477 (2022)
   PUBMED   36183038
  REMARK    GeneRIF: Enamel defects in Acp4(R110C/R110C) mice and human ACP4
            mutations.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Kim,Y.J., Lee,Y., Kasimoglu,Y., Seymen,F., Simmer,J.P., Hu,J.C.,
            Cho,E.S. and Kim,J.W.
  TITLE     Recessive Mutations in ACP4 Cause Amelogenesis Imperfecta
  JOURNAL   J Dent Res 101 (1), 37-45 (2022)
   PUBMED   34036831
  REMARK    GeneRIF: Recessive Mutations in ACP4 Cause Amelogenesis Imperfecta.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Smith,C.E., Whitehouse,L.L., Poulter,J.A., Brookes,S.J., Day,P.F.,
            Soldani,F., Kirkham,J., Inglehearn,C.F. and Mighell,A.J.
  TITLE     Defects in the acid phosphatase ACPT cause recessive hypoplastic
            amelogenesis imperfecta
  JOURNAL   Eur J Hum Genet 25 (8), 1015-1019 (2017)
   PUBMED   28513613
  REMARK    GeneRIF: ACPT missense mutation segregates with hypoplastic
            amelogenesis imperfecta in two unrelated families.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Seymen,F., Kim,Y.J., Lee,Y.J., Kang,J., Kim,T.H., Choi,H.,
            Koruyucu,M., Kasimoglu,Y., Tuna,E.B., Gencay,K., Shin,T.J.,
            Hyun,H.K., Kim,Y.J., Lee,S.H., Lee,Z.H., Zhang,H., Hu,J.C.,
            Simmer,J.P., Cho,E.S. and Kim,J.W.
  TITLE     Recessive Mutations in ACPT, Encoding Testicular Acid Phosphatase,
            Cause Hypoplastic Amelogenesis Imperfecta
  JOURNAL   Am J Hum Genet 99 (5), 1199-1205 (2016)
   PUBMED   27843125
  REMARK    GeneRIF: ACPT biallelic mutations caused non-syndromic, generalized
            hypoplastic autosomal-recessive amelogenesis imperfecta in
            individuals from six unrelated Turkish families. Analysis of the
            ACPT crystal structure suggests that these mutations damaged the
            activity of ACPT by altering the sizes and charges of key amino
            acid side chains, limiting accessibility of the catalytic core, and
            interfering with homodimerization.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Fleisig,H., El-Din El-Husseini,A. and Vincent,S.R.
  TITLE     Regulation of ErbB4 phosphorylation and cleavage by a novel
            histidine acid phosphatase
  JOURNAL   Neuroscience 127 (1), 91-100 (2004)
   PUBMED   15219672
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Yousef,G.M., Diamandis,M., Jung,K. and Diamandis,E.P.
  TITLE     Molecular cloning of a novel human acid phosphatase gene (ACPT)
            that is highly expressed in the testis
  JOURNAL   Genomics 74 (3), 385-395 (2001)
   PUBMED   11414767
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010325.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Acid phosphatases are enzymes capable of hydrolyzing
            orthophosphoric acid esters in an acid medium. This gene is
            up-regulated by androgens and is down-regulated by estrogens in the
            prostate cancer cell line. This gene exhibits a lower level of
            expression in testicular cancer tissues than in normal tissues. The
            protein encoded by this gene has structural similarity to prostatic
            and lysosomal acid phosphatases. Alternatively spliced transcript
            variants have been described, but their biological validity has not
            been determined. [provided by RefSeq, Jul 2008].
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270593.2/ ENSP00000270593.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..426
                     /product="testicular acid phosphatase precursor"
                     /EC_number="3.1.3.2"
                     /note="testicular acid phosphatase; acid phosphatase,
                     testicular"
                     /calculated_mol_wt=43174
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2934
     mat_peptide     29..426
                     /product="testicular acid phosphatase"
                     /calculated_mol_wt=43174
     Region          32..316
                     /region_name="HP_HAP_like"
                     /note="Histidine phosphatase domain found in histidine
                     acid phosphatases and phytases; contains a His residue
                     which is phosphorylated during the reaction; cd07061"
                     /db_xref="CDD:132717"
     Site            order(40..41,44,111,288..289)
                     /site_type="active"
                     /note="catalytic core [active]"
                     /db_xref="CDD:132717"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZG2.1)"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZG2.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZG2.1)"
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZG2.1)"
     Site            394..414
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZG2.1)"
     CDS             1..426
                     /gene="ACP4"
                     /gene_synonym="ACPT; AI1J"
                     /coded_by="NM_033068.3:1..1281"
                     /db_xref="CCDS:CCDS12802.1"
                     /db_xref="GeneID:93650"
                     /db_xref="HGNC:HGNC:14376"
                     /db_xref="MIM:606362"
ORIGIN      
        1 maglgfwghp agplllllll vlppralpeg plvfvalvfr hgdraplasy pmdphkevas
       61 tlwprglgql ttegvrqqle lgrflrsrye aflspeyrre evyirstdfd rtlesaqanl
      121 aglfpeaapg spearwrpip vhtvpvaedk llrfpmrscp ryhellreat eaaeyqeale
      181 gwtgflsrle nftglslvge plrrawkvld tlmcqqahgl plpawaspdv lrtlaqisal
      241 digahvgppr aaekaqltgg illnailanf srvqrlglpl kmvmysahds tllalqgalg
      301 lydghtppya aclgfefrkh lgnpakdggn vtvslfyrnd sahlplplsl pgcpapcplg
      361 rfyqltapar ppahgvschg pyeaaippap vvpllagava vlvalslglg llawrpgclr
      421 alggpv
//
