ID   C3Z555_BRAFL            Unreviewed;       356 AA.
AC   C3Z555;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BRAFLDRAFT_76217 {ECO:0000313|EMBL:EEN52412.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN52412.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN52412.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN52412.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; GG666582; EEN52412.1; -; Genomic_DNA.
DR   RefSeq; XP_002596400.1; XM_002596354.1.
DR   AlphaFoldDB; C3Z555; -.
DR   STRING; 7739.C3Z555; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   InParanoid; C3Z555; -.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..356
FT                   /note="Acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002936398"
FT   REGION          325..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  40497 MW;  E41A90FB62574BF8 CRC64;
     MVGRLCPLVA IFVLESFVVT TGQSVKDERS LVQAHVLFRH GDRSPTETFP NDVHQESAWE
     QGFGFLSSIG IEQHHNLGEF FRKRYGKEGF GVLSEEFRRD ELFVRSTDTD RTLMSAEANL
     DRLYPDQPVP IHTVRTGLDK LLRAFFLNCP RSDELLEEAM NSAEFKQKEK ENEEFMAFVV
     EKAGWSEPHS ILDAWRTQDP LLCEKAHNMK WPAWVTPDVY KRLTELTSYA SDIQFRGDEK
     GRLMAGLLVN HIVSNMTTAQ QEVQENKKPL RLIMYSAHDI DISALMSALN IYNGLSPPYA
     SCVMAELYRD NQGVSLRRVL REHRAARGAE PDAPSSATRL IGRQEDSVVT PLHDVS
//