ID   ACP7_DANRE              Reviewed;         443 AA.
AC   A5D6U8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Acid phosphatase type 7 {ECO:0000305};
DE            EC=3.1.3.2;
DE   AltName: Full=Purple acid phosphatase long form {ECO:0000250|UniProtKB:Q6ZNF0};
DE   Flags: Precursor;
GN   Name=acp7 {ECO:0000250|UniProtKB:Q6ZNF0};
GN   Synonyms=papl {ECO:0000250|UniProtKB:Q6ZNF0}; ORFNames=zgc:162913;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC       acid phosphatase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC139891; AAI39892.1; -; mRNA.
DR   RefSeq; NP_001092720.1; NM_001099250.1.
DR   AlphaFoldDB; A5D6U8; -.
DR   SMR; A5D6U8; -.
DR   STRING; 7955.ENSDARP00000141174; -.
DR   GlyCosmos; A5D6U8; 7 sites, No reported glycans.
DR   PaxDb; 7955-ENSDARP00000087672; -.
DR   GeneID; 571830; -.
DR   KEGG; dre:571830; -.
DR   AGR; ZFIN:ZDB-GENE-070615-9; -.
DR   CTD; 390928; -.
DR   ZFIN; ZDB-GENE-070615-9; acp7.
DR   eggNOG; KOG1378; Eukaryota.
DR   InParanoid; A5D6U8; -.
DR   OrthoDB; 203742at2759; -.
DR   PhylomeDB; A5D6U8; -.
DR   PRO; PR:A5D6U8; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   InterPro; IPR015914; Purple_acid_Pase_N.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   PANTHER; PTHR45867:SF3; ACID PHOSPHATASE TYPE 7; 1.
DR   PANTHER; PTHR45867; PURPLE ACID PHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   Pfam; PF16656; Pur_ac_phosph_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Iron; Metal-binding; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..443
FT                   /note="Acid phosphatase type 7"
FT                   /id="PRO_0000316826"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  50745 MW;  50C1B424AE238465 CRC64;
     MAAAPPPPPP LLLLLLCVCA VFADVPIGTQ PEQVHISYPG VQNSMLVTWS SANKTDSVVE
     YGLWGGKLFS HSATGNSSIF INEGAEYRVM YIHRVLLTDL RPAASYVYHC GSGAGWSELF
     FFTALNESVF FSPGFALFGD LGNENPQSLS RLQKETQIGT YDVILHIGDF AYDLYEDNGR
     IGDEFMKQIQ SIAAYVPYMT CPGNHEWAFN FSQYRARFSM PGDTEGLWYS WNVGPAHIIS
     FSTEVYFYYL EYGLDLLFRQ YEWLRADLQE ANRPENRAER PWIITMGHRP MYCSNDDDDD
     CTHFQSYVRL GRNDTKPPAP GLEELFYQYG VDLELWAHEH TYERLWPVYD YKVFNGSSEE
     PYVNPKAPVH IITGSAGCRE KHDGFIPKPR DWSAFRSTDY GYTRLQLINN THLYLEQVSD
     DQYGKVIDQM TLVKEKHGPD AWR
//