ACP7_DANRE
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 03-AUG-2022, entry version 77.
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}.
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DR EMBL; BC139891; AAI39892.1; -; mRNA.
DR RefSeq; NP_001092720.1; NM_001099250.1.
DR AlphaFoldDB; A5D6U8; -.
DR SMR; A5D6U8; -.
DR STRING; 7955.ENSDARP00000087672; -.
DR PaxDb; A5D6U8; -.
DR GeneID; 571830; -.
DR KEGG; dre:571830; -.
DR CTD; 390928; -.
DR ZFIN; ZDB-GENE-070615-9; acp7.
DR eggNOG; KOG1378; Eukaryota.
DR InParanoid; A5D6U8; -.
DR OrthoDB; 426430at2759; -.
DR PhylomeDB; A5D6U8; -.
DR PRO; PR:A5D6U8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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 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 Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 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
