ID A0A2G8JQT5_STIJA Unreviewed; 350 AA.
AC A0A2G8JQT5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=Tartrate-resistant acid phosphatase type 5 {ECO:0000256|ARBA:ARBA00015822, ECO:0000256|PIRNR:PIRNR000898};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000898};
GN ORFNames=BSL78_25017 {ECO:0000313|EMBL:PIK38132.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK38132.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK38132.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK38132.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK38132.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 ECO:0000256|PIRNR:PIRNR000898};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR000898-1};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000898-1};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK38132.1}.
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; MRZV01001399; PIK38132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JQT5; -.
DR STRING; 307972.A0A2G8JQT5; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07378; MPP_ACP5; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024927; Acid_PPase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000898};
KW Iron {ECO:0000256|PIRNR:PIRNR000898, ECO:0000256|PIRSR:PIRSR000898-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000898-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..350
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013634437"
FT DOMAIN 42..259
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 48
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-3"
SQ SEQUENCE 350 AA; 39114 MW; 284116210323ED2B CRC64;
MAFNWSPLLQ VIALFIVAVS VTGTKSKEAR DLGNRTAEDE LNFLVIADWG GIPIWPYVSP
DELSVAVQMA KISAEVDAKF VLAYGDNFYE DGVKDVNDKR FTETFENVFS QTSLQIPWYV
VAGNHDHRGN VSGQIAYSDK SNRWNFPSEY YRLNFKIPGG GATMVVLMID TVVLCGGAHD
DVPGCDLRGP DNPVHAETQW QWIEKELEAS KDADYVIVGG HYPVWSISEH GPTIRLVDRL
RPLLLKYNVT AYFSGHDHNL QHIRESNTSL DVFVIGSANI VQPSLAHMDS VPAEWVKFYY
AHLGSLGGFA YVTATSDKLK LTFVTGVGNR DIYSIDMMPR PKNHILEQNL
//
