ID W5MNB1_LEPOC Unreviewed; 325 AA.
AC W5MNB1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009870.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009870.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR EMBL; AHAT01016122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MNB1; -.
DR STRING; 7918.ENSLOCP00000009870; -.
DR Ensembl; ENSLOCT00000009882.1; ENSLOCP00000009870.1; ENSLOCG00000008124.1.
DR eggNOG; KOG2679; Eukaryota.
DR GeneTree; ENSGT00390000016735; -.
DR HOGENOM; CLU_043332_1_0_1; -.
DR InParanoid; W5MNB1; -.
DR OMA; VWSIGNH; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000008124; Expressed in intestine and 11 other cell types or tissues.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0045453; P:bone resorption; IBA:GO_Central.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
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:SF29; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR000898-2};
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:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..325
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866288"
FT DOMAIN 27..242
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 34
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 72
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 72
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-3"
FT DISULFID 162..218
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-2"
SQ SEQUENCE 325 AA; 36734 MW; 31093BEAF229EB23 CRC64;
MGKVTCLLLV CLQAILSNCQ SKENDYLRFV AIGDWGGSPD SPFFTPLEKA VAAEMGRVAQ
TVGLDFVLSL GDHFYYQGVK DIDDFRFKAT FENVFADPSL LSVPWYLVAG NHDHLRNVTA
QVAYSKRSKR WNFPELYYDL YFKVPHSNTS VTILLIDTVL LCGNTYDGIQ PEKPENHEAA
AKQFIWIKEK LEKSKSEFLI VAGHYPVWSI GHHGPTQCLV EQLRPLLKKH NVTAYLSGHD
HSLQFIQEDN GMAYIVSGSG NFVDMSIYHK NKFPHAWQLF SSAVNNTFGG FAYFTVTKEK
MFINYISAAG EGVYQTSLSK RSAEW
//
