ID B7P2M5_IXOSC Unreviewed; 341 AA.
AC B7P2M5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 75.
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=IscW_ISCW015933 {ECO:0000313|EMBL:EEC00847.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC00847.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC00847.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW015933-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW015933-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; ABJB011109336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS623090; EEC00847.1; -; Genomic_DNA.
DR RefSeq; XP_002402580.1; XM_002402536.1.
DR AlphaFoldDB; B7P2M5; -.
DR STRING; 6945.B7P2M5; -.
DR GlyCosmos; B7P2M5; 1 site, No reported glycans.
DR PaxDb; 6945-B7P2M5; -.
DR EnsemblMetazoa; ISCW015933-RA; ISCW015933-PA; ISCW015933.
DR KEGG; isc:IscW_ISCW015933; -.
DR VEuPathDB; VectorBase:ISCI015933; -.
DR VEuPathDB; VectorBase:ISCP_010004; -.
DR VEuPathDB; VectorBase:ISCW015933; -.
DR HOGENOM; CLU_043332_1_0_1; -.
DR InParanoid; B7P2M5; -.
DR OMA; VTVAIFM; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
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 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 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:UP000001555};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..341
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010825752"
FT DOMAIN 37..259
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 43
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 84
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-1"
FT BINDING 119
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 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-3"
FT DISULFID 170..235
FT /evidence="ECO:0000256|PIRSR:PIRSR000898-2"
SQ SEQUENCE 341 AA; 38775 MW; F869499EE0BFA313 CRC64;
MAAAVVPLLP TWLGAGVQAL QTSSIRVSGP ADNQSVRFLV FGDWGGLPFY PYTTRIQRNL
AKTMAAVATI KNIDFVLSLG DNFYFKGVRN ADDRRFKRTF EDVYHAASLQ VPWLILAGNH
DHDGNVSAQI AYTKKSKRWY FPNYYYKKNY KIPGSDGTLD ILMLDTVLLC GNTDPEDEES
QPIPQKRNEA LYNRQFRWIN KQLAESTQVS VTARYILVAG HYPIYSACSH GTTKCLERDL
VPLLQKYRVN AYLAGHDHDL QHIRPDTENW TVEYFISGCT NFINPSLIHR RSLPRNSLKF
AWASVFSYGG FAYMEAATDS MAITFYDSTG KILHENVMKP R
//
