PPA5_RAT
ID PPA5_RAT Reviewed; 327 AA.
AC P29288;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Tartrate-resistant acid phosphatase type 5;
DE Short=TR-AP;
DE EC=3.1.3.2;
DE AltName: Full=Tartrate-resistant acid ATPase;
DE Short=TrATPase;
DE AltName: Full=Type 5 acid phosphatase;
DE Flags: Precursor;
GN Name=Acp5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RX PubMed=1722212; DOI=10.1016/s0021-9258(18)54284-8;
RA Ek-Rylander B., Bill P., Norgaard M., Nilsson S., Andersson G.;
RT "Cloning, sequence, and developmental expression of a type 5, tartrate-
RT resistant, acid phosphatase of rat bone.";
RL J. Biol. Chem. 266:24684-24689(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 23-42.
RX PubMed=1830446; DOI=10.1002/jbmr.5650060408;
RA Ek-Rylander B., Bergman T., Andersson G.;
RT "Characterization of a tartrate-resistant acid phosphatase (ATPase) from
RT rat bone: hydrodynamic properties and N-terminal amino acid sequence.";
RL J. Bone Miner. Res. 6:365-373(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-327.
RX PubMed=10388567; DOI=10.1006/jmbi.1999.2896;
RA Uppenberg J., Lindqvist F., Svensson C., Ek-Rylander B., Andersson G.;
RT "Crystal structure of a mammalian purple acid phosphatase.";
RL J. Mol. Biol. 290:201-211(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=10438611; DOI=10.1006/jmbi.1999.2962;
RA Lindqvist Y., Johansson E., Kaija H., Vihko P., Schneider G.;
RT "Three-dimensional structure of a mammalian purple acid phosphatase at 2.2
RT A resolution with a gamma-(hydr)oxo bridged di-iron center.";
RL J. Mol. Biol. 291:135-147(1999).
CC -!- FUNCTION: May play a role in the process of bone resorption. The
CC osteoclastic trap acts on nucleotide tri- and diphosphates with higher
CC affinity, compared with other substrates.
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;
CC Note=Binds 2 iron ions per subunit.;
CC -!- SUBUNIT: Exists either as monomer or, after proteolytic processing, as
CC a dimer of two chains linked by disulfide bond(s).
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Characteristic constituent of osteoclasts and some
CC mononuclear preosteoclasts. Preferentially expressed in skeletal
CC tissues.
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DR EMBL; M76110; AAA42305.1; -; mRNA.
DR EMBL; BC078847; AAH78847.1; -; mRNA.
DR PIR; A41720; A41720.
DR RefSeq; NP_001257818.1; NM_001270889.1.
DR RefSeq; NP_062017.2; NM_019144.2.
DR RefSeq; XP_006242754.1; XM_006242692.3.
DR RefSeq; XP_006242755.1; XM_006242693.3.
DR RefSeq; XP_006242756.1; XM_006242694.2.
DR PDB; 1QFC; X-ray; 2.70 A; A=22-327.
DR PDB; 1QHW; X-ray; 2.20 A; A=1-327.
DR PDBsum; 1QFC; -.
DR PDBsum; 1QHW; -.
DR AlphaFoldDB; P29288; -.
DR SMR; P29288; -.
DR IntAct; P29288; 1.
DR MINT; P29288; -.
DR STRING; 10116.ENSRNOP00000066364; -.
DR CarbonylDB; P29288; -.
DR GlyGen; P29288; 2 sites.
DR jPOST; P29288; -.
DR PaxDb; P29288; -.
DR GeneID; 25732; -.
DR KEGG; rno:25732; -.
DR CTD; 54; -.
DR RGD; 2022; Acp5.
DR VEuPathDB; HostDB:ENSRNOG00000046261; -.
DR eggNOG; KOG2679; Eukaryota.
DR HOGENOM; CLU_043332_1_0_1; -.
DR InParanoid; P29288; -.
DR PhylomeDB; P29288; -.
DR Reactome; R-RNO-196843; Vitamin B2 (riboflavin) metabolism.
DR EvolutionaryTrace; P29288; -.
DR PRO; PR:P29288; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000046261; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; P29288; baseline and differential.
DR Genevisible; P29288; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:RGD.
DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IDA:RGD.
DR GO; GO:0060349; P:bone morphogenesis; ISO:RGD.
DR GO; GO:0045453; P:bone resorption; IEP:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:RGD.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; IEP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0070723; P:response to cholesterol; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
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 Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Iron; Lysosome; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1830446"
FT CHAIN 23..327
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /id="PRO_0000023985"
FT BINDING 35
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..221
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1QFC"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1QHW"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1QHW"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1QFC"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1QHW"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1QHW"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1QFC"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:1QHW"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:1QHW"
SQ SEQUENCE 327 AA; 36726 MW; 5121A66A635ED854 CRC64;
MDTWMVLLGL QILLLPLLAH CTAPASTLRF VAVGDWGGVP NAPFHTAREM ANAKEIARTV
QIMGADFIMS LGDNFYFTGV HDANDKRFQE TFEDVFSDRA LRNIPWYVLA GNHDHLGNVS
AQIAYSKISK RWNFPSPYYR LRFKVPRSNI TVAIFMLDTV MLCGNSDDFV SQQPEMPRDL
GVARTQLSWL KKQLAAAKED YVLVAGHYPI WSIAEHGPTR CLVKNLRPLL AAYGVTAYLC
GHDHNLQYLQ DENGVGYVLS GAGNFMDPSV RHQRKVPNGY LRFHYGSEDS LGGFTYVEIG
SKEMSITYVE ASGKSLFKTS LPRRPRP
