PPA5_PIG
ID PPA5_PIG Reviewed; 340 AA.
AC P09889;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 4.
DT 03-AUG-2022, entry version 155.
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 AltName: Full=Uteroferrin;
DE Short=UF;
DE Flags: Precursor;
GN Name=ACP5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=8463220; DOI=10.1016/s0021-9258(18)53124-0;
RA Ling P., Roberts R.M.;
RT "Uteroferrin and intracellular tartrate-resistant acid phosphatases are the
RT products of the same gene.";
RL J. Biol. Chem. 268:6896-6902(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2598770; DOI=10.1089/dna.1989.8.543;
RA Simmen R.C.M., Srinivas V., Roberts R.M.;
RT "cDNA sequence, gene organization, and progesterone induction of mRNA for
RT uteroferrin, a porcine uterine iron transport protein.";
RL DNA 8:543-554(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11098218; DOI=10.1089/10445490050199072;
RA Vallet J.L., Fahrenkrug S.C.;
RT "Structure of the gene for uteroferrin.";
RL DNA Cell Biol. 19:689-696(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 186-215 AND 247-301.
RX PubMed=2969454; DOI=10.1210/mend-2-3-253;
RA Simmen R.C.M., Baumbach G.A., Roberts R.M.;
RT "Molecular cloning and temporal expression during pregnancy of the
RT messenger ribonucleic acid encoding uteroferrin, a progesterone-induced
RT uterine secretory protein.";
RL Mol. Endocrinol. 2:253-262(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 108-195.
RX PubMed=7587387; DOI=10.1159/000134120;
RA Yasue H., Kusumoto H., Mikami H.;
RT "Assignment of the uteroferrin gene (ACP5) to swine chromosome 2q12-q21 by
RT fluorescence in situ hybridization.";
RL Cytogenet. Cell Genet. 71:249-252(1995).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3579955; DOI=10.1016/0006-291x(87)91432-x;
RA Hunt D.F., Yates J.R. III, Shabanowitz J., Zhu N.-Z., Zirino T.,
RA Averill B.A., Daurat-Larroque S.T., Shewale J.G., Roberts R.M., Brew K.;
RT "Sequence homology in the metalloproteins; purple acid phosphatase from
RT beef spleen and uteroferrin from porcine uterus.";
RL Biochem. Biophys. Res. Commun. 144:1154-1160(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 28-340.
RX PubMed=10425678; DOI=10.1016/s0969-2126(99)80100-2;
RA Guddat L.W., McAlpine A.S., Hume D., Hamilton S., de Jersey J.,
RA Martin J.L.;
RT "Crystal structure of mammalian purple acid phosphatase.";
RL Structure 7:757-767(1999).
CC -!- FUNCTION: Uteroferrin is a phosphoprotein phosphatase, synthesized in
CC response to progesterone. It appears to function in transplacental
CC transport of iron in pig.
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 -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; M98553; AAA31129.1; -; mRNA.
DR EMBL; M30284; AAA31139.1; -; mRNA.
DR EMBL; M30283; AAA31138.1; -; Genomic_DNA.
DR EMBL; AF292105; AAG10065.1; -; Genomic_DNA.
DR EMBL; M31214; AAA31134.1; -; mRNA.
DR EMBL; M31215; AAA31135.1; -; mRNA.
DR EMBL; S80099; AAD14321.1; -; mRNA.
DR PIR; A46096; A46096.
DR RefSeq; NP_999374.1; NM_214209.1.
DR PDB; 1UTE; X-ray; 1.55 A; A=28-340.
DR PDB; 5UQ6; X-ray; 1.18 A; A=28-340.
DR PDB; 7OV2; X-ray; 2.10 A; A=28-340.
DR PDB; 7OV3; X-ray; 2.00 A; A=28-340.
DR PDB; 7OV8; X-ray; 2.30 A; A=1-331.
DR PDBsum; 1UTE; -.
DR PDBsum; 5UQ6; -.
DR PDBsum; 7OV2; -.
DR PDBsum; 7OV3; -.
DR PDBsum; 7OV8; -.
DR AlphaFoldDB; P09889; -.
DR SMR; P09889; -.
DR STRING; 9823.ENSSSCP00000014466; -.
DR BindingDB; P09889; -.
DR ChEMBL; CHEMBL4295708; -.
DR PaxDb; P09889; -.
DR PeptideAtlas; P09889; -.
DR PRIDE; P09889; -.
DR Ensembl; ENSSSCT00025026575; ENSSSCP00025011265; ENSSSCG00025019530.
DR Ensembl; ENSSSCT00050051467; ENSSSCP00050021599; ENSSSCG00050038159.
DR Ensembl; ENSSSCT00055058257; ENSSSCP00055046602; ENSSSCG00055029348.
DR Ensembl; ENSSSCT00065064276; ENSSSCP00065027841; ENSSSCG00065047000.
DR Ensembl; ENSSSCT00070050077; ENSSSCP00070042305; ENSSSCG00070025047.
DR GeneID; 397414; -.
DR KEGG; ssc:397414; -.
DR CTD; 54; -.
DR eggNOG; KOG2679; Eukaryota.
DR InParanoid; P09889; -.
DR OMA; VTVAIFM; -.
DR OrthoDB; 711825at2759; -.
DR BRENDA; 3.1.3.2; 6170.
DR Reactome; R-SSC-196843; Vitamin B2 (riboflavin) metabolism.
DR EvolutionaryTrace; P09889; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0045453; P:bone resorption; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; 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 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; Ion transport; Iron; Iron transport; Metal-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..340
FT /note="Tartrate-resistant acid phosphatase type 5"
FT /id="PRO_0000023984"
FT BINDING 41
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 250
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 169..227
FT CONFLICT 183..184
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5UQ6"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:5UQ6"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7OV2"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:5UQ6"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1UTE"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:5UQ6"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:5UQ6"
SQ SEQUENCE 340 AA; 38012 MW; CEE15351288179F7 CRC64;
MDTWTVLLIL QASLVLPGAV GTRTNTRTAP TPILRFVAVG DWGGVPNAPF HTAREMANAK
AIATTVKTLG ADFILSLGDN FYFTGVHDAK DKRFQETFED VFSDPSLRNV PWHVLAGNHD
HLGNVSAQIA YSKISKRWNF PSPYYRLRFK IPRSNVSVAI FMLDTVTLCG NSDDFVSQQP
ERPRNLALAR TQLAWIKKQL AAAKEDYVLV AGHYPVWSIA EHGPTHCLVK QLLPLLTTHK
VTAYLCGHDH NLQYLQDENG LGFVLSGAGN FMDPSKKHLR KVPNGYLRFH FGAENSLGGF
AYVEITPKEM SVTYIEASGK SLFKTKLPRR ARSEHQHRRA
