PXYP1_XENTR
ID PXYP1_XENTR Reviewed; 501 AA.
AC Q0IHQ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000250|UniProtKB:Q8TE99};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q8TE99};
DE AltName: Full=Acid phosphatase-like protein 2;
GN Name=pxylp1 {ECO:0000250|UniProtKB:Q8TE99}; Synonyms=acpl2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for the 2-O-dephosphorylation of xylose in the
CC glycosaminoglycan-protein linkage region of proteoglycans thereby
CC regulating the amount of mature glycosaminoglycan (GAG) chains.
CC Sulfated glycosaminoglycans (GAGs), including heparan sulfate and
CC chondroitin sulfate, are synthesized on the so-called common GAG-
CC protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser)
CC of core proteins, which is formed by the stepwise addition of
CC monosaccharide residues by the respective specific
CC glycosyltransferases. Xylose 2-O-dephosphorylation during completion of
CC linkage region formation is a prerequisite for the initiation and
CC efficient elongation of the repeating disaccharide region of GAG
CC chains. {ECO:0000250|UniProtKB:Q8TE99}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-2-O-P-Xyl]-L-seryl-[protein] + H2O = 3-O-(beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:56512, Rhea:RHEA-COMP:12573, Rhea:RHEA-
CC COMP:14559, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:132093,
CC ChEBI:CHEBI:140495; Evidence={ECO:0000250|UniProtKB:Q8TE99};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8TE99}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; BC123016; AAI23017.1; -; mRNA.
DR RefSeq; NP_001072621.1; NM_001079153.1.
DR AlphaFoldDB; Q0IHQ9; -.
DR SMR; Q0IHQ9; -.
DR STRING; 8364.ENSXETP00000063266; -.
DR PaxDb; Q0IHQ9; -.
DR PRIDE; Q0IHQ9; -.
DR DNASU; 780077; -.
DR GeneID; 780077; -.
DR KEGG; xtr:780077; -.
DR CTD; 92370; -.
DR Xenbase; XB-GENE-979576; pxylp1.
DR eggNOG; KOG3672; Eukaryota.
DR InParanoid; Q0IHQ9; -.
DR OrthoDB; 995564at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="2-phosphoxylose phosphatase 1"
FT /id="PRO_0000314928"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..501
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 402
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 501 AA; 57977 MW; 92FB07C4CBF11B71 CRC64;
MLLRNRFLLL LALAGLLAFL SLSLQFFSRW LPVSLQLKTE MQVFPEFPVR LIQVGQGREE
GLGAKNRKRI MPEPLTEPPA LNPLYEANLY CNTPGAKERS MEGHAPPNLK LLSVQVIIRH
GDRYPLYTIP KTKRPDIDCV LEPGRKPSHP HLTDFISHMS KGVDTQMDGT LGSLPRLPNH
ILCEMGELTQ TGVVQHLRNG QLLKEIYLKK HRLLTSAWTA KHLYFESTGK SRTLQSGLAL
LYSLLPNFDW KKINVKHQWS TIFCSNHCDC PMRNHYLEEE QRRQYNFRVK NSLLEKTYIN
MAKIVGIPTR QLRASNPIDS LLCNFCHNAT FPCTKNGCID LEHFKVIKTH QLEDEKERYE
KQLYFKYALM ATHPLLNQTA NRMLRIAEGK KDELFALYSA HDVTLSPILS ALGLREARFP
RFAARLVFEL WHDPEKANNH YVRVLYNGED VTFQTSFCRD QLRSSKRPLC PLKKFSTFVQ
KDMFSSLNST SYYDACHQRL F
