PXYP1_DANRE
ID PXYP1_DANRE Reviewed; 503 AA.
AC Q6DH46;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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;
GN ORFNames=zgc:92652;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larval eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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. {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; BC076136; AAH76136.1; -; mRNA.
DR RefSeq; NP_001002430.1; NM_001002430.1.
DR AlphaFoldDB; Q6DH46; -.
DR SMR; Q6DH46; -.
DR STRING; 7955.ENSDARP00000111067; -.
DR PaxDb; Q6DH46; -.
DR GeneID; 436703; -.
DR KEGG; dre:436703; -.
DR CTD; 92370; -.
DR ZFIN; ZDB-GENE-040718-127; pxylp1.
DR eggNOG; KOG3672; Eukaryota.
DR InParanoid; Q6DH46; -.
DR OrthoDB; 995564at2759; -.
DR PhylomeDB; Q6DH46; -.
DR PRO; PR:Q6DH46; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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..503
FT /note="2-phosphoxylose phosphatase 1"
FT /id="PRO_0000314927"
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..503
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 503 AA; 57021 MW; 6A7AC989468E8D12 CRC64;
MLARSRFILV LVVGALLAVL SFSLQYLHLI PTNPVAEQRS AGRSRKRVNP VLHTDPPAPD
PIRDTHQYCN YPNLTEHGWE GHCPPDYKLL SVQVMIRHGD RFPLYSIPKT KKPTIDCILS
EKRKPSHPLL ASFISHMALG GRGHWDASLG SLPRLPSHST CEMGELTQTG VVRQLKNGDH
LRQAYISRHN LLAADWLPRQ LWAETTGKSR TLQSGLAFLF GFLPHFDWSR LTVRQQWSTL
FCGQSCDCPA RNRYLDQEQR RQYRQRIADA ELERTYVTMA KTLGVATKTL RAANPVDALL
CHFCHGLPFP CSSTQTSSNA PDEGACLTLE HFAVIRRQQK DDELERREAG LYRRYAVLAA
HPYLNRSAAR LERIARGSQM RKSKEDAVFA LASAHDVTMA PLLSALGLEG AGFPKFAARL
VFELWSSPET KERRSDRKLD NMFIRVLYNG EDLTFDTAFC REHNRRSTQP LCPLGNFLSF
VRKDMFSVVN ATSYQQACHQ TVL
