ID A0A2Y9NZE2_DELLE Unreviewed; 480 AA.
AC A0A2Y9NZE2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000256|ARBA:ARBA00040357};
DE AltName: Full=Acid phosphatase-like protein 2 {ECO:0000256|ARBA:ARBA00041499};
GN Name=PXYLP1 {ECO:0000313|RefSeq:XP_022438329.1,
GN ECO:0000313|RefSeq:XP_022438331.1, ECO:0000313|RefSeq:XP_022438332.1,
GN ECO:0000313|RefSeq:XP_022438333.1, ECO:0000313|RefSeq:XP_022438334.1,
GN ECO:0000313|RefSeq:XP_022438335.1, ECO:0000313|RefSeq:XP_022438336.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022438336.1};
RN [1] {ECO:0000313|RefSeq:XP_022438329.1, ECO:0000313|RefSeq:XP_022438331.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022438329.1,
RC ECO:0000313|RefSeq:XP_022438331.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036311};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR RefSeq; XP_022438329.1; XM_022582621.1.
DR RefSeq; XP_022438331.1; XM_022582623.1.
DR RefSeq; XP_022438332.1; XM_022582624.1.
DR RefSeq; XP_022438333.1; XM_022582625.1.
DR RefSeq; XP_022438334.1; XM_022582626.1.
DR RefSeq; XP_022438335.1; XM_022582627.1.
DR RefSeq; XP_022438336.1; XM_022582628.1.
DR STRING; 9749.A0A2Y9NZE2; -.
DR Ensembl; ENSDLET00000001994; ENSDLEP00000001748; ENSDLEG00000001445.
DR KEGG; dle:111179249; -.
DR OrthoDB; 3403603at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:Ensembl.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:Ensembl.
DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IEA:Ensembl.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF125; 2-PHOSPHOXYLOSE PHOSPHATASE 1; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..480
FT /note="2-phosphoxylose phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041069561"
SQ SEQUENCE 480 AA; 55339 MW; 1D5C153CA3AB4334 CRC64;
MLFRNRFMLL LALAALLAFV SLSLQFFHLI PVSAAKNGVT SKNRKRIMPD PVTEPPVTDP
VYEALLYCNI PRVAERSMEG HAPHHFKLVS VHVFIRHGDR YPLYVIPKTK RPEIDCTLVA
NRKPYHPKLE AFVSHMSKGS GASFESPLHS LPLYPSHQLC EMGELTQTGV VQHLQNGQLL
RDVYLKKHKL LPSDWSTEQL RLETTGKSRT LQSGLALLYG FLPDFDWKKI YFRHQPSALF
CSGNCYCPLR NQYLEKEQRR QYLLRLKNRQ LERTYEEMAR IVDTSTKQLR AANPIDAMLC
LFCHNVSFPC TRNGCVNMEH FKVIKRHQIE DESERREKKL YLGYALLGAH PILNQTVGRM
RRAAEGWKEE LFALSSAHDV TLAPILSALG LTEARFPRFA ARLIFELWQD REKPGEHSVR
ILYDGVDVTF HTSFCQDHHK RSPKPMCPLE NFVRFVKRDM FVALGSGSTN YYDACHREGS
//
