ID M3YLK6_MUSPF Unreviewed; 481 AA.
AC M3YLK6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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|Ensembl:ENSMPUP00000012213.1,
GN ECO:0000313|RefSeq:XP_044944378.1, ECO:0000313|RefSeq:XP_044944379.1,
GN ECO:0000313|RefSeq:XP_044944380.1, ECO:0000313|RefSeq:XP_044944381.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012213.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012213.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044944378.1, ECO:0000313|RefSeq:XP_044944379.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044944378.1,
RC ECO:0000313|RefSeq:XP_044944379.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEYP01101324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01101325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01101326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004780915.1; XM_004780858.1.
DR RefSeq; XP_004780916.1; XM_004780859.2.
DR RefSeq; XP_044944378.1; XM_045088443.1.
DR RefSeq; XP_044944379.1; XM_045088444.1.
DR RefSeq; XP_044944380.1; XM_045088445.1.
DR RefSeq; XP_044944381.1; XM_045088446.1.
DR STRING; 9669.ENSMPUP00000012213; -.
DR Ensembl; ENSMPUT00000012413.1; ENSMPUP00000012213.1; ENSMPUG00000012309.1.
DR KEGG; mpuf:101675418; -.
DR eggNOG; KOG3672; Eukaryota.
DR GeneTree; ENSGT00390000016324; -.
DR HOGENOM; CLU_033855_1_0_1; -.
DR OMA; DWEWNYY; -.
DR OrthoDB; 3403603at2759; -.
DR Proteomes; UP000000715; 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:UP000000715};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..481
FT /note="2-phosphoxylose phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041198576"
SQ SEQUENCE 481 AA; 55415 MW; 7A587DBE4D0BA45E CRC64;
MLFRSRFLLL LALAAVLAFV SLSLQFFHLT PVSTAKNGVS SKSRKRVMPE PVTEPPVTDP
IYEALLYCNI PSVAERSMEG HAPHHFKLVS VHVFIRHGDR YPLYVIPKTK RPEIDCTLVA
NRKPYHPKLE AFVSHMSKGS GASFESPLHS LPLYPNHPLC EMGELTQTGV VQHLQNGQLL
RDIYLKKHKL LPSDWSTDHL YLETTGKSRT LQSGLALLYG FLPDFDWKKI HFRHQPSALF
CSGNCYCPMR NQYLEKEQRR QYLLRLKNSQ LERTYEDMAR IVDVPTKQLR AANPIDSMLC
RFCHNVSFPC TRNGCIDMEH FKVIKTHQIE DERERREKKL YLGYALLGAH PILNQTVNRM
QRAAEGRREE VFALYSAHDV TLSPVLSALG LMEARFPRFA ARLILELWQD REKPSEHSVR
ILYNGVDVTF HTSFCQDHHK HSSKPMCPLE NLVRFVKRDM FVALGSSGSP NYYDACHREG
F
//