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Database: UniProt
Entry: M3YLK6_MUSPF
LinkDB: M3YLK6_MUSPF
Original site: M3YLK6_MUSPF 
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}.
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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
//
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