ID A0A3Q7TX67_VULVU Unreviewed; 481 AA.
AC A0A3Q7TX67;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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_025874376.1,
GN ECO:0000313|RefSeq:XP_025874377.1, ECO:0000313|RefSeq:XP_025874378.1,
GN ECO:0000313|RefSeq:XP_025874379.1, ECO:0000313|RefSeq:XP_025874380.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025874378.1};
RN [1]
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025874377.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025874377.1};
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025874376.1, ECO:0000313|RefSeq:XP_025874378.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025874376.1,
RC ECO:0000313|RefSeq:XP_025874378.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025874376.1,
RC ECO:0000313|RefSeq:XP_025874378.1};
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_025874376.1; XM_026018591.1.
DR RefSeq; XP_025874377.1; XM_026018592.1.
DR RefSeq; XP_025874378.1; XM_026018593.1.
DR RefSeq; XP_025874379.1; XM_026018594.1.
DR RefSeq; XP_025874380.1; XM_026018595.1.
DR STRING; 9627.ENSVVUP00000036658; -.
DR KEGG; vvp:112935009; -.
DR OrthoDB; 3403603at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:UP000286640};
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..481
FT /note="2-phosphoxylose phosphatase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041129678"
SQ SEQUENCE 481 AA; 55552 MW; 7A6441B11950C6A7 CRC64;
MLFRNRFLLL LALAALLAFV SLSLQFFHLT PVSTAKNGVS SKSRKRIMPD PVTEPPVMDP
IYEALLYCNI PSVAERSMEG HAPHHFKLIS VHVFIRHGDR YPLYVIPKTK RPEIDCTLVA
NRKPYHPKLE AFVSHMSKGS GASFESPLHS LPLYPNHPLC EMGELTQTGV VQHLQNGQLL
RDIYLKKHKL LPNDWSTDQL YLETTGKSRT LQSGLALLYG FLPDFDWKKI HFRHQPSALF
CSGNCYCPVR NQYLEKEQRR QYLLRLKNSQ LERTYEDMAR IVDVPTKQLR AANPIDSMLC
HFCHNVSFPC TRNGCIDMEH FKVIKTHQIE DERERREKKL YLGYALLGAH PILNQTISRM
QRTAEGRKEE VFALYSAHDV TLSPVLSALG LMEARFPRFA ARLIFELWQD REKPSEHSVR
ILYNGVDVTF HTSFCQDHHK HSSKPMCPLE NLVRFVRRDM FVALGSSSST NYYDACHREG
F
//
