PXYP1_MOUSE
ID PXYP1_MOUSE Reviewed; 480 AA.
AC Q8BHA9; Q8BZ12;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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:0000312|MGI:MGI:2442444}; Synonyms=Acpl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Embryo, Embryonic head, Embryonic heart, Lung, and
RC Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Xylose 2-O-dephosphorylation during completion of
CC linkage region formation is a prerequisite for the initiation and
CC efficient elongation of the repeating disaccharide region of GAG
CC chains. {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 -!- SUBUNIT: Interacts with B3GAT3; the interaction increases the 2-
CC phosphoxylose phosphatase activity of PXYLP1 during completion of
CC linkage region formation in a B3GAT3-mediated manner.
CC {ECO:0000250|UniProtKB:Q8TE99}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8TE99}; Single-pass type II membrane protein
CC {ECO:0000255}. Note=Colocalizes to Golgi apparatus in a B3GAT3-
CC dependent manner. {ECO:0000250|UniProtKB:Q8TE99}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AK036973; BAC29653.1; -; mRNA.
DR EMBL; AK043758; BAC31644.1; -; mRNA.
DR EMBL; AK082059; BAC38400.1; -; mRNA.
DR EMBL; AK083712; BAC39001.1; -; mRNA.
DR EMBL; AK084605; BAC39227.1; -; mRNA.
DR EMBL; AK144699; BAE26021.1; -; mRNA.
DR EMBL; AK164254; BAE37705.1; -; mRNA.
DR EMBL; BC023960; AAH23960.1; -; mRNA.
DR EMBL; BC036342; AAH36342.1; -; mRNA.
DR CCDS; CCDS23418.1; -.
DR RefSeq; NP_001276574.1; NM_001289645.1.
DR RefSeq; NP_001276575.1; NM_001289646.1.
DR RefSeq; NP_001276576.1; NM_001289647.1.
DR RefSeq; NP_700469.1; NM_153420.3.
DR RefSeq; XP_006511201.1; XM_006511138.3.
DR RefSeq; XP_017168835.1; XM_017313346.1.
DR AlphaFoldDB; Q8BHA9; -.
DR SMR; Q8BHA9; -.
DR STRING; 10090.ENSMUSP00000108574; -.
DR GlyGen; Q8BHA9; 3 sites.
DR PhosphoSitePlus; Q8BHA9; -.
DR EPD; Q8BHA9; -.
DR MaxQB; Q8BHA9; -.
DR PaxDb; Q8BHA9; -.
DR PeptideAtlas; Q8BHA9; -.
DR PRIDE; Q8BHA9; -.
DR ProteomicsDB; 300362; -.
DR Antibodypedia; 2523; 138 antibodies from 19 providers.
DR DNASU; 235534; -.
DR Ensembl; ENSMUST00000078478; ENSMUSP00000077571; ENSMUSG00000043587.
DR Ensembl; ENSMUST00000112951; ENSMUSP00000108574; ENSMUSG00000043587.
DR Ensembl; ENSMUST00000119141; ENSMUSP00000113489; ENSMUSG00000043587.
DR Ensembl; ENSMUST00000120101; ENSMUSP00000113210; ENSMUSG00000043587.
DR GeneID; 235534; -.
DR KEGG; mmu:235534; -.
DR UCSC; uc009rcu.2; mouse.
DR CTD; 92370; -.
DR MGI; MGI:2442444; Pxylp1.
DR VEuPathDB; HostDB:ENSMUSG00000043587; -.
DR eggNOG; KOG3672; Eukaryota.
DR GeneTree; ENSGT00390000016324; -.
DR HOGENOM; CLU_033855_1_0_1; -.
DR InParanoid; Q8BHA9; -.
DR OMA; FCHNISF; -.
DR OrthoDB; 995564at2759; -.
DR PhylomeDB; Q8BHA9; -.
DR TreeFam; TF318821; -.
DR BioGRID-ORCS; 235534; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Pxylp1; mouse.
DR PRO; PR:Q8BHA9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BHA9; protein.
DR Bgee; ENSMUSG00000043587; Expressed in humerus cartilage element and 225 other tissues.
DR ExpressionAtlas; Q8BHA9; baseline and differential.
DR Genevisible; Q8BHA9; MM.
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; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..480
FT /note="2-phosphoxylose phosphatase 1"
FT /id="PRO_0000314925"
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..480
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 123
FT /note="K -> N (in Ref. 1; BAC29653)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="L -> H (in Ref. 1; BAC29653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 54937 MW; 3A8E2476B9E10BB4 CRC64;
MLHRNRFLVL LALAGLLAFL SLSLQFFHLI PVSATKNGGS SKSRKRIMPD PVTEPPTVDP
VYEALLYCNI PSVAEHSMEG HAPHHYKLVS VHVFIRHGDR YPLYAIPKTK RPEIDCTLVA
SRKPYHPKLE AFISHMLKGS GASFESPLNS LPLYPNHPLC ETGELTQTGV VQHLLNGQLL
RDIYLRKHKL LPNNWSSDQL YLESTGKSRT LQSGLALLYG FLPEFDWKKV YFKHQPSALF
CSGSCYCPLR NQYLEKEQRR QYLLRLKNSD LERTYGEMAK IVDIPTKQLR AANPIDSMLC
HFCHNVSFPC SRSGCLGMEH FKVIKTHQIE DERERHEKLL YFGYSLLGAH PILNQTVNRM
QRAASGWRDE LFTLYSAHDV TLSPILSALG LLEARFPRFA ARLVFELWQD RQKPSEHSVR
ILYNGADVTF HTSFCHDFHK RSPKPMCPLE NLVRFVKRDM FVALDGSSTN YYDACHGEGA
