ID   PXYP1_HUMAN             Reviewed;         480 AA.
AC   Q8TE99; D3DNF5; Q49AJ2; W0TR04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000303|PubMed:24425863};
DE            EC=3.1.3.- {ECO:0000269|PubMed:24425863};
DE   AltName: Full=Acid phosphatase-like protein 2;
DE   AltName: Full=Xylosyl phosphatase {ECO:0000303|PubMed:24425863, ECO:0000312|EMBL:BAO45795.1};
DE   AltName: Full=epididymis luminal protein 124 {ECO:0000303|Ref.2, ECO:0000312|EMBL:ACJ13731.1};
GN   Name=PXYLP1 {ECO:0000312|HGNC:HGNC:26303};
GN   Synonyms=ACPL2, HEL124 {ECO:0000303|Ref.2,
GN   ECO:0000312|EMBL:ACJ13731.1}, XYLP {ECO:0000303|PubMed:24425863};
GN   ORFNames=UNQ370/PRO706;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH B3GAT3, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary {ECO:0000312|EMBL:BAO45795.1};
RX   PubMed=24425863; DOI=10.1074/jbc.m113.520536;
RA   Koike T., Izumikawa T., Sato B., Kitagawa H.;
RT   "Identification of phosphatase that dephosphorylates xylose in the
RT   glycosaminoglycan-protein linkage region of proteoglycans.";
RL   J. Biol. Chem. 289:6695-6708(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li J.Y., Wang H.Y., Liu F.J., Liu J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hepatoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Ovary, and Testis;
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:0000269|PubMed:24425863}.
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:0000269|PubMed:24425863};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.8. {ECO:0000269|PubMed:24425863};
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:0000269|PubMed:24425863}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:24425863}; Single-pass type II membrane protein
CC       {ECO:0000255}. Note=Colocalizes to Golgi apparatus in a B3GAT3-
CC       dependent manner. {ECO:0000269|PubMed:24425863}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TE99-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TE99-2; Sequence=VSP_030432;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in spleen,
CC       fetal liver, moderately in placenta, pancreas, kidney, thymus and
CC       colon. {ECO:0000269|PubMed:24425863}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AB827640; BAO45795.1; -; mRNA.
DR   EMBL; EU794677; ACJ13731.1; -; mRNA.
DR   EMBL; AY358460; AAQ88825.1; -; mRNA.
DR   EMBL; AK074331; BAB85053.1; -; mRNA.
DR   EMBL; CH471052; EAW79007.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79009.1; -; Genomic_DNA.
DR   EMBL; BC035834; AAH35834.1; -; mRNA.
DR   EMBL; BC036701; AAH36701.1; -; mRNA.
DR   CCDS; CCDS3116.1; -. [Q8TE99-1]
DR   RefSeq; NP_001032249.1; NM_001037172.2. [Q8TE99-1]
DR   RefSeq; NP_001269657.1; NM_001282728.1.
DR   RefSeq; NP_689495.1; NM_152282.4. [Q8TE99-1]
DR   RefSeq; XP_016862999.1; XM_017007510.1.
DR   AlphaFoldDB; Q8TE99; -.
DR   SMR; Q8TE99; -.
DR   BioGRID; 124942; 31.
DR   IntAct; Q8TE99; 7.
DR   STRING; 9606.ENSP00000286353; -.
DR   DEPOD; PXYLP1; -.
DR   GlyCosmos; Q8TE99; 3 sites, 1 glycan.
DR   GlyGen; Q8TE99; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TE99; -.
DR   PhosphoSitePlus; Q8TE99; -.
DR   BioMuta; PXYLP1; -.
DR   DMDM; 74730610; -.
DR   EPD; Q8TE99; -.
DR   jPOST; Q8TE99; -.
DR   MassIVE; Q8TE99; -.
DR   PaxDb; 9606-ENSP00000286353; -.
DR   PeptideAtlas; Q8TE99; -.
DR   ProteomicsDB; 74427; -. [Q8TE99-1]
DR   ProteomicsDB; 74428; -. [Q8TE99-2]
DR   Pumba; Q8TE99; -.
DR   Antibodypedia; 2523; 156 antibodies from 20 providers.
DR   DNASU; 92370; -.
DR   Ensembl; ENST00000286353.9; ENSP00000286353.4; ENSG00000155893.13. [Q8TE99-1]
DR   Ensembl; ENST00000393010.6; ENSP00000376733.2; ENSG00000155893.13. [Q8TE99-1]
DR   GeneID; 92370; -.
DR   KEGG; hsa:92370; -.
DR   MANE-Select; ENST00000286353.9; ENSP00000286353.4; NM_001037172.3; NP_001032249.1.
DR   UCSC; uc003etu.5; human. [Q8TE99-1]
DR   AGR; HGNC:26303; -.
DR   CTD; 92370; -.
DR   DisGeNET; 92370; -.
DR   GeneCards; PXYLP1; -.
DR   HGNC; HGNC:26303; PXYLP1.
DR   HPA; ENSG00000155893; Tissue enhanced (epididymis).
DR   MIM; 619732; gene.
DR   neXtProt; NX_Q8TE99; -.
DR   OpenTargets; ENSG00000155893; -.
DR   PharmGKB; PA134964387; -.
DR   VEuPathDB; HostDB:ENSG00000155893; -.
DR   eggNOG; KOG3672; Eukaryota.
DR   GeneTree; ENSGT00390000016324; -.
DR   InParanoid; Q8TE99; -.
DR   OMA; DWEWNYY; -.
DR   OrthoDB; 3403603at2759; -.
DR   PhylomeDB; Q8TE99; -.
DR   TreeFam; TF318821; -.
DR   PathwayCommons; Q8TE99; -.
DR   SignaLink; Q8TE99; -.
DR   BioGRID-ORCS; 92370; 12 hits in 1156 CRISPR screens.
DR   ChiTaRS; PXYLP1; human.
DR   GenomeRNAi; 92370; -.
DR   Pharos; Q8TE99; Tbio.
DR   PRO; PR:Q8TE99; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8TE99; Protein.
DR   Bgee; ENSG00000155893; Expressed in corpus epididymis and 186 other cell types or tissues.
DR   ExpressionAtlas; Q8TE99; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
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.
DR   Genevisible; Q8TE99; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..480
FT                   /note="2-phosphoxylose phosphatase 1"
FT                   /id="PRO_0000314924"
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        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   VAR_SEQ         1..27
FT                   /note="MLFRNRFLLLLALAALLAFVSLSLQFF -> MEHSVCPSSAV (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030432"
SQ   SEQUENCE   480 AA;  55240 MW;  C1A8BEC2B68ECA62 CRC64;
     MLFRNRFLLL LALAALLAFV SLSLQFFHLI PVSTPKNGMS SKSRKRIMPD PVTEPPVTDP
     VYEALLYCNI PSVAERSMEG HAPHHFKLVS VHVFIRHGDR YPLYVIPKTK RPEIDCTLVA
     NRKPYHPKLE AFISHMSKGS GASFESPLNS LPLYPNHPLC EMGELTQTGV VQHLQNGQLL
     RDIYLKKHKL LPNDWSADQL YLETTGKSRT LQSGLALLYG FLPDFDWKKI YFRHQPSALF
     CSGSCYCPVR NQYLEKEQRR QYLLRLKNSQ LEKTYGEMAK IVDVPTKQLR AANPIDSMLC
     HFCHNVSFPC TRNGCVDMEH FKVIKTHQIE DERERREKKL YFGYSLLGAH PILNQTIGRM
     QRATEGRKEE LFALYSAHDV TLSPVLSALG LSEARFPRFA ARLIFELWQD REKPSEHSVR
     ILYNGVDVTF HTSFCQDHHK RSPKPMCPLE NLVRFVKRDM FVALGGSGTN YYDACHREGF
//