PXYP1_HUMAN
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 03-AUG-2022, entry version 140.
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, ECO:0000312|EMBL:ACJ13731.1},
GN XYLP {ECO:0000303|PubMed:24425863}; 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; 30.
DR IntAct; Q8TE99; 7.
DR STRING; 9606.ENSP00000286353; -.
DR DEPOD; PXYLP1; -.
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; Q8TE99; -.
DR PeptideAtlas; Q8TE99; -.
DR PRIDE; Q8TE99; -.
DR ProteomicsDB; 74427; -. [Q8TE99-1]
DR ProteomicsDB; 74428; -. [Q8TE99-2]
DR Antibodypedia; 2523; 138 antibodies from 19 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 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; RYMGNVE; -.
DR PhylomeDB; Q8TE99; -.
DR TreeFam; TF318821; -.
DR PathwayCommons; Q8TE99; -.
DR SignaLink; Q8TE99; -.
DR BioGRID-ORCS; 92370; 12 hits in 1066 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 184 other tissues.
DR ExpressionAtlas; Q8TE99; baseline and differential.
DR Genevisible; Q8TE99; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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; 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; -; 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 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
