RXLT1_DANRE
ID RXLT1_DANRE Reviewed; 434 AA.
AC Q08CD5; F1RDU5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ribitol-5-phosphate xylosyltransferase 1 {ECO:0000250|UniProtKB:Q9Y2B1};
DE EC=2.4.2.61 {ECO:0000250|UniProtKB:Q9Y2B1};
DE AltName: Full=Transmembrane protein 5 {ECO:0000250|UniProtKB:Q9Y2B1};
DE AltName: Full=UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase {ECO:0000250|UniProtKB:Q9Y2B1};
GN Name=rxylt1; Synonyms=tmem5;
GN ORFNames=zgc:153239 {ECO:0000303|PubMed:27130732};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27130732; DOI=10.7554/elife.14473;
RA Praissman J.L., Willer T., Sheikh M.O., Toi A., Chitayat D., Lin Y.Y.,
RA Lee H., Stalnaker S.H., Wang S., Prabhakar P.K., Nelson S.F., Stemple D.L.,
RA Moore S.A., Moremen K.W., Campbell K.P., Wells L.;
RT "The functional O-mannose glycan on alpha-dystroglycan contains a phospho-
RT ribitol primed for matriglycan addition.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Acts as a UDP-D-xylose:ribitol-5-phosphate beta1,4-
CC xylosyltransferase, which catalyzes the transfer of UDP-D-xylose to
CC ribitol 5-phosphate (Rbo5P) to form the Xylbeta1-4Rbo5P linkage on O-
CC mannosyl glycan (By similarity). Participates in the biosynthesis of
CC the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-
CC beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a
CC carbohydrate structure present in alpha-dystroglycan (DAG1), which is
CC required for binding laminin G-like domain-containing extracellular
CC proteins with high affinity (PubMed:27130732).
CC {ECO:0000250|UniProtKB:Q9Y2B1, ECO:0000269|PubMed:27130732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-
CC (1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-xylose = 3-O-
CC [beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-
CC GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:57880, Rhea:RHEA-COMP:15021, Rhea:RHEA-COMP:15023,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:142403, ChEBI:CHEBI:142405; EC=2.4.2.61;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2B1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57881;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2B1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9Y2B1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9Y2B1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9Y2B1}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout early embryonic development.
CC {ECO:0000269|PubMed:27130732}.
CC -!- DISRUPTION PHENOTYPE: Embryos display mild to severe hydrocephalus and
CC significantly reduced eye size, reminiscent of pathological defects in
CC Walker-Warburg syndrome. {ECO:0000269|PubMed:27130732}.
CC -!- SIMILARITY: Belongs to the TMEM5 family. {ECO:0000305}.
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DR EMBL; CABZ01034123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01070849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01081731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124285; AAI24286.1; -; mRNA.
DR RefSeq; NP_001068580.1; NM_001075112.1.
DR AlphaFoldDB; Q08CD5; -.
DR STRING; 7955.ENSDARP00000087080; -.
DR PaxDb; Q08CD5; -.
DR PRIDE; Q08CD5; -.
DR Ensembl; ENSDART00000092648; ENSDARP00000087080; ENSDARG00000063414.
DR GeneID; 557187; -.
DR KEGG; dre:557187; -.
DR CTD; 10329; -.
DR ZFIN; ZDB-GENE-060929-1018; rxylt1.
DR eggNOG; ENOG502QT2E; Eukaryota.
DR GeneTree; ENSGT00390000003526; -.
DR InParanoid; Q08CD5; -.
DR OMA; PVVEPSW; -.
DR OrthoDB; 912057at2759; -.
DR PhylomeDB; Q08CD5; -.
DR TreeFam; TF328717; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q08CD5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000063414; Expressed in early embryo and 21 other tissues.
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:0120053; F:ribitol beta-1,4-xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Ribitol-5-phosphate xylosyltransferase 1"
FT /id="PRO_0000360147"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 40
FT /note="V -> M (in Ref. 2; AAI24286)"
FT CONFLICT 211
FT /note="L -> P (in Ref. 2; AAI24286)"
FT CONFLICT 230
FT /note="V -> I (in Ref. 2; AAI24286)"
FT CONFLICT 280
FT /note="S -> T (in Ref. 2; AAI24286)"
SQ SEQUENCE 434 AA; 50383 MW; 1EA51700B90CBD47 CRC64;
MRFFRRKIAI IVILAYAIFS LYAAYNVFFS KRVISRVHRV VKKGSVIIET GKAGEKEWNP
WEEDERAHSV VVQKRRDAFR LYRDQAAKNR PKTYKVQIWG KAAIGLYLWE HILEGSLNPS
DKSSQWREGE IQSGKIHFSF YTGPAVVQGH VPPDTDSVVL VLNGREQQKI SYSVQWLQHV
QSLIQARTIS RVAVVLLGNE QCNNNWISPY LKRNGGFVDL LFLVYDSPWV NDKDIFQWPL
GVATYRHFPV VTLSSQMVKK DRPYLCNFLG TIYKNSSRES LMNLLKQNNM EKDCLMHARE
KWLPQETSDT SRQYQMALAQ SDLTLCPVGV NSECYRIYEA CAYGSVPVVE DVLTPGACAV
GNRSPLRLLK DAGAPFIFLK DWKELPVILE RERAMSQKEK TERRMRLLEW YSSFRQQMKD
RFTEVLEENF FKIT
