RXLT1_MOUSE
ID RXLT1_MOUSE Reviewed; 444 AA.
AC Q8VDX6; Q8R566;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ribitol-5-phosphate xylosyltransferase 1 {ECO:0000305};
DE EC=2.4.2.61 {ECO:0000250|UniProtKB:Q9Y2B1};
DE AltName: Full=Transmembrane protein 5 {ECO:0000305};
DE AltName: Full=UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase {ECO:0000250|UniProtKB:Q9Y2B1};
GN Name=Rxylt1 {ECO:0000312|MGI:MGI:2384919}; Synonyms=Tmem5;
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=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: 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. Participates in the biosynthesis of the phosphorylated
CC O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-
CC acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate
CC structure present in alpha-dystroglycan (DAG1), which is required for
CC binding laminin G-like domain-containing extracellular proteins with
CC high affinity. {ECO:0000250|UniProtKB:Q9Y2B1}.
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 -!- SUBUNIT: Forms a complex composed of FKTN/fukutin, FKRP and
CC RXYLT1/TMEM5. {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 -!- SIMILARITY: Belongs to the RXYLT1 family. {ECO:0000305}.
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DR EMBL; BC020100; AAH20100.1; -; mRNA.
DR EMBL; BC023194; AAH23194.1; -; mRNA.
DR CCDS; CCDS24214.1; -.
DR RefSeq; NP_694699.1; NM_153059.1.
DR AlphaFoldDB; Q8VDX6; -.
DR BioGRID; 229741; 1.
DR STRING; 10090.ENSMUSP00000119308; -.
DR iPTMnet; Q8VDX6; -.
DR PhosphoSitePlus; Q8VDX6; -.
DR jPOST; Q8VDX6; -.
DR MaxQB; Q8VDX6; -.
DR PaxDb; Q8VDX6; -.
DR PeptideAtlas; Q8VDX6; -.
DR PRIDE; Q8VDX6; -.
DR ProteomicsDB; 259427; -.
DR Antibodypedia; 29125; 157 antibodies from 24 providers.
DR DNASU; 216395; -.
DR Ensembl; ENSMUST00000140299; ENSMUSP00000119308; ENSMUSG00000034620.
DR GeneID; 216395; -.
DR KEGG; mmu:216395; -.
DR UCSC; uc007hgd.1; mouse.
DR CTD; 10329; -.
DR MGI; MGI:2384919; Rxylt1.
DR VEuPathDB; HostDB:ENSMUSG00000034620; -.
DR eggNOG; ENOG502QT2E; Eukaryota.
DR GeneTree; ENSGT00390000003526; -.
DR HOGENOM; CLU_040812_0_0_1; -.
DR InParanoid; Q8VDX6; -.
DR OMA; PVVEPSW; -.
DR OrthoDB; 912057at2759; -.
DR PhylomeDB; Q8VDX6; -.
DR TreeFam; TF328717; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 216395; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Rxylt1; mouse.
DR PRO; PR:Q8VDX6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VDX6; protein.
DR Bgee; ENSMUSG00000034620; Expressed in ectoplacental cone and 252 other tissues.
DR ExpressionAtlas; Q8VDX6; baseline and differential.
DR Genevisible; Q8VDX6; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
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:0005654; C:nucleoplasm; ISO:MGI.
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..444
FT /note="Ribitol-5-phosphate xylosyltransferase 1"
FT /id="PRO_0000072588"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 38..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 51386 MW; 6A4F0548D91024FF CRC64;
MRLTRTRLCS LLVALYCLFS IYAAYHVFFG RRRRPLGTTS RNSRKAAAAQ AKERRGREQS
ALESEEWNPW EGDEKNEQRH RVKTNLQILN KSTKEKIEHR VQIWGKAAIG LYLWEHIFEG
TLDPADVTAQ WREGQSVVGR THYSFITGPA VVPGYFSIDV DNVVLVLNGR EKAKIFHATQ
WLIYAQNLMK TQKLQHLAVV LLGNEHCEND WIMQFLKRNG GFVDLLFITY DSPWINGADI
LQWPLGVATY RQFPVVEASW TMLHDERPYI CNFLGTAYEN SSRQALMNIL KQDGNDKLCW
VSAREQWQPQ ETNESLKNYQ DALLHSDLTL CPVGVNTECY RIYEACSFGS IPVVEDVMTA
GHCGNTTSQH SAPLQLLKAM GAPFIFIKNW KELPAILEKE KTISLQEKIQ RRKVLLHWYQ
HFKTELKWKF TKILESSFFI NNKV
