ISPD_XENTR
ID ISPD_XENTR Reviewed; 411 AA.
AC Q28CZ7; B7ZU47; Q28CQ3;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=D-ribitol-5-phosphate cytidylyltransferase {ECO:0000250|UniProtKB:A4D126};
DE EC=2.7.7.40 {ECO:0000250|UniProtKB:A4D126};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein {ECO:0000250|UniProtKB:A4D126};
DE AltName: Full=Isoprenoid synthase domain-containing protein {ECO:0000250|UniProtKB:A4D126};
GN Name=crppa; Synonyms=ispd {ECO:0000250|UniProtKB:A4D126};
GN ORFNames=TEgg020n22.1 {ECO:0000303|Ref.1},
GN TGas037c08.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Egg, and Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytidylyltransferase required for protein O-linked
CC mannosylation (By similarity). Catalyzes the formation of CDP-ribitol
CC nucleotide sugar from D-ribitol 5-phosphate. CDP-ribitol is a substrate
CC of FKTN during the biosynthesis of the phosphorylated O-mannosyl
CC trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-
CC (phosphate-6-)mannose), a carbohydrate structure present in alpha-
CC dystroglycan (DAG1), which is required for binding laminin G-like
CC domain-containing extracellular proteins with high affinity (By
CC similarity). Shows activity toward other pentose phosphate sugars and
CC mediates formation of CDP-ribulose or CDP-ribose using CTP and
CC ribulose-5-phosphate or ribose-5-phosphate, respectively (By
CC similarity). Not involved in dolichol production (By similarity).
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol +
CC diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608,
CC ChEBI:CHEBI:57695; EC=2.7.7.40;
CC Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribose 5-phosphate + H(+) = CDP-D-ribose +
CC diphosphate; Xref=Rhea:RHEA:53872, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:137525; Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + D-ribulose 5-phosphate + H(+) = CDP-D-ribulose +
CC diphosphate; Xref=Rhea:RHEA:53612, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58121,
CC ChEBI:CHEBI:137524; Evidence={ECO:0000250|UniProtKB:A4D126};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A4D126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A4D126}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q28CZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28CZ7-2; Sequence=VSP_044047, VSP_044048;
CC Name=3;
CC IsoId=Q28CZ7-3; Sequence=VSP_044048;
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
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DR EMBL; CR855789; CAJ83376.1; -; mRNA.
DR EMBL; CR926258; CAJ81436.1; -; mRNA.
DR EMBL; AAMC01021497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01021503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC171103; AAI71103.1; -; mRNA.
DR RefSeq; NP_001016240.1; NM_001016240.1. [Q28CZ7-2]
DR RefSeq; XP_012820139.1; XM_012964685.2. [Q28CZ7-1]
DR RefSeq; XP_012820140.1; XM_012964686.2.
DR RefSeq; XP_017950136.1; XM_018094647.1. [Q28CZ7-1]
DR RefSeq; XP_017950137.1; XM_018094648.1. [Q28CZ7-3]
DR AlphaFoldDB; Q28CZ7; -.
DR SMR; Q28CZ7; -.
DR PaxDb; Q28CZ7; -.
DR Ensembl; ENSXETT00000049329; ENSXETP00000049329; ENSXETG00000022799.
DR GeneID; 548994; -.
DR KEGG; xtr:548994; -.
DR CTD; 729920; -.
DR Xenbase; XB-GENE-1014860; crppa.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR HOGENOM; CLU_033636_0_0_1; -.
DR InParanoid; Q28CZ7; -.
DR OMA; LKEWNFI; -.
DR OrthoDB; 1356473at2759; -.
DR TreeFam; TF328415; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022799; Expressed in skeletal muscle tissue and 12 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070567; F:cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR GO; GO:0060049; P:regulation of protein glycosylation; IEA:Ensembl.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR040635; ISPD_C.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF18706; ISPD_C; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..411
FT /note="D-ribitol-5-phosphate cytidylyltransferase"
FT /id="PRO_0000418387"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 30
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 170
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 228
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT VAR_SEQ 276
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_044047"
FT VAR_SEQ 378..411
FT /note="DKVQLQQTVCEGTAIITALIKDRNPALVGQLMVA -> QTEMCNAIGAVLST
FT SKPCHSAEKDIFDPM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.3"
FT /id="VSP_044048"
SQ SEQUENCE 411 AA; 45558 MW; 45293DBEBBF6D7CF CRC64;
MDDAAKDLGR CAVVLPAGGC GERLGSLTPK QFCTVLGRPL ISHTLEAFER ASWIKDIIVV
VASESLDLMK AIIHKYGHQR VTLVKGGETR HRSIFNGLKV FSENHSDDTA IDKPEVVIIH
DAVRPFVDED FLLQVAKSAK QHGAAGAIRP LVSTVIASSS DGFLDYSLER ARHRASEMPQ
AFQYDVIYRA YLQCTDYDLD FGTECLHLAL QYSNVKAKLL EGPPDLWKVT YKRDLYAAES
VIKESISQQL CIVTNVKKEA IEVGFLLHEN LKLHYKVKAV SSSMCKTIHH LQNIFHGQCC
NFICINVKDL DFEETQNLVD LLQTTNASIS YPLVIVSVHL TTEDSSSGNK LSGVRKLAKE
AHKSNILVYG LLINIDQDKV QLQQTVCEGT AIITALIKDR NPALVGQLMV A
