ISPD_RAT
ID ISPD_RAT Reviewed; 447 AA.
AC Q5S6T3; Q5S6T4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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:0000312|RGD:1359368};
DE AltName: Full=Notch1-induced protein {ECO:0000303|Ref.1};
GN Name=Crppa;
GN Synonyms=Ispd {ECO:0000312|RGD:1359368}, Nip {ECO:0000303|Ref.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Thymus;
RA Kwon S.H., Reichardt H.M.;
RL Submitted (OCT-2004) 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=2;
CC Name=1;
CC IsoId=Q5S6T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5S6T3-2; Sequence=VSP_034674;
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
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DR EMBL; AY769991; AAV53695.1; -; mRNA.
DR EMBL; AY769992; AAV53696.1; -; mRNA.
DR RefSeq; NP_001008387.1; NM_001008386.1. [Q5S6T3-1]
DR AlphaFoldDB; Q5S6T3; -.
DR SMR; Q5S6T3; -.
DR STRING; 10116.ENSRNOP00000008312; -.
DR PaxDb; Q5S6T3; -.
DR PRIDE; Q5S6T3; -.
DR Ensembl; ENSRNOT00000008312; ENSRNOP00000008312; ENSRNOG00000006199. [Q5S6T3-1]
DR GeneID; 493574; -.
DR KEGG; rno:493574; -.
DR UCSC; RGD:1359368; rat. [Q5S6T3-1]
DR CTD; 729920; -.
DR RGD; 1359368; Crppa.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR GeneTree; ENSGT00390000006412; -.
DR InParanoid; Q5S6T3; -.
DR OMA; LKEWNFI; -.
DR OrthoDB; 1356473at2759; -.
DR PhylomeDB; Q5S6T3; -.
DR TreeFam; TF328415; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5S6T3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000006199; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q5S6T3; baseline and differential.
DR Genevisible; Q5S6T3; RN.
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:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
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..447
FT /note="D-ribitol-5-phosphate cytidylyltransferase"
FT /id="PRO_0000343699"
FT SITE 57
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 203
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT SITE 261
FT /note="Positions substrate for the nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:Q46893"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034674"
SQ SEQUENCE 447 AA; 49192 MW; 63FC38515B4F8FDE CRC64;
MESGPCSRPA EPRHCVSGRA GAGLAFPAFP LSAAGAEPGS RIGTVAAVLP AGGCGERMGV
RTPKQFCRVL ERPLISYTLQ AMERVCWIKD IVVTVTGENM EAMRSIIQRY GHKRISLAEA
GATRHRSIFN GLKALAEDQP GCELTRPEVV IIHDAVRPFV EEDILLRVVL AAKEHGAAGA
IRPLVSTVVS PSADGHLDHS LDRAKHRASE MPQAFHFDVI YEAYQKCSDF DLEFGTECLQ
LALKYCHRKA KLVEGTPDLW KVTYKQDLCA AEAMIKEKIS QEICVVVNTK DEESVGHLLE
EVLRNELNCI KVTSTVLDRT SGDIENFIDQ CYSFICVNVV SSESRETRKL LSILEESSLP
LLYPVVVVLV HCFDFTVVPL AQKMENLVWI RELAKEAKGR NVLLSGVLLN HSQDEQKLQE
SLVQSAAIIA ALVKERNSAL VGQLLVA
