ISPD_MOUSE
ID ISPD_MOUSE Reviewed; 447 AA.
AC Q5RJG7; Q148Q0; Q501J8; Q8BR14; Q8C934; Q8CAE0; Q8CIF0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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|MGI:MGI:1923097};
GN Name=Crppa; Synonyms=Ispd {ECO:0000312|MGI:MGI:1923097};
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] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Eye, and 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: Cytidylyltransferase required for protein O-linked
CC mannosylation (By similarity). Catalyzes the formation of CDP-ribitol
CC nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-
CC ribitol is a substrate of FKTN during the biosynthesis of the
CC phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-
CC N-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 (By similarity). Shows activity toward other pentose
CC phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose
CC using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively
CC (By 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=5;
CC Name=1;
CC IsoId=Q5RJG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RJG7-2; Sequence=VSP_034670, VSP_034671;
CC Name=3;
CC IsoId=Q5RJG7-3; Sequence=VSP_034668, VSP_034669;
CC Name=4;
CC IsoId=Q5RJG7-4; Sequence=VSP_034667, VSP_034668, VSP_034669;
CC Name=5;
CC IsoId=Q5RJG7-5; Sequence=VSP_034672, VSP_034673;
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32538.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK039004; BAC30199.1; -; mRNA.
DR EMBL; AK043122; BAC31463.1; -; mRNA.
DR EMBL; AK045940; BAC32538.1; ALT_FRAME; mRNA.
DR EMBL; BC024061; AAH24061.1; -; mRNA.
DR EMBL; BC086665; AAH86665.1; -; mRNA.
DR EMBL; BC096030; AAH96030.1; -; mRNA.
DR EMBL; BC118038; AAI18039.1; -; mRNA.
DR CCDS; CCDS49051.1; -. [Q5RJG7-1]
DR CCDS; CCDS88329.1; -. [Q5RJG7-5]
DR CCDS; CCDS88330.1; -. [Q5RJG7-3]
DR RefSeq; NP_001276431.1; NM_001289502.1.
DR RefSeq; NP_001276432.1; NM_001289503.1.
DR RefSeq; NP_001276433.1; NM_001289504.1. [Q5RJG7-3]
DR RefSeq; NP_848744.2; NM_178629.6. [Q5RJG7-1]
DR RefSeq; XP_006515307.1; XM_006515244.3.
DR AlphaFoldDB; Q5RJG7; -.
DR SMR; Q5RJG7; -.
DR STRING; 10090.ENSMUSP00000061646; -.
DR PhosphoSitePlus; Q5RJG7; -.
DR MaxQB; Q5RJG7; -.
DR PaxDb; Q5RJG7; -.
DR PRIDE; Q5RJG7; -.
DR ProteomicsDB; 301675; -. [Q5RJG7-1]
DR ProteomicsDB; 301676; -. [Q5RJG7-2]
DR ProteomicsDB; 301677; -. [Q5RJG7-3]
DR ProteomicsDB; 301678; -. [Q5RJG7-4]
DR ProteomicsDB; 301679; -. [Q5RJG7-5]
DR Antibodypedia; 43951; 103 antibodies from 15 providers.
DR DNASU; 75847; -.
DR Ensembl; ENSMUST00000062041; ENSMUSP00000061646; ENSMUSG00000043153. [Q5RJG7-1]
DR Ensembl; ENSMUST00000220519; ENSMUSP00000152423; ENSMUSG00000043153. [Q5RJG7-3]
DR Ensembl; ENSMUST00000221452; ENSMUSP00000152115; ENSMUSG00000043153. [Q5RJG7-5]
DR Ensembl; ENSMUST00000221895; ENSMUSP00000152392; ENSMUSG00000043153. [Q5RJG7-2]
DR Ensembl; ENSMUST00000223068; ENSMUSP00000152318; ENSMUSG00000043153. [Q5RJG7-4]
DR GeneID; 75847; -.
DR KEGG; mmu:75847; -.
DR UCSC; uc007njy.3; mouse. [Q5RJG7-3]
DR UCSC; uc007njz.3; mouse. [Q5RJG7-2]
DR UCSC; uc007nkb.3; mouse. [Q5RJG7-1]
DR UCSC; uc007nkd.1; mouse. [Q5RJG7-4]
DR CTD; 729920; -.
DR MGI; MGI:1923097; Crppa.
DR VEuPathDB; HostDB:ENSMUSG00000043153; -.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR GeneTree; ENSGT00390000006412; -.
DR HOGENOM; CLU_033636_0_0_1; -.
DR InParanoid; Q5RJG7; -.
DR OMA; LKEWNFI; -.
DR OrthoDB; 1356473at2759; -.
DR PhylomeDB; Q5RJG7; -.
DR TreeFam; TF328415; -.
DR BRENDA; 2.7.7.40; 3474.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 75847; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Crppa; mouse.
DR PRO; PR:Q5RJG7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q5RJG7; protein.
DR Bgee; ENSMUSG00000043153; Expressed in lumbar dorsal root ganglion and 148 other tissues.
DR ExpressionAtlas; Q5RJG7; baseline and differential.
DR Genevisible; Q5RJG7; MM.
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; IMP:MGI.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
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_0000343698"
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 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034667"
FT VAR_SEQ 277..286
FT /note="EKISQEICVV -> GVFNLVTVSA (in isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034668"
FT VAR_SEQ 287..447
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034669"
FT VAR_SEQ 309..324
FT /note="CMKITSTVMDHIGGDI -> VSIQRMTWIKCHTFLW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034670"
FT VAR_SEQ 325..447
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034671"
FT VAR_SEQ 414..419
FT /note="DEQKLQ -> NFYYGG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034672"
FT VAR_SEQ 420..447
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034673"
FT CONFLICT 178
FT /note="A -> E (in Ref. 1; BAC31463)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="S -> N (in Ref. 2; AAI18039)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="P -> L (in Ref. 2; AAH24061)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="R -> H (in Ref. 2; AAH24061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 49136 MW; AD883B5816D222AB CRC64;
MEPGPCSRPA EPGHCVSGPA GAGSAFPESP LSVAGAEPGN RPGTVAAVLP AGGCGERMGV
RTPKQFCRVL ERPLISYTLQ AMERVCWIKD IVVTVTGENM EAMRSIIQRY GHKRISLAEA
GATRHRSIFN GLKALAEDQP DCKLTKPEVV IIHDAVRPFV EEDILLRVVL AAKEHGAAGA
IRPLVSTVIS PSADGHLDHS LDRAKHRASE MPQAFLFDVI YEAYQQCSDF DLEFGTECLQ
LALKYCHRKA KLVEGPPALW KVTYKQDLCA AEAMIKEKIS QEICVVMNTK DEESVGHLLE
EALRKELNCM KITSTVMDHI GGDIRNFIEQ CYSFICVNVV SPDSQETRKL LRILEESSLP
LLYPVVVVLV HCFDFTSVPL AQKMESLVWI RGLAKEVKER NILLSGLLLN YSQDEQKLQE
SLGQSAAIIA ALVKERNSAL VGQLLVA
