ID G1U4Y8_RABIT Unreviewed; 440 AA.
AC G1U4Y8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=D-ribitol-5-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00015848};
DE EC=2.7.7.40 {ECO:0000256|ARBA:ARBA00012488};
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein {ECO:0000256|ARBA:ARBA00031950};
DE AltName: Full=Isoprenoid synthase domain-containing protein {ECO:0000256|ARBA:ARBA00032606};
GN Name=CRPPA {ECO:0000313|Ensembl:ENSOCUP00000024464.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000024464.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000024464.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000024464.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000024464.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000831};
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:0000256|ARBA:ARBA00000413};
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:0000256|ARBA:ARBA00000888};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
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DR RefSeq; XP_002720898.1; XM_002720852.3.
DR AlphaFoldDB; G1U4Y8; -.
DR SMR; G1U4Y8; -.
DR STRING; 9986.ENSOCUP00000024464; -.
DR PaxDb; 9986-ENSOCUP00000024464; -.
DR Ensembl; ENSOCUT00000031868.2; ENSOCUP00000024464.2; ENSOCUG00000026591.3.
DR GeneID; 100337768; -.
DR KEGG; ocu:100337768; -.
DR CTD; 729920; -.
DR eggNOG; ENOG502QUUE; Eukaryota.
DR GeneTree; ENSGT00390000006412; -.
DR HOGENOM; CLU_033636_0_0_1; -.
DR InParanoid; G1U4Y8; -.
DR OrthoDB; 5405361at2759; -.
DR TreeFam; TF328415; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000026591; Expressed in testis and 15 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0035269; P:protein O-linked mannosylation; IEA:Ensembl.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR040635; ISPD_C.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43015; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43015:SF1; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF18706; ISPD_C; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 272..419
FT /note="D-ribitol-5-phosphate cytidylyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18706"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48202 MW; 7FA638B996AB6CC2 CRC64;
MEPGAAGDSR PAKPGPCVSG AALAASGEPG RRMPTVAAVL PAGGCGERMG VGTPKQFCPI
LERPLISYTL QALERVCWIK DIVVAVTAEN MGVMERIVQK YQHTRVSLAE AGVTRHRSIF
NGLKALAEDE PGCKLSKPQV VIIHDAVRPF VEEDILLQVA LAAEEHGAAG AIRPLVSTVI
SASADGCLDH SLERATHRAS EMPQAFLFDV IYEAYQQCSD YDLEFGTECL QLALKYSDTK
AKLVEGSPDL WKVTYKRDLS AAESIIKERI SQEICMVMDT KEDTERVGYL LEEVLKKELN
NVKIVSGVRS HGGRDIQQIT LPQCYNFVCV NGAASDFPET QQLLSVLEQS SLSILYPVVV
VLVYFLDFKS VPLGQKMESL MWIREFAKEV KKRNILLCGL LICYPQDEQT LQESLKQGAA
IIAALIKDRN PGLIGQLLVA
//
