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ISPD_HUMAN
ID   ISPD_HUMAN              Reviewed;         451 AA.
AC   A4D126; A8MU35; H9KVB2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=D-ribitol-5-phosphate cytidylyltransferase {ECO:0000305};
DE            EC=2.7.7.40 {ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27130732};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein;
DE   AltName: Full=Isoprenoid synthase domain-containing protein {ECO:0000312|HGNC:HGNC:37276};
DE            Short=hISPD {ECO:0000303|PubMed:26687144};
GN   Name=CRPPA {ECO:0000312|HGNC:HGNC:37276};
GN   Synonyms=ISPD {ECO:0000312|HGNC:HGNC:37276};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   FUNCTION, VARIANT MDDGA7 ILE-93 DEL, AND TISSUE SPECIFICITY.
RX   PubMed=22522420; DOI=10.1038/ng.2252;
RA   Willer T., Lee H., Lommel M., Yoshida-Moriguchi T., de Bernabe D.B.,
RA   Venzke D., Cirak S., Schachter H., Vajsar J., Voit T., Muntoni F.,
RA   Loder A.S., Dobyns W.B., Winder T.L., Strahl S., Mathews K.D., Nelson S.F.,
RA   Moore S.A., Campbell K.P.;
RT   "ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and
RT   cause Walker-Warburg syndrome.";
RL   Nat. Genet. 44:575-580(2012).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=26923585; DOI=10.1016/j.celrep.2016.02.017;
RA   Kanagawa M., Kobayashi K., Tajiri M., Manya H., Kuga A., Yamaguchi Y.,
RA   Akasaka-Manya K., Furukawa J.I., Mizuno M., Kawakami H., Shinohara Y.,
RA   Wada Y., Endo T., Toda T.;
RT   "Identification of a Post-translational Modification with Ribitol-Phosphate
RT   and Its Defect in Muscular Dystrophy.";
RL   Cell Rep. 14:2209-2223(2016).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=27130732; DOI=10.7554/elife.14473;
RA   Praissman J.L., Willer T., Sheikh M.O., Toi A., Chitayat D., Lin Y.Y.,
RA   Lee H., Stalnaker S.H., Wang S., Prabhakar P.K., Nelson S.F., Stemple D.L.,
RA   Moore S.A., Moremen K.W., Campbell K.P., Wells L.;
RT   "The functional O-mannose glycan on alpha-dystroglycan contains a phospho-
RT   ribitol primed for matriglycan addition.";
RL   Elife 5:0-0(2016).
RN   [6]
RP   FUNCTION.
RX   PubMed=27601598; DOI=10.1074/mcp.m116.062729;
RA   Yagi H., Kuo C.W., Obayashi T., Ninagawa S., Khoo K.H., Kato K.;
RT   "Direct mapping of additional modifications on phosphorylated O-glycans of
RT   alpha-dystroglycan by mass spectrometry analysis in conjunction with
RT   knocking out of causative genes for dystroglycanopathy.";
RL   Mol. Cell. Proteomics 15:3424-3434(2016).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 43-451, FUNCTION, CATALYTIC
RP   ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=26687144; DOI=10.1016/j.chembiol.2015.10.014;
RA   Riemersma M., Froese D.S., van Tol W., Engelke U.F., Kopec J.,
RA   van Scherpenzeel M., Ashikov A., Krojer T., von Delft F., Tessari M.,
RA   Buczkowska A., Swiezewska E., Jae L.T., Brummelkamp T.R., Manya H.,
RA   Endo T., van Bokhoven H., Yue W.W., Lefeber D.J.;
RT   "Human ISPD is a cytidyltransferase required for dystroglycan O-
RT   mannosylation.";
RL   Chem. Biol. 22:1643-1652(2015).
RN   [8]
RP   VARIANTS MDDGA7 ASN-156; ARG-213; HIS-226 AND ILE-238.
RX   PubMed=23217329; DOI=10.1016/j.ajhg.2012.10.009;
RA   Vuillaumier-Barrot S., Bouchet-Seraphin C., Chelbi M., Devisme L.,
RA   Quentin S., Gazal S., Laquerriere A., Fallet-Bianco C., Loget P., Odent S.,
RA   Carles D., Bazin A., Aziza J., Clemenson A., Guimiot F., Bonniere M.,
RA   Monnot S., Bole-Feysot C., Bernard J.P., Loeuillet L., Gonzales M.,
RA   Socha K., Grandchamp B., Attie-Bitach T., Encha-Razavi F., Seta N.;
RT   "Identification of mutations in TMEM5 and ISPD as a cause of severe
RT   cobblestone lissencephaly.";
RL   Am. J. Hum. Genet. 91:1135-1143(2012).
RN   [9]
RP   VARIANTS MDDGA7 PRO-122; HIS-126 AND ASP-216, AND FUNCTION.
RX   PubMed=22522421; DOI=10.1038/ng.2253;
RA   Roscioli T., Kamsteeg E.J., Buysse K., Maystadt I., van Reeuwijk J.,
RA   van den Elzen C., van Beusekom E., Riemersma M., Pfundt R., Vissers L.E.,
RA   Schraders M., Altunoglu U., Buckley M.F., Brunner H.G., Grisart B.,
RA   Zhou H., Veltman J.A., Gilissen C., Mancini G.M., Delree P.,
RA   Willemsen M.A., Ramadza D.P., Chitayat D., Bennett C., Sheridan E.,
RA   Peeters E.A., Tan-Sindhunata G.M., de Die-Smulders C.E., Devriendt K.,
RA   Kayserili H., El-Hashash O.A., Stemple D.L., Lefeber D.J., Lin Y.Y.,
RA   van Bokhoven H.;
RT   "Mutations in ISPD cause Walker-Warburg syndrome and defective
RT   glycosylation of alpha-dystroglycan.";
RL   Nat. Genet. 44:581-585(2012).
RN   [10]
RP   VARIANTS MDDGC7 THR-53; LEU-149; 215-GLN--ALA-451 DEL; CYS-226; VAL-372 DEL
RP   AND 395-ARG--ALA-451 DEL, AND VARIANT MDDGA7 HIS-126.
RX   PubMed=23288328; DOI=10.1093/brain/aws312;
RG   UK10K Consortium;
RA   Cirak S., Foley A.R., Herrmann R., Willer T., Yau S., Stevens E.,
RA   Torelli S., Brodd L., Kamynina A., Vondracek P., Roper H., Longman C.,
RA   Korinthenberg R., Marrosu G., Nuernberg P., Michele D.E., Plagnol V.,
RA   Hurles M., Moore S.A., Sewry C.A., Campbell K.P., Voit T., Muntoni F.;
RT   "ISPD gene mutations are a common cause of congenital and limb-girdle
RT   muscular dystrophies.";
RL   Brain 136:269-281(2013).
RN   [11]
RP   VARIANT MDDGA7 HIS-205.
RX   PubMed=24120487; DOI=10.1016/j.ejmg.2013.09.014;
RA   Czeschik J.C., Hehr U., Hartmann B., Luedecke H.J., Rosenbaum T.,
RA   Schweiger B., Wieczorek D.;
RT   "160 kb deletion in ISPD unmasking a recessive mutation in a patient with
RT   Walker-Warburg syndrome.";
RL   Eur. J. Med. Genet. 56:689-694(2013).
RN   [12]
RP   VARIANTS MDDGC7 ALA-54 AND VAL-372 DEL, INVOLVEMENT IN MDDGC7, AND
RP   CHARACTERIZATION OF VARIANTS MDDGC7 ALA-54 AND VAL-372 DEL.
RX   PubMed=23390185; DOI=10.1212/wnl.0b013e3182840cbc;
RA   Tasca G., Moro F., Aiello C., Cassandrini D., Fiorillo C., Bertini E.,
RA   Bruno C., Santorelli F.M., Ricci E.;
RT   "Limb-girdle muscular dystrophy with alpha-dystroglycan deficiency and
RT   mutations in the ISPD gene.";
RL   Neurology 80:963-965(2013).
RN   [13]
RP   VARIANT MDDGC7 VAL-372 DEL.
RX   PubMed=27234031; DOI=10.1111/cge.12810;
RA   Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A.,
RA   Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K.,
RA   Kariminejad A., Najmabadi H.;
RT   "Improved diagnostic yield of neuromuscular disorders applying clinical
RT   exome sequencing in patients arising from a consanguineous population.";
RL   Clin. Genet. 91:386-402(2017).
CC   -!- FUNCTION: Cytidylyltransferase required for protein O-linked
CC       mannosylation (PubMed:22522420, PubMed:27130732, PubMed:27601598,
CC       PubMed:26687144, PubMed:22522421, PubMed:26923585). Catalyzes the
CC       formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate
CC       (PubMed:27130732, PubMed:26687144, PubMed:26923585). CDP-ribitol is a
CC       substrate of FKTN during the biosynthesis of the phosphorylated O-
CC       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 (PubMed:27130732, PubMed:26687144, PubMed:26923585).
CC       Shows activity toward other pentose phosphate sugars and mediates
CC       formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-
CC       phosphate or ribose-5-phosphate, respectively (PubMed:26687144). Not
CC       Involved in dolichol production (PubMed:26687144).
CC       {ECO:0000269|PubMed:22522420, ECO:0000269|PubMed:22522421,
CC       ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585,
CC       ECO:0000269|PubMed:27130732, ECO:0000269|PubMed:27601598}.
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:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585,
CC         ECO:0000269|PubMed:27130732};
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:0000269|PubMed:26687144,
CC         ECO:0000269|PubMed:27130732};
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:0000269|PubMed:26687144};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:26687144, ECO:0000269|PubMed:26923585,
CC       ECO:0000269|PubMed:27130732}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26687144}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26687144}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A4D126-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A4D126-2; Sequence=VSP_044044;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high expression in
CC       brain. {ECO:0000269|PubMed:22522420}.
CC   -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC       and eye anomalies A7 (MDDGA7) [MIM:614643]: An autosomal recessive
CC       disorder characterized by congenital muscular dystrophy associated with
CC       cobblestone lissencephaly and other brain anomalies, eye malformations,
CC       profound intellectual disability, and death usually in the first years
CC       of life. Included diseases are the more severe Walker-Warburg syndrome
CC       and the slightly less severe muscle-eye-brain disease.
CC       {ECO:0000269|PubMed:22522420, ECO:0000269|PubMed:22522421,
CC       ECO:0000269|PubMed:23217329, ECO:0000269|PubMed:23288328,
CC       ECO:0000269|PubMed:24120487}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C7 (MDDGC7)
CC       [MIM:616052]: A form of muscular dystrophy resulting from defective
CC       glycosylation of alpha-dystroglycan, and characterized by a limb-girdle
CC       phenotype with muscular weakness apparent after ambulation is achieved.
CC       MDDGC7 individuals do not show epilepsy, intellectual disability,
CC       structural eye/brain abnormalities, or white matter changes.
CC       {ECO:0000269|PubMed:23288328, ECO:0000269|PubMed:23390185,
CC       ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL24288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC006035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236948; EAL24288.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471073; EAW93668.1; -; Genomic_DNA.
DR   RefSeq; NP_001094887.1; NM_001101417.3. [A4D126-2]
DR   RefSeq; NP_001094896.1; NM_001101426.3. [A4D126-1]
DR   PDB; 4CVH; X-ray; 2.39 A; A=43-451.
DR   PDBsum; 4CVH; -.
DR   AlphaFoldDB; A4D126; -.
DR   SMR; A4D126; -.
DR   BioGRID; 610311; 1.
DR   IntAct; A4D126; 2.
DR   STRING; 9606.ENSP00000385478; -.
DR   iPTMnet; A4D126; -.
DR   PhosphoSitePlus; A4D126; -.
DR   BioMuta; ISPD; -.
DR   MassIVE; A4D126; -.
DR   PaxDb; A4D126; -.
DR   PeptideAtlas; A4D126; -.
DR   PRIDE; A4D126; -.
DR   ProteomicsDB; 602; -. [A4D126-1]
DR   ProteomicsDB; 603; -. [A4D126-2]
DR   Antibodypedia; 43951; 103 antibodies from 15 providers.
DR   DNASU; 729920; -.
DR   Ensembl; ENST00000399310.3; ENSP00000382249.3; ENSG00000214960.11. [A4D126-2]
DR   Ensembl; ENST00000407010.7; ENSP00000385478.2; ENSG00000214960.11. [A4D126-1]
DR   GeneID; 729920; -.
DR   KEGG; hsa:729920; -.
DR   MANE-Select; ENST00000407010.7; ENSP00000385478.2; NM_001101426.4; NP_001094896.1.
DR   UCSC; uc010ktx.2; human. [A4D126-1]
DR   CTD; 729920; -.
DR   DisGeNET; 729920; -.
DR   GeneCards; CRPPA; -.
DR   HGNC; HGNC:37276; CRPPA.
DR   HPA; ENSG00000214960; Tissue enriched (choroid).
DR   MalaCards; CRPPA; -.
DR   MIM; 614631; gene.
DR   MIM; 614643; phenotype.
DR   MIM; 616052; phenotype.
DR   neXtProt; NX_A4D126; -.
DR   OpenTargets; ENSG00000214960; -.
DR   Orphanet; 370980; Congenital muscular dystrophy without intellectual disability.
DR   Orphanet; 352479; ISPD-related limb-girdle muscular dystrophy R20.
DR   Orphanet; 899; Walker-Warburg syndrome.
DR   PharmGKB; PA165618128; -.
DR   VEuPathDB; HostDB:ENSG00000214960; -.
DR   eggNOG; ENOG502QUUE; Eukaryota.
DR   GeneTree; ENSGT00390000006412; -.
DR   HOGENOM; CLU_033636_0_0_1; -.
DR   InParanoid; A4D126; -.
DR   OMA; LKEWNFI; -.
DR   OrthoDB; 1356473at2759; -.
DR   PhylomeDB; A4D126; -.
DR   TreeFam; TF328415; -.
DR   BioCyc; MetaCyc:MON66-43822; -.
DR   BRENDA; 2.7.7.40; 2681.
DR   PathwayCommons; A4D126; -.
DR   SignaLink; A4D126; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 729920; 5 hits in 244 CRISPR screens.
DR   ChiTaRS; ISPD; human.
DR   GenomeRNAi; 729920; -.
DR   Pharos; A4D126; Tbio.
DR   PRO; PR:A4D126; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; A4D126; protein.
DR   Bgee; ENSG00000214960; Expressed in corpus callosum and 111 other tissues.
DR   ExpressionAtlas; A4D126; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070567; F:cytidylyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; IMP: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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Congenital muscular dystrophy;
KW   Cytoplasm; Disease variant; Dystroglycanopathy;
KW   Limb-girdle muscular dystrophy; Lissencephaly; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..451
FT                   /note="D-ribitol-5-phosphate cytidylyltransferase"
FT                   /id="PRO_0000343697"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            59
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q46893"
FT   SITE            66
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q46893"
FT   SITE            205
FT                   /note="Positions substrate for the nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:Q46893"
FT   SITE            263
FT                   /note="Positions substrate for the nucleophilic attack"
FT                   /evidence="ECO:0000250|UniProtKB:Q46893"
FT   VAR_SEQ         179..228
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044044"
FT   VARIANT         53
FT                   /note="A -> T (in MDDGC7)"
FT                   /evidence="ECO:0000269|PubMed:23288328"
FT                   /id="VAR_078970"
FT   VARIANT         54
FT                   /note="G -> A (in MDDGC7; decreased alpha-dystroglycan
FT                   glycosylation; dbSNP:rs587777797)"
FT                   /evidence="ECO:0000269|PubMed:23390185"
FT                   /id="VAR_071955"
FT   VARIANT         93
FT                   /note="Missing (in MDDGA7; dbSNP:rs397515398)"
FT                   /evidence="ECO:0000269|PubMed:22522420"
FT                   /id="VAR_069740"
FT   VARIANT         122
FT                   /note="A -> P (in MDDGA7; dbSNP:rs387907162)"
FT                   /evidence="ECO:0000269|PubMed:22522421"
FT                   /id="VAR_068101"
FT   VARIANT         126
FT                   /note="R -> H (in MDDGA7; also found in a patient with an
FT                   atypical phenotype presenting with limb-girdle muscular
FT                   dystrophy, ocular features and cerebellar involvement;
FT                   dbSNP:rs752817129)"
FT                   /evidence="ECO:0000269|PubMed:22522421,
FT                   ECO:0000269|PubMed:23288328"
FT                   /id="VAR_068102"
FT   VARIANT         149
FT                   /note="P -> L (in MDDGC7; atypical form presenting with
FT                   congenital muscular dystrophy; dbSNP:rs369219851)"
FT                   /evidence="ECO:0000269|PubMed:23288328"
FT                   /id="VAR_078948"
FT   VARIANT         156
FT                   /note="D -> N (in MDDGA7; dbSNP:rs397514547)"
FT                   /evidence="ECO:0000269|PubMed:23217329"
FT                   /id="VAR_069741"
FT   VARIANT         205
FT                   /note="R -> H (in MDDGA7; dbSNP:rs566179705)"
FT                   /evidence="ECO:0000269|PubMed:24120487"
FT                   /id="VAR_078949"
FT   VARIANT         213
FT                   /note="M -> R (in MDDGA7; dbSNP:rs397515408)"
FT                   /evidence="ECO:0000269|PubMed:23217329"
FT                   /id="VAR_069742"
FT   VARIANT         215..451
FT                   /note="Missing (in MDDGC7; atypical form presenting with
FT                   congenital muscular dystrophy)"
FT                   /evidence="ECO:0000269|PubMed:23288328"
FT                   /id="VAR_078950"
FT   VARIANT         216
FT                   /note="A -> D (in MDDGA7; dbSNP:rs387907160)"
FT                   /evidence="ECO:0000269|PubMed:22522421"
FT                   /id="VAR_068103"
FT   VARIANT         226
FT                   /note="Y -> C (in MDDGC7; atypical form with learning
FT                   difficulties; dbSNP:rs1289931198)"
FT                   /evidence="ECO:0000269|PubMed:23288328"
FT                   /id="VAR_078951"
FT   VARIANT         226
FT                   /note="Y -> H (in MDDGA7; dbSNP:rs1282788711)"
FT                   /evidence="ECO:0000269|PubMed:23217329"
FT                   /id="VAR_069743"
FT   VARIANT         238
FT                   /note="T -> I (in MDDGA7; dbSNP:rs397515409)"
FT                   /evidence="ECO:0000269|PubMed:23217329"
FT                   /id="VAR_069744"
FT   VARIANT         372
FT                   /note="Missing (in MDDGC7; decreased alpha-dystroglycan
FT                   glycosylation; dbSNP:rs587777798)"
FT                   /evidence="ECO:0000269|PubMed:23288328,
FT                   ECO:0000269|PubMed:23390185, ECO:0000269|PubMed:27234031"
FT                   /id="VAR_071956"
FT   VARIANT         395..451
FT                   /note="Missing (in MDDGC7)"
FT                   /evidence="ECO:0000269|PubMed:23288328"
FT                   /id="VAR_078952"
FT   STRAND          45..52
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           76..85
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           126..137
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           164..177
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          178..185
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          209..218
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           219..228
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           231..236
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           240..248
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          253..256
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           267..280
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          283..289
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           293..309
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          314..319
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          337..344
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           349..360
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           363..366
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          369..377
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          380..382
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           385..391
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           394..402
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   TURN            403..405
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          406..414
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           419..439
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   HELIX           442..444
FT                   /evidence="ECO:0007829|PDB:4CVH"
FT   STRAND          448..450
FT                   /evidence="ECO:0007829|PDB:4CVH"
SQ   SEQUENCE   451 AA;  49873 MW;  988B9D1CFE98935C CRC64;
     MEAGPPGSAR PAEPGPCLSG QRGADHTASA SLQSVAGTEP GRHPQAVAAV LPAGGCGERM
     GVPTPKQFCP ILERPLISYT LQALERVCWI KDIVVAVTGE NMEVMKSIIQ KYQHKRISLV
     EAGVTRHRSI FNGLKALAED QINSKLSKPE VVIIHDAVRP FVEEGVLLKV VTAAKEHGAA
     GAIRPLVSTV VSPSADGCLD YSLERARHRA SEMPQAFLFD VIYEAYQQCS DYDLEFGTEC
     LQLALKYCCT KAKLVEGSPD LWKVTYKRDL YAAESIIKER ISQEICVVMD TEEDNKHVGH
     LLEEVLKSEL NHVKVTSEAL GHAGRHLQQI ILDQCYNFVC VNVTTSDFQE TQKLLSMLEE
     SSLCILYPVV VVSVHFLDFK LVPPSQKMEN LMQIREFAKE VKERNILLYG LLISYPQDDQ
     KLQESLRQGA IIIASLIKER NSGLIGQLLI A
 
 
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