ID CMAH_MOUSE Reviewed; 577 AA.
AC Q61419; Q7TMR9; Q8JZM9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 166.
DE RecName: Full=Cytidine monophosphate-N-acetylneuraminic acid hydroxylase;
DE Short=CMP-N-acetylneuraminic acid hydroxylase;
DE EC=1.14.18.2;
DE AltName: Full=CMP-N-acetylneuraminate monooxygenase;
DE AltName: Full=CMP-Neu5Ac hydroxylase;
DE AltName: Full=CMP-NeuAc hydroxylase;
DE Flags: Precursor;
GN Name=Cmah;
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 [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 5-33; 504-524
RP AND 543-561, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7608218; DOI=10.1074/jbc.270.27.16458;
RA Kawano T., Koyama S., Takematsu H., Kozutsumi Y., Kawasaki H.,
RA Kawashima S., Kawasaki T., Suzuki A.;
RT "Molecular cloning of cytidine monophospho-N-acetylneuraminic acid
RT hydroxylase.";
RL J. Biol. Chem. 270:16458-16463(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Koyama S., Takematsu H., Takasaki-Nishigaki M., Kawasaki T., Suzuki A.,
RA Kozutsumi Y.;
RT "Isolation and analysis of the mouse gene encoding CMP-N-acetylneuraminic
RT acid hydroxylase.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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).
RN [5]
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8132639; DOI=10.1016/s0021-9258(17)37071-0;
RA Kawano T., Kozutsumi Y., Kawasaki T., Suzuki A.;
RT "Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates.
RT Purification and characterization of the key enzyme of the cytidine
RT monophospho-N-acetylneuraminic acid hydroxylation system.";
RL J. Biol. Chem. 269:9024-9029(1994).
RN [6]
RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=8781965; DOI=10.1007/bf00731467;
RA Koyama S., Yamaji T., Takematsu H., Kawano T., Kozutsumi Y., Suzuki A.,
RA Kawasaki T.;
RT "A naturally occurring 46-amino acid deletion of cytidine monophospho-N-
RT acetylneuraminic acid hydroxylase leads to a change in the intracellular
RT distribution of the protein.";
RL Glycoconj. J. 13:353-358(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22692205; DOI=10.1074/jbc.m112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating
RT the intracellular fate of the non-human sialic acid N-glycolylneuraminic
RT acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
CC -!- FUNCTION: Sialic acids are components of carbohydrate chains of
CC glycoconjugates and are involved in cell-cell recognition and cell-
CC pathogen interactions. Catalyzes the conversion of CMP-N-
CC acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative
CC CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly
CC expressed at the surface of many cells. {ECO:0000269|PubMed:22692205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = CMP-N-glycoloyl-beta-neuraminate + 2 Fe(III)-[cytochrome
CC b5] + H2O; Xref=Rhea:RHEA:16145, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:58376; EC=1.14.18.2;
CC Evidence={ECO:0000269|PubMed:22692205};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000305|PubMed:8132639};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000305|PubMed:8132639};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for CMP-NeuAc {ECO:0000269|PubMed:8132639};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7608218,
CC ECO:0000269|PubMed:8781965}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61419-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61419-2; Sequence=VSP_013769;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, except in brain.
CC {ECO:0000269|PubMed:7608218}.
CC -!- DISRUPTION PHENOTYPE: Mice do not synthesize N-glycolylneuraminic acid
CC (Neu5Gc). {ECO:0000269|PubMed:22692205}.
CC -!- MISCELLANEOUS: [Isoform 2]: Inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB91361.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB91362.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB91553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D21826; BAA04850.1; -; mRNA.
DR EMBL; AB061276; BAB91361.1; ALT_INIT; mRNA.
DR EMBL; AB061277; BAB91362.1; ALT_INIT; mRNA.
DR EMBL; AB061346; BAB91553.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL589744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055079; AAH55079.1; -; mRNA.
DR CCDS; CCDS26376.1; -. [Q61419-1]
DR PIR; A57469; A57469.
DR RefSeq; NP_001104580.1; NM_001111110.2. [Q61419-1]
DR RefSeq; NP_001271448.1; NM_001284519.1. [Q61419-1]
DR RefSeq; NP_001271449.1; NM_001284520.1. [Q61419-2]
DR RefSeq; NP_031743.3; NM_007717.5. [Q61419-1]
DR AlphaFoldDB; Q61419; -.
DR STRING; 10090.ENSMUSP00000106021; -.
DR iPTMnet; Q61419; -.
DR PhosphoSitePlus; Q61419; -.
DR EPD; Q61419; -.
DR jPOST; Q61419; -.
DR MaxQB; Q61419; -.
DR PaxDb; 10090-ENSMUSP00000129007; -.
DR ProteomicsDB; 283635; -. [Q61419-1]
DR ProteomicsDB; 283636; -. [Q61419-2]
DR DNASU; 12763; -.
DR Ensembl; ENSMUST00000050859.13; ENSMUSP00000061045.6; ENSMUSG00000016756.18. [Q61419-1]
DR Ensembl; ENSMUST00000110391.4; ENSMUSP00000106021.3; ENSMUSG00000016756.18. [Q61419-1]
DR Ensembl; ENSMUST00000167746.8; ENSMUSP00000129007.2; ENSMUSG00000016756.18. [Q61419-1]
DR Ensembl; ENSMUST00000224657.2; ENSMUSP00000153495.2; ENSMUSG00000016756.18. [Q61419-1]
DR Ensembl; ENSMUST00000224953.2; ENSMUSP00000153652.2; ENSMUSG00000016756.18. [Q61419-1]
DR GeneID; 12763; -.
DR KEGG; mmu:12763; -.
DR UCSC; uc007pvq.3; mouse. [Q61419-1]
DR UCSC; uc011yxn.2; mouse. [Q61419-2]
DR AGR; MGI:103227; -.
DR CTD; 12763; -.
DR MGI; MGI:103227; Cmah.
DR VEuPathDB; HostDB:ENSMUSG00000016756; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR GeneTree; ENSGT00390000010830; -.
DR HOGENOM; CLU_034056_0_0_1; -.
DR InParanoid; Q61419; -.
DR OMA; WKSFLMC; -.
DR PhylomeDB; Q61419; -.
DR TreeFam; TF331273; -.
DR BioCyc; MetaCyc:MONOMER-14525; -.
DR SABIO-RK; Q61419; -.
DR UniPathway; UPA00628; -.
DR BioGRID-ORCS; 12763; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Cmah; mouse.
DR PRO; PR:Q61419; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61419; Protein.
DR Bgee; ENSMUSG00000016756; Expressed in conjunctival fornix and 189 other cell types or tissues.
DR ExpressionAtlas; Q61419; baseline and differential.
DR Genevisible; Q61419; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046381; P:CMP-N-acetylneuraminate metabolic process; IDA:MGI.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:MGI.
DR CDD; cd03473; Rieske_CMP_Neu5Ac_hydrolase_N; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR037339; CMP-Neu5Ac_hydroxylase_Rieske.
DR InterPro; IPR027033; Cnh.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR46522; CYTIDINE MONOPHOSPHATE-N-ACETYLNEURAMINIC ACID HYDROXYLASE; 1.
DR PANTHER; PTHR46522:SF1; CYTIDINE MONOPHOSPHATE-N-ACETYLNEURAMINIC ACID HYDROXYLASE; 1.
DR Pfam; PF13483; Lactamase_B_3; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Electron transport; Endoplasmic reticulum; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome; Transport.
FT PROPEP 1..4
FT /evidence="ECO:0000305|PubMed:7608218"
FT /id="PRO_0000030699"
FT CHAIN 5..577
FT /note="Cytidine monophosphate-N-acetylneuraminic acid
FT hydroxylase"
FT /id="PRO_0000030700"
FT DOMAIN 14..112
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 54
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT VAR_SEQ 279..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013769"
FT CONFLICT 515
FT /note="I -> T (in Ref. 4; AAH55079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 66936 MW; 6808ECC75E4F6B78 CRC64;
MMDRKQTAET LLTLSPAEVA NLKEGINFFR NKTTGKEYIL YKEKDHLKAC KNLCKHQGGL
FMKDIEDLDG RSVKCTKHNW KLDVSTMKYI NPPGSFCQDE LVIEMDENNG LSLVELNPPN
PWDSDPRSPE ELAFGEVQIT YLTHACMDLK LGDKRMVFDP WLIGPAFARG WWLLHEPPSD
WLERLCKADL IYISHMHSDH LSYPTLKQLS QRRPDIPIYV GDTERPVFWN LDQSGVGLTN
INVVPFGIWQ QVDKSLRFMI LMDGVHPEMD TCIIVEYKGH KILNTVDCTR PNGGRLPEKV
ALMMSDFAGG ASGFPMTFSG GKFTEEWKAQ FIKAERRKLL NYKAQLVKDL QPRIYCPFAG
YFVESHPSDK YIKETNTKND PNQLNNLIRK NSDVVTWTPR PGAVLDLGRM LKDPTDSKGI
VEPPEGTKIY KDSWDFGPYL EILNSAVRDE IFCHSSWIKE YFTWAGFKNY NLVVRMIETD
EDFSPFPGGY DYLVDFLDLS FPKERPSREH PYEEIHSRVD VIRYVVKNGL LWDDLYIGFQ
TRLLRDPDIY HHLFWNHFQI KLPLTPPNWK SFLMHCD
//
