ID A0A0G2JWT4_RAT Unreviewed; 432 AA.
AC A0A0G2JWT4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cytidine monophosphate-N-acetylneuraminic acid hydroxylase {ECO:0000256|ARBA:ARBA00015403};
DE EC=1.14.18.2 {ECO:0000256|ARBA:ARBA00011904};
DE AltName: Full=CMP-N-acetylneuraminate monooxygenase {ECO:0000256|ARBA:ARBA00033362};
DE AltName: Full=CMP-Neu5Ac hydroxylase {ECO:0000256|ARBA:ARBA00030460};
DE AltName: Full=CMP-NeuAc hydroxylase {ECO:0000256|ARBA:ARBA00029883};
GN Name=Cmahp {ECO:0000313|Ensembl:ENSRNOP00000070006.2,
GN ECO:0000313|RGD:1311930}; Synonyms=Cmah {ECO:0000313|RGD:1311930};
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 {ECO:0000313|Ensembl:ENSRNOP00000070006.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000070006.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070006.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000070006.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070006.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00003414}.
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:0000256|ARBA:ARBA00029339};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC {ECO:0000256|ARBA:ARBA00005141}.
CC -!- SIMILARITY: Belongs to the CMP-Neu5Ac hydroxylase family.
CC {ECO:0000256|ARBA:ARBA00010303}.
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DR AlphaFoldDB; A0A0G2JWT4; -.
DR STRING; 10116.ENSRNOP00000070006; -.
DR PaxDb; 10116-ENSRNOP00000018699; -.
DR Ensembl; ENSRNOT00000081105.2; ENSRNOP00000070006.2; ENSRNOG00000003094.8.
DR AGR; RGD:1311930; -.
DR RGD; 1311930; Cmahp.
DR VEuPathDB; HostDB:ENSRNOG00000003094; -.
DR eggNOG; ENOG502QR0M; Eukaryota.
DR GeneTree; ENSGT00390000010830; -.
DR InParanoid; A0A0G2JWT4; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000003094; Expressed in thymus and 16 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JWT4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030338; F:CMP-N-acetylneuraminate monooxygenase activity; ISO:RGD.
DR GO; GO:0046381; P:CMP-N-acetylneuraminate metabolic process; ISO:RGD.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:RGD.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR027033; Cnh.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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 SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ SEQUENCE 432 AA; 50815 MW; 6AE30E21A2BB782F CRC64;
MEVVEMDENN GLCLVELNPP NPWDSDPRSP EELAFGEVQI TYLTHACMDL KLGDKRMAFD
PWLIGPAFAR GWWLLHEPPS DWLERLCKAD LIYISHMHSD HLSYPTLKQL SQRRPDIPIY
VGDTERPVFW NLNHSGVQLT NINVVPFGIW QQVDKNLRFM ILMDGVHPEM DTCIIVEYKE
EWKAQFIKAE RRKLLNYKAQ LVKDLQPRIY CPFAGYFVEA HPSDKYIKET NTKNDPNQLN
NLIKKNSNVV TWTPRPGATL DLGRMLKDPT DSKGIVEPPE GTKIYKDSWD FEPYLKTLNS
SVRDSIFLHS SWIKEYFTWA GFKNYNLVVR MIETDEDFSP VPGGYDYLVD FLDLSFPKER
PSREHPYEEI RSRVDVIRHV VKNGLLWDDL YIGFQTRLQR DPDIYHHLFW NHFQIKLPLT
PPNWKLFLMR CG
//
