NEUAA_DANRE
ID NEUAA_DANRE Reviewed; 430 AA.
AC Q0E671; B3DJV3; Q1RMB6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=N-acylneuraminate cytidylyltransferase A {ECO:0000305|PubMed:22351762};
DE EC=2.7.7.43 {ECO:0000269|PubMed:22351762};
DE AltName: Full=CMP-sialic acid synthetase 1 {ECO:0000303|PubMed:22351762};
GN Name=cmasa {ECO:0000312|ZFIN:ZDB-GENE-050420-277};
GN Synonyms=cmas {ECO:0000312|ZFIN:ZDB-GENE-050420-277},
GN cmas1 {ECO:0000303|PubMed:22351762};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AFC17880.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MOTIF, AND MUTAGENESIS OF
RP 9-LYS--LYS-13; 24-LYS--LYS-27 AND 184-PRO--ARG-190.
RX PubMed=22351762; DOI=10.1074/jbc.m111.327544;
RA Schaper W., Bentrop J., Ustinova J., Blume L., Kats E., Tiralongo J.,
RA Weinhold B., Bastmeyer M., Munster-Kuhnel A.K.;
RT "Identification and biochemical characterization of two functional CMP-
RT sialic acid synthetases in Danio rerio.";
RL J. Biol. Chem. 287:13239-13248(2012).
RN [2] {ECO:0000312|EMBL:CAK18993.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lehmann F.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000312|EMBL:AAI15047.1, ECO:0000312|EMBL:AAI63617.1, ECO:0000312|EMBL:AAI65783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:AAI15047.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc)
CC to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a
CC substrate required for the addition of sialic acid. Also has activity
CC towards N-glycolylneuraminic acid (Neu5Gc). Has weak activity towards
CC 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN).
CC {ECO:0000269|PubMed:22351762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate +
CC diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43;
CC Evidence={ECO:0000269|PubMed:22351762};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism.
CC {ECO:0000269|PubMed:22351762}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22351762}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22351762}.
CC -!- DEVELOPMENTAL STAGE: Detected in the axial mesoderm at 9 hours post-
CC fertilization (hpf). Expressed in the central nervous system, somites,
CC notochord and developing pronephric duct at 18 hpf. At later stages
CC (48-72 hpf) expression decreases in the trunk but persists in the
CC central nervous system, and is also found in liver and kidney
CC primordia. {ECO:0000269|PubMed:22351762}.
CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI15047.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI63617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI65783.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown origin at N terminus.; Evidence={ECO:0000305};
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DR EMBL; BX571719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JQ015186; AFC17880.1; -; mRNA.
DR EMBL; AM262833; CAK18993.1; -; mRNA.
DR EMBL; BC115046; AAI15047.1; ALT_SEQ; mRNA.
DR EMBL; BC163617; AAI63617.1; ALT_INIT; mRNA.
DR EMBL; BC165783; AAI65783.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001035342.2; NM_001040252.2.
DR AlphaFoldDB; Q0E671; -.
DR SMR; Q0E671; -.
DR STRING; 7955.ENSDARP00000074418; -.
DR PaxDb; Q0E671; -.
DR Ensembl; ENSDART00000158094; ENSDARP00000134059; ENSDARG00000057334.
DR GeneID; 561018; -.
DR KEGG; dre:561018; -.
DR CTD; 561018; -.
DR ZFIN; ZDB-GENE-050420-277; cmasa.
DR eggNOG; ENOG502QQH3; Eukaryota.
DR GeneTree; ENSGT00390000004237; -.
DR InParanoid; Q0E671; -.
DR OrthoDB; 781897at2759; -.
DR PhylomeDB; Q0E671; -.
DR TreeFam; TF324840; -.
DR BRENDA; 2.7.7.43; 928.
DR Reactome; R-DRE-4085001; Sialic acid metabolism.
DR UniPathway; UPA00628; -.
DR PRO; PR:Q0E671; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000057334; Expressed in mature ovarian follicle and 27 other tissues.
DR ExpressionAtlas; Q0E671; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IDA:ZFIN.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..430
FT /note="N-acylneuraminate cytidylyltransferase A"
FT /id="PRO_0000438685"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..27
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22351762"
FT COMPBIAS 6..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99KK2"
FT MUTAGEN 9..13
FT /note="Missing: Fails to localize to the nucleus. No effect
FT on catalytic activity."
FT /evidence="ECO:0000269|PubMed:22351762"
FT MUTAGEN 24..27
FT /note="Missing: Fails to localize to the nucleus. No effect
FT on catalytic activity."
FT /evidence="ECO:0000269|PubMed:22351762"
FT MUTAGEN 184..190
FT /note="Missing: Abolishes catalytic activity. No effect on
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:22351762"
FT CONFLICT 322
FT /note="R -> K (in Ref. 4; AAI15047/AAI65783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 48227 MW; 6449AF3D6C81C2EC CRC64;
MDAVNENGKR AMKDDSHGNS TSPKRRKSRH ISALILARGG SKGIPLKNIK MLAGVPLIGW
VIRAAVDSNV FNSVWVSTDH EEIAKVALAW GAKVHKRSPE VSQDSSSSLD TIREFSRQHR
EVDVICNIQA TSPCLHPKHL TEAVELITKQ GYDSVFSVVR RHNFRWKEVE KGGDCSTEPM
NLNPACRPRR QDWSGELCEN GSFYFAKKEL IEQGLLQGGK KTYYEMKPEY SVDIDVDIDW
PVAEQRVLRF GYFGKDKPEV VRLLLCNVSG CLTDGQIYTS ASGEEMVSIN IRDQIGISML
KKEGVKVILL ETYPIAKALA VRLSERMGCP LLHHMDDKLK EVERIMVEEK LEWKEVAYLG
NDEADVKCLE LAGLSGVPVD APTVALNHTK YTCHNAAGHG AVREFAEHIL LLKKKAKSQM
EQDRICRDAF
