NANP_MOUSE
ID NANP_MOUSE Reviewed; 248 AA.
AC Q9CPT3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-acylneuraminate-9-phosphatase;
DE EC=3.1.3.29;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 4;
DE AltName: Full=Neu5Ac-9-Pase;
GN Name=Nanp; Synonyms=Hdhd4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of protein C20orf147 homolog (17391249) from Mus
RT musculus at 1.90 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylneuraminate 9-phosphate + H2O = an N-acylneuraminate
CC + phosphate; Xref=Rhea:RHEA:13057, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57537, ChEBI:CHEBI:60073; EC=3.1.3.29;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate and calcium. {ECO:0000250}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NANP family.
CC {ECO:0000305}.
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DR EMBL; AK005566; BAB24126.1; -; mRNA.
DR EMBL; AK021344; BAB32381.1; -; mRNA.
DR EMBL; BC018527; AAH18527.1; -; mRNA.
DR EMBL; BC083086; AAH83086.1; -; mRNA.
DR CCDS; CCDS16864.1; -.
DR RefSeq; NP_080362.1; NM_026086.2.
DR PDB; 2GFH; X-ray; 1.90 A; A=1-248.
DR PDBsum; 2GFH; -.
DR AlphaFoldDB; Q9CPT3; -.
DR SMR; Q9CPT3; -.
DR BioGRID; 212095; 1.
DR STRING; 10090.ENSMUSP00000063895; -.
DR iPTMnet; Q9CPT3; -.
DR PhosphoSitePlus; Q9CPT3; -.
DR EPD; Q9CPT3; -.
DR MaxQB; Q9CPT3; -.
DR PaxDb; Q9CPT3; -.
DR PeptideAtlas; Q9CPT3; -.
DR PRIDE; Q9CPT3; -.
DR ProteomicsDB; 252765; -.
DR Antibodypedia; 10091; 378 antibodies from 27 providers.
DR DNASU; 67311; -.
DR Ensembl; ENSMUST00000066640; ENSMUSP00000063895; ENSMUSG00000053916.
DR GeneID; 67311; -.
DR KEGG; mmu:67311; -.
DR UCSC; uc008muv.2; mouse.
DR CTD; 140838; -.
DR MGI; MGI:1914561; Nanp.
DR VEuPathDB; HostDB:ENSMUSG00000053916; -.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00390000003094; -.
DR HOGENOM; CLU_045011_8_2_1; -.
DR InParanoid; Q9CPT3; -.
DR OMA; WLKLRYR; -.
DR OrthoDB; 1113437at2759; -.
DR PhylomeDB; Q9CPT3; -.
DR TreeFam; TF324589; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR UniPathway; UPA00630; -.
DR BioGRID-ORCS; 67311; 1 hit in 35 CRISPR screens.
DR ChiTaRS; Nanp; mouse.
DR EvolutionaryTrace; Q9CPT3; -.
DR PRO; PR:Q9CPT3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CPT3; protein.
DR Bgee; ENSMUSG00000053916; Expressed in lobe of liver and 62 other tissues.
DR Genevisible; Q9CPT3; MM.
DR GO; GO:0050124; F:N-acylneuraminate-9-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046380; P:N-acetylneuraminate biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011950; HAD-SF_hydro_IA_CTE7.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02253; CTE7; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium;
KW Reference proteome.
FT CHAIN 1..248
FT /note="N-acylneuraminate-9-phosphatase"
FT /id="PRO_0000083939"
FT BINDING 12..14
FT /ligand="substrate"
FT BINDING 131..132
FT /ligand="substrate"
FT BINDING 164
FT /ligand="substrate"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2GFH"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 20..37
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2GFH"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2GFH"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2GFH"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2GFH"
SQ SEQUENCE 248 AA; 27808 MW; FA1703873D7CC069 CRC64;
MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD KVQVKLSKEC
FHPYSTCITD VRTSHWEEAI QETKGGADNR KLAEECYFLW KSTRLQHMIL ADDVKAMLTE
LRKEVRLLLL TNGDRQTQRE KIEACACQSY FDAIVIGGEQ KEEKPAPSIF YHCCDLLGVQ
PGDCVMVGDT LETDIQGGLN AGLKATVWIN KSGRVPLTSS PMPHYMVSSV LELPALLQSI
DCKVSMSV
