NANP_HUMAN
ID NANP_HUMAN Reviewed; 248 AA.
AC Q8TBE9; B3KP12; Q5JYN8; Q8TE97; Q9Y3N0;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
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=C20orf147, HDHD4;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16237198; DOI=10.1093/glycob/cwj050;
RA Maliekal P., Vertommen D., Delpierre G., Van Schaftingen E.;
RT "Identification of the sequence encoding N-acetylneuraminate-9-phosphate
RT phosphatase.";
RL Glycobiology 16:165-172(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human N-acetylneuraminic acid phosphatase,
RT NANP.";
RL Submitted (DEC-2008) 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 Evidence={ECO:0000269|PubMed:16237198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16237198};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate and calcium.
CC {ECO:0000269|PubMed:16237198}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for N-acetylneuraminate 9-P {ECO:0000269|PubMed:16237198};
CC KM=19.2 mM for fructose 1,6-P2 {ECO:0000269|PubMed:16237198};
CC KM=2.7 mM for 6-P-gluconate {ECO:0000269|PubMed:16237198};
CC KM=5.9 mM for N-acetylglucosamine 6-P {ECO:0000269|PubMed:16237198};
CC Vmax=112 umol/min/mg enzyme with N-acetylneuraminate 9-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=6.10 umol/min/mg enzyme with fructose 1,6-P2 as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=2.79 umol/min/mg enzyme with 6-P-gluconate as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=2.46 umol/min/mg enzyme with N-acetylglucosamine 6-P as
CC substrate {ECO:0000269|PubMed:16237198};
CC Vmax=0.149 umol/min/mg enzyme with sorbitol 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.140 umol/min/mg enzyme with 3-P glycerate as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.095 umol/min/mg enzyme with P-serine as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.094 umol/min/mg enzyme with glycerol 3-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.090 umol/min/mg enzyme with ribulose 5-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.072 umol/min/mg enzyme with N-acetylmannosamine 6-P as
CC substrate {ECO:0000269|PubMed:16237198};
CC Vmax=0.063 umol/min/mg enzyme with arabinose 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.042 umol/min/mg enzyme with ribose 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.023 umol/min/mg enzyme with glucosamine 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.019 umol/min/mg enzyme with phosphoglycolate as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.019 umol/min/mg enzyme with fructose 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.017 umol/min/mg enzyme with glycerol 2-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.016 umol/min/mg enzyme with glucose 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.015 umol/min/mg enzyme with mannose 6-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.004 umol/min/mg enzyme with glucose 1-P as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.002 umol/min/mg enzyme with P-enolpyruvate as substrate
CC {ECO:0000269|PubMed:16237198};
CC Vmax=0.001 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:16237198};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NANP family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85055.1; Type=Miscellaneous discrepancy; Note=It seems to be derived from genomic DNA and not from cDNA.; Evidence={ECO:0000305};
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DR EMBL; AK055472; BAG51524.1; -; mRNA.
DR EMBL; AK074335; BAB85055.1; ALT_SEQ; mRNA.
DR EMBL; AL031673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10081.1; -; Genomic_DNA.
DR EMBL; BC022552; AAH22552.1; -; mRNA.
DR CCDS; CCDS13173.1; -.
DR RefSeq; NP_689880.1; NM_152667.2.
DR PDB; 2W4M; X-ray; 2.60 A; A=1-248.
DR PDB; 4KNV; X-ray; 1.99 A; A/B=7-242.
DR PDB; 4KNW; X-ray; 2.70 A; A/B/C=2-248.
DR PDBsum; 2W4M; -.
DR PDBsum; 4KNV; -.
DR PDBsum; 4KNW; -.
DR AlphaFoldDB; Q8TBE9; -.
DR BMRB; Q8TBE9; -.
DR SMR; Q8TBE9; -.
DR BioGRID; 126729; 14.
DR IntAct; Q8TBE9; 6.
DR STRING; 9606.ENSP00000302441; -.
DR BindingDB; Q8TBE9; -.
DR ChEMBL; CHEMBL2401602; -.
DR DEPOD; NANP; -.
DR iPTMnet; Q8TBE9; -.
DR PhosphoSitePlus; Q8TBE9; -.
DR BioMuta; NANP; -.
DR DMDM; 30315932; -.
DR EPD; Q8TBE9; -.
DR jPOST; Q8TBE9; -.
DR MassIVE; Q8TBE9; -.
DR MaxQB; Q8TBE9; -.
DR PaxDb; Q8TBE9; -.
DR PeptideAtlas; Q8TBE9; -.
DR PRIDE; Q8TBE9; -.
DR ProteomicsDB; 74002; -.
DR Antibodypedia; 10091; 378 antibodies from 27 providers.
DR DNASU; 140838; -.
DR Ensembl; ENST00000304788.4; ENSP00000302441.3; ENSG00000170191.5.
DR GeneID; 140838; -.
DR KEGG; hsa:140838; -.
DR MANE-Select; ENST00000304788.4; ENSP00000302441.3; NM_152667.3; NP_689880.1.
DR UCSC; uc002wuy.5; human.
DR CTD; 140838; -.
DR DisGeNET; 140838; -.
DR GeneCards; NANP; -.
DR HGNC; HGNC:16140; NANP.
DR HPA; ENSG00000170191; Low tissue specificity.
DR MIM; 610763; gene.
DR neXtProt; NX_Q8TBE9; -.
DR OpenTargets; ENSG00000170191; -.
DR PharmGKB; PA25689; -.
DR VEuPathDB; HostDB:ENSG00000170191; -.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00390000003094; -.
DR HOGENOM; CLU_045011_8_2_1; -.
DR InParanoid; Q8TBE9; -.
DR OMA; WLKLRYR; -.
DR OrthoDB; 1113437at2759; -.
DR PhylomeDB; Q8TBE9; -.
DR TreeFam; TF324589; -.
DR BioCyc; MetaCyc:HS10082-MON; -.
DR PathwayCommons; Q8TBE9; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR SABIO-RK; Q8TBE9; -.
DR SignaLink; Q8TBE9; -.
DR UniPathway; UPA00630; -.
DR BioGRID-ORCS; 140838; 33 hits in 1078 CRISPR screens.
DR EvolutionaryTrace; Q8TBE9; -.
DR GenomeRNAi; 140838; -.
DR Pharos; Q8TBE9; Tbio.
DR PRO; PR:Q8TBE9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TBE9; protein.
DR Bgee; ENSG00000170191; Expressed in kidney epithelium and 162 other tissues.
DR Genevisible; Q8TBE9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0050124; F:N-acylneuraminate-9-phosphatase activity; IDA: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; IDA: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_0000083938"
FT BINDING 12..14
FT /ligand="substrate"
FT BINDING 131..132
FT /ligand="substrate"
FT BINDING 164
FT /ligand="substrate"
FT CONFLICT 32..55
FT /note="IKLLQSKYHYKEEAEIICDKVQVK -> TSPPMALLWAGSVRPAPSCTLTSP
FT (in Ref. 1; BAB85055)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:4KNV"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:4KNV"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2W4M"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 90..107
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4KNV"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4KNV"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4KNV"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:4KNV"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:4KNV"
SQ SEQUENCE 248 AA; 27813 MW; 360E6D7AB965294B CRC64;
MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD KVQVKLSKEC
FHPYNTCITD LRTSHWEEAI QETKGGAANR KLAEECYFLW KSTRLQHMTL AEDVKAMLTE
LRKEVRLLLL TNGDRQTQRE KIEACACQSY FDAVVVGGEQ REEKPAPSIF YYCCNLLGVQ
PGDCVMVGDT LETDIQGGLN AGLKATVWIN KNGIVPLKSS PVPHYMVSSV LELPALLQSI
DCKVSMST
