ID   NANP_RAT                Reviewed;         248 AA.
AC   Q5M969;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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 {ECO:0000250|UniProtKB:Q9CPT3}; Synonyms=Hdhd4;
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;
RN   [1]
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   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, COFACTOR, AND
RP   ACTIVITY REGULATION.
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).
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   -!- 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; BC087587; AAH87587.1; -; mRNA.
DR   RefSeq; NP_001009409.1; NM_001009409.1.
DR   AlphaFoldDB; Q5M969; -.
DR   SMR; Q5M969; -.
DR   STRING; 10116.ENSRNOP00000011315; -.
DR   PaxDb; Q5M969; -.
DR   Ensembl; ENSRNOT00000011315; ENSRNOP00000011315; ENSRNOG00000008307.
DR   GeneID; 311530; -.
DR   KEGG; rno:311530; -.
DR   UCSC; RGD:1306009; rat.
DR   CTD; 140838; -.
DR   RGD; 1306009; Nanp.
DR   eggNOG; KOG3085; Eukaryota.
DR   GeneTree; ENSGT00390000003094; -.
DR   HOGENOM; CLU_045011_8_2_1; -.
DR   InParanoid; Q5M969; -.
DR   OMA; WLKLRYR; -.
DR   OrthoDB; 1113437at2759; -.
DR   PhylomeDB; Q5M969; -.
DR   TreeFam; TF324589; -.
DR   BioCyc; MetaCyc:MON-14517; -.
DR   Reactome; R-RNO-4085001; Sialic acid metabolism.
DR   SABIO-RK; Q5M969; -.
DR   UniPathway; UPA00630; -.
DR   PRO; PR:Q5M969; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000008307; Expressed in liver and 18 other tissues.
DR   Genevisible; Q5M969; RN.
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   Carbohydrate metabolism; Hydrolase; Magnesium; Reference proteome.
FT   CHAIN           1..248
FT                   /note="N-acylneuraminate-9-phosphatase"
FT                   /id="PRO_0000233379"
FT   BINDING         12..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   248 AA;  27741 MW;  7ABF6063C67BF1AB CRC64;
     MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEVICD KVQVKLSKEC
     FHPYSTCITD VRTSHWEEAI QETKGGADNR KLAEECYFLW KSTRLQHMTL EEDVKAMLTE
     LRKEVRLLLL TNGDRQTQRE KIEACACQSY FDAIVVGGEQ KEEKPAPSIF YHCCDLLGVQ
     PGDCVMVGDT LETDIQGGLN AGLKATVWIN KSGGVPLTSS PMPHYMVSSV LELPALLQSI
     DCKVSMSV