Full text data of NPL
NPL
(C1orf13)
[Confidence: low (only semi-automatic identification from reviews)]
N-acetylneuraminate lyase; NALase; 4.1.3.3 (N-acetylneuraminate pyruvate-lyase; N-acetylneuraminic acid aldolase; Sialate lyase; Sialate-pyruvate lyase; Sialic acid aldolase; Sialic acid lyase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-acetylneuraminate lyase; NALase; 4.1.3.3 (N-acetylneuraminate pyruvate-lyase; N-acetylneuraminic acid aldolase; Sialate lyase; Sialate-pyruvate lyase; Sialic acid aldolase; Sialic acid lyase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BXD5
ID NPL_HUMAN Reviewed; 320 AA.
AC Q9BXD5; B2R839; Q4G0Q8; Q4G0Z2; Q64L88; Q6PEL0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=N-acetylneuraminate lyase;
DE Short=NALase;
DE EC=4.1.3.3;
DE AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE AltName: Full=N-acetylneuraminic acid aldolase;
DE AltName: Full=Sialate lyase;
DE AltName: Full=Sialate-pyruvate lyase;
DE AltName: Full=Sialic acid aldolase;
DE AltName: Full=Sialic acid lyase;
GN Name=NPL; Synonyms=C1orf13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human
RT RGS8 gene from the 1q25 region encompassing the hereditary prostate
RT cancer (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=16147865; DOI=10.1080/10425170400020373;
RA Wu M., Gu S., Xu J., Zou X., Zheng H., Jin Z., Xie Y., Ji C., Mao Y.;
RT "A novel splice variant of human gene NPL, mainly expressed in human
RT liver, kidney and peripheral blood leukocyte.";
RL DNA Seq. 16:137-142(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Hypothalamus, Kidney, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.M112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups:
RT elucidating the intracellular fate of the non-human sialic acid N-
RT glycolylneuraminic acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
CC -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid
CC (sialic acid) to form pyruvate and N-acetylmannosamine via a
CC Schiff base intermediate. It prevents sialic acids from being
CC recycled and returning to the cell surface. Involved in the N-
CC glycolylneuraminic acid (Neu5Gc) degradation pathway. Although
CC human is not able to catalyze formation of Neu5Gc due to the
CC inactive CMAHP enzyme, Neu5Gc is present in food and must be
CC degraded (By similarity).
CC -!- CATALYTIC ACTIVITY: N-acetylneuraminate = N-acetyl-D-mannosamine +
CC pyruvate.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BXD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXD5-2; Sequence=VSP_022518;
CC Name=3;
CC IsoId=Q9BXD5-3; Sequence=VSP_022522;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9BXD5-4; Sequence=VSP_022521, VSP_022522;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9BXD5-5; Sequence=VSP_022519, VSP_022520;
CC Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in placenta, liver,
CC kidney, pancreas, spleen, thymus, ovary, small intestine and
CC peripheral blood leukocyte.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC042003; Type=Frameshift; Positions=213;
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DR EMBL; AF338436; AAK25795.1; -; mRNA.
DR EMBL; AY336748; AAQ82432.1; -; mRNA.
DR EMBL; AK313225; BAG36036.1; -; mRNA.
DR EMBL; AL355999; CAH71702.1; -; Genomic_DNA.
DR EMBL; AL513344; CAH71702.1; JOINED; Genomic_DNA.
DR EMBL; AL355999; CAH71703.1; -; Genomic_DNA.
DR EMBL; AL513344; CAH71703.1; JOINED; Genomic_DNA.
DR EMBL; AL513344; CAI16502.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI16502.1; JOINED; Genomic_DNA.
DR EMBL; AL513344; CAI16503.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI16503.1; JOINED; Genomic_DNA.
DR EMBL; BC034966; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC042003; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC058003; AAH58003.1; -; mRNA.
DR EMBL; BC125051; AAI25052.1; -; mRNA.
DR RefSeq; NP_001186979.1; NM_001200050.1.
DR RefSeq; NP_001186980.1; NM_001200051.1.
DR RefSeq; NP_001186985.1; NM_001200056.1.
DR RefSeq; NP_110396.1; NM_030769.2.
DR RefSeq; XP_005245561.1; XM_005245504.1.
DR UniGene; Hs.496969; -.
DR UniGene; Hs.731792; -.
DR ProteinModelPortal; Q9BXD5; -.
DR SMR; Q9BXD5; 8-280.
DR STRING; 9606.ENSP00000258317; -.
DR PhosphoSite; Q9BXD5; -.
DR DMDM; 74752428; -.
DR PaxDb; Q9BXD5; -.
DR PRIDE; Q9BXD5; -.
DR Ensembl; ENST00000258317; ENSP00000258317; ENSG00000135838.
DR Ensembl; ENST00000367552; ENSP00000356523; ENSG00000135838.
DR Ensembl; ENST00000367553; ENSP00000356524; ENSG00000135838.
DR Ensembl; ENST00000367554; ENSP00000356525; ENSG00000135838.
DR Ensembl; ENST00000367555; ENSP00000356526; ENSG00000135838.
DR GeneID; 80896; -.
DR KEGG; hsa:80896; -.
DR UCSC; uc009wyb.3; human.
DR CTD; 80896; -.
DR GeneCards; GC01P182758; -.
DR HGNC; HGNC:16781; NPL.
DR HPA; HPA028345; -.
DR MIM; 611412; gene.
DR neXtProt; NX_Q9BXD5; -.
DR PharmGKB; PA25602; -.
DR eggNOG; COG0329; -.
DR HOGENOM; HOG000218206; -.
DR HOVERGEN; HBG082055; -.
DR InParanoid; Q9BXD5; -.
DR KO; K01639; -.
DR OMA; PWNKDVL; -.
DR OrthoDB; EOG7NKKKP; -.
DR PhylomeDB; Q9BXD5; -.
DR UniPathway; UPA00629; -.
DR ChiTaRS; NPL; human.
DR GenomeRNAi; 80896; -.
DR NextBio; 71336; -.
DR PRO; PR:Q9BXD5; -.
DR ArrayExpress; Q9BXD5; -.
DR Bgee; Q9BXD5; -.
DR CleanEx; HS_NPL; -.
DR Genevestigator; Q9BXD5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR PROSITE; PS00665; DHDPS_1; FALSE_NEG.
DR PROSITE; PS00666; DHDPS_2; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Complete proteome;
KW Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1 320 N-acetylneuraminate lyase.
FT /FTId=PRO_0000273352.
FT REGION 51 52 Substrate binding (By similarity).
FT ACT_SITE 173 173 Schiff-base intermediate with substrate
FT (By similarity).
FT SITE 143 143 Involved in proton transfer during
FT cleavage (By similarity).
FT VAR_SEQ 1 77 MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQ
FT GVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDK -> M
FT SRAPGILASWRRAPSLSVQKGSQTARHTCHPEVPLGNCFLP
FT VYKASPLTVTRLWAER (in isoform 2).
FT /FTId=VSP_022518.
FT VAR_SEQ 78 109 LDQVIIHVGALSLKESQELAQHAAEIGADGIA -> SNHHK
FT LGTIRTTQSRQSSFRRQLKAWHSGSHL (in isoform
FT 5).
FT /FTId=VSP_022519.
FT VAR_SEQ 110 320 Missing (in isoform 5).
FT /FTId=VSP_022520.
FT VAR_SEQ 203 246 Missing (in isoform 4).
FT /FTId=VSP_022521.
FT VAR_SEQ 260 320 GFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKL
FT KSLDFLSFTDLKDGNLEAGS -> ENSKLKVSKNQRTLPLG
FT TTNFPFLH (in isoform 3 and isoform 4).
FT /FTId=VSP_022522.
FT CONFLICT 4 4 P -> S (in Ref. 5; BC034966).
FT CONFLICT 98 98 Q -> E (in Ref. 5; BC042003).
FT CONFLICT 212 212 A -> E (in Ref. 5; BC042003).
FT CONFLICT 260 260 G -> V (in Ref. 3; BAG36036).
SQ SEQUENCE 320 AA; 35163 MW; FC0EBA9B05FE9E62 CRC64;
MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV
SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT
KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL
DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS
LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL
KSLDFLSFTD LKDGNLEAGS
//
ID NPL_HUMAN Reviewed; 320 AA.
AC Q9BXD5; B2R839; Q4G0Q8; Q4G0Z2; Q64L88; Q6PEL0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=N-acetylneuraminate lyase;
DE Short=NALase;
DE EC=4.1.3.3;
DE AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE AltName: Full=N-acetylneuraminic acid aldolase;
DE AltName: Full=Sialate lyase;
DE AltName: Full=Sialate-pyruvate lyase;
DE AltName: Full=Sialic acid aldolase;
DE AltName: Full=Sialic acid lyase;
GN Name=NPL; Synonyms=C1orf13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human
RT RGS8 gene from the 1q25 region encompassing the hereditary prostate
RT cancer (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=16147865; DOI=10.1080/10425170400020373;
RA Wu M., Gu S., Xu J., Zou X., Zheng H., Jin Z., Xie Y., Ji C., Mao Y.;
RT "A novel splice variant of human gene NPL, mainly expressed in human
RT liver, kidney and peripheral blood leukocyte.";
RL DNA Seq. 16:137-142(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Hypothalamus, Kidney, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.M112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups:
RT elucidating the intracellular fate of the non-human sialic acid N-
RT glycolylneuraminic acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
CC -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid
CC (sialic acid) to form pyruvate and N-acetylmannosamine via a
CC Schiff base intermediate. It prevents sialic acids from being
CC recycled and returning to the cell surface. Involved in the N-
CC glycolylneuraminic acid (Neu5Gc) degradation pathway. Although
CC human is not able to catalyze formation of Neu5Gc due to the
CC inactive CMAHP enzyme, Neu5Gc is present in food and must be
CC degraded (By similarity).
CC -!- CATALYTIC ACTIVITY: N-acetylneuraminate = N-acetyl-D-mannosamine +
CC pyruvate.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BXD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXD5-2; Sequence=VSP_022518;
CC Name=3;
CC IsoId=Q9BXD5-3; Sequence=VSP_022522;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9BXD5-4; Sequence=VSP_022521, VSP_022522;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9BXD5-5; Sequence=VSP_022519, VSP_022520;
CC Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in placenta, liver,
CC kidney, pancreas, spleen, thymus, ovary, small intestine and
CC peripheral blood leukocyte.
CC -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC042003; Type=Frameshift; Positions=213;
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DR EMBL; AF338436; AAK25795.1; -; mRNA.
DR EMBL; AY336748; AAQ82432.1; -; mRNA.
DR EMBL; AK313225; BAG36036.1; -; mRNA.
DR EMBL; AL355999; CAH71702.1; -; Genomic_DNA.
DR EMBL; AL513344; CAH71702.1; JOINED; Genomic_DNA.
DR EMBL; AL355999; CAH71703.1; -; Genomic_DNA.
DR EMBL; AL513344; CAH71703.1; JOINED; Genomic_DNA.
DR EMBL; AL513344; CAI16502.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI16502.1; JOINED; Genomic_DNA.
DR EMBL; AL513344; CAI16503.1; -; Genomic_DNA.
DR EMBL; AL355999; CAI16503.1; JOINED; Genomic_DNA.
DR EMBL; BC034966; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC042003; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC058003; AAH58003.1; -; mRNA.
DR EMBL; BC125051; AAI25052.1; -; mRNA.
DR RefSeq; NP_001186979.1; NM_001200050.1.
DR RefSeq; NP_001186980.1; NM_001200051.1.
DR RefSeq; NP_001186985.1; NM_001200056.1.
DR RefSeq; NP_110396.1; NM_030769.2.
DR RefSeq; XP_005245561.1; XM_005245504.1.
DR UniGene; Hs.496969; -.
DR UniGene; Hs.731792; -.
DR ProteinModelPortal; Q9BXD5; -.
DR SMR; Q9BXD5; 8-280.
DR STRING; 9606.ENSP00000258317; -.
DR PhosphoSite; Q9BXD5; -.
DR DMDM; 74752428; -.
DR PaxDb; Q9BXD5; -.
DR PRIDE; Q9BXD5; -.
DR Ensembl; ENST00000258317; ENSP00000258317; ENSG00000135838.
DR Ensembl; ENST00000367552; ENSP00000356523; ENSG00000135838.
DR Ensembl; ENST00000367553; ENSP00000356524; ENSG00000135838.
DR Ensembl; ENST00000367554; ENSP00000356525; ENSG00000135838.
DR Ensembl; ENST00000367555; ENSP00000356526; ENSG00000135838.
DR GeneID; 80896; -.
DR KEGG; hsa:80896; -.
DR UCSC; uc009wyb.3; human.
DR CTD; 80896; -.
DR GeneCards; GC01P182758; -.
DR HGNC; HGNC:16781; NPL.
DR HPA; HPA028345; -.
DR MIM; 611412; gene.
DR neXtProt; NX_Q9BXD5; -.
DR PharmGKB; PA25602; -.
DR eggNOG; COG0329; -.
DR HOGENOM; HOG000218206; -.
DR HOVERGEN; HBG082055; -.
DR InParanoid; Q9BXD5; -.
DR KO; K01639; -.
DR OMA; PWNKDVL; -.
DR OrthoDB; EOG7NKKKP; -.
DR PhylomeDB; Q9BXD5; -.
DR UniPathway; UPA00629; -.
DR ChiTaRS; NPL; human.
DR GenomeRNAi; 80896; -.
DR NextBio; 71336; -.
DR PRO; PR:Q9BXD5; -.
DR ArrayExpress; Q9BXD5; -.
DR Bgee; Q9BXD5; -.
DR CleanEx; HS_NPL; -.
DR Genevestigator; Q9BXD5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR PROSITE; PS00665; DHDPS_1; FALSE_NEG.
DR PROSITE; PS00666; DHDPS_2; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Complete proteome;
KW Cytoplasm; Lyase; Reference proteome; Schiff base.
FT CHAIN 1 320 N-acetylneuraminate lyase.
FT /FTId=PRO_0000273352.
FT REGION 51 52 Substrate binding (By similarity).
FT ACT_SITE 173 173 Schiff-base intermediate with substrate
FT (By similarity).
FT SITE 143 143 Involved in proton transfer during
FT cleavage (By similarity).
FT VAR_SEQ 1 77 MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQ
FT GVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDK -> M
FT SRAPGILASWRRAPSLSVQKGSQTARHTCHPEVPLGNCFLP
FT VYKASPLTVTRLWAER (in isoform 2).
FT /FTId=VSP_022518.
FT VAR_SEQ 78 109 LDQVIIHVGALSLKESQELAQHAAEIGADGIA -> SNHHK
FT LGTIRTTQSRQSSFRRQLKAWHSGSHL (in isoform
FT 5).
FT /FTId=VSP_022519.
FT VAR_SEQ 110 320 Missing (in isoform 5).
FT /FTId=VSP_022520.
FT VAR_SEQ 203 246 Missing (in isoform 4).
FT /FTId=VSP_022521.
FT VAR_SEQ 260 320 GFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKL
FT KSLDFLSFTDLKDGNLEAGS -> ENSKLKVSKNQRTLPLG
FT TTNFPFLH (in isoform 3 and isoform 4).
FT /FTId=VSP_022522.
FT CONFLICT 4 4 P -> S (in Ref. 5; BC034966).
FT CONFLICT 98 98 Q -> E (in Ref. 5; BC042003).
FT CONFLICT 212 212 A -> E (in Ref. 5; BC042003).
FT CONFLICT 260 260 G -> V (in Ref. 3; BAG36036).
SQ SEQUENCE 320 AA; 35163 MW; FC0EBA9B05FE9E62 CRC64;
MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV
SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT
KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL
DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS
LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL
KSLDFLSFTD LKDGNLEAGS
//
MIM
611412
*RECORD*
*FIELD* NO
611412
*FIELD* TI
*611412 N-ACETYLNEURAMINATE PYRUVATE LYASE; NPL
;;CHROMOSOME 1 OPEN READING FRAME 13; C1ORF13;;
read moreDIHYDRODIPICOLINATE SYNTHASE;;
C112
*FIELD* TX
DESCRIPTION
N-acetylneuraminate pyruvate lyase (EC 4.1.3.3) controls the cellular
concentration of sialic acid by catalyzing the conversion of sialic acid
into acylmannosamines and pyruvate (Wu et al., 2005).
CLONING
By searching for genes in a region of chromosome 1 associated with
hereditary prostate cancer (HPC1; 601518), followed by screening cDNA
libraries, Sood et al. (2001) cloned NPL, which they called C112. The
deduced protein contains 320 amino acids. Northern blot analysis
detected weak expression of a 5-kb transcript in all human tissues
examined.
By large-scale sequence analysis of clones obtained from a fetal brain
cDNA library, Wu et al. (2005) cloned a splice variant of NPL. The
deduced 301-amino acid splice variant, which they called NPLV2, contains
an N-terminal dihydrodipicolinate synthase (DHDPS) domain and 5 putative
N-terminal phosphorylation sites. RT-PCR detected highest expression in
liver, kidney, and peripheral blood leukocytes, and lower expression in
placenta, pancreas, spleen, thymus, ovary, and small intestine. By
database analysis, Wu et al. (2005) identified 3 other NPL splice
variants.
GENE STRUCTURE
Wu et al. (2005) determined that the NPL gene contains 11 exons and
spans over 40 kb.
MAPPING
By genomic sequence analysis, Sood et al. (2001) mapped the NPL gene to
chromosome 1q25.
*FIELD* RF
1. Sood, R.; Bonner, T. I.; Makalowska, I.; Stephan, D. A.; Robbins,
C. M.; Connors, T. D.; Morgenbesser, S. D.; Su, K.; Faruque, M. U.;
Pinkett, H.; Graham, C.; Baxevanis, A. D.; Klinger, K. W.; Landes,
G. M.; Trent, J. M.; Carpten, J. D.: Cloning and characterization
of 13 novel transcripts and the human RGS8 gene from the 1q25 region
encompassing the hereditary prostate cancer (HPC1) locus. Genomics 73:
211-222, 2001.
2. Wu, M.; Gu, S.; Xu, J.; Zou, X.; Zheng, H.; Jin, Z.; Xie, Y.; Ji,
C.; Mao, Y.: A novel splice variant of human gene NPL, mainly expressed
in human liver, kidney and peripheral blood leukocyte. DNA Seq. 16:
137-142, 2005.
*FIELD* CD
Patricia A. Hartz: 9/7/2007
*FIELD* ED
wwang: 09/07/2007
*RECORD*
*FIELD* NO
611412
*FIELD* TI
*611412 N-ACETYLNEURAMINATE PYRUVATE LYASE; NPL
;;CHROMOSOME 1 OPEN READING FRAME 13; C1ORF13;;
read moreDIHYDRODIPICOLINATE SYNTHASE;;
C112
*FIELD* TX
DESCRIPTION
N-acetylneuraminate pyruvate lyase (EC 4.1.3.3) controls the cellular
concentration of sialic acid by catalyzing the conversion of sialic acid
into acylmannosamines and pyruvate (Wu et al., 2005).
CLONING
By searching for genes in a region of chromosome 1 associated with
hereditary prostate cancer (HPC1; 601518), followed by screening cDNA
libraries, Sood et al. (2001) cloned NPL, which they called C112. The
deduced protein contains 320 amino acids. Northern blot analysis
detected weak expression of a 5-kb transcript in all human tissues
examined.
By large-scale sequence analysis of clones obtained from a fetal brain
cDNA library, Wu et al. (2005) cloned a splice variant of NPL. The
deduced 301-amino acid splice variant, which they called NPLV2, contains
an N-terminal dihydrodipicolinate synthase (DHDPS) domain and 5 putative
N-terminal phosphorylation sites. RT-PCR detected highest expression in
liver, kidney, and peripheral blood leukocytes, and lower expression in
placenta, pancreas, spleen, thymus, ovary, and small intestine. By
database analysis, Wu et al. (2005) identified 3 other NPL splice
variants.
GENE STRUCTURE
Wu et al. (2005) determined that the NPL gene contains 11 exons and
spans over 40 kb.
MAPPING
By genomic sequence analysis, Sood et al. (2001) mapped the NPL gene to
chromosome 1q25.
*FIELD* RF
1. Sood, R.; Bonner, T. I.; Makalowska, I.; Stephan, D. A.; Robbins,
C. M.; Connors, T. D.; Morgenbesser, S. D.; Su, K.; Faruque, M. U.;
Pinkett, H.; Graham, C.; Baxevanis, A. D.; Klinger, K. W.; Landes,
G. M.; Trent, J. M.; Carpten, J. D.: Cloning and characterization
of 13 novel transcripts and the human RGS8 gene from the 1q25 region
encompassing the hereditary prostate cancer (HPC1) locus. Genomics 73:
211-222, 2001.
2. Wu, M.; Gu, S.; Xu, J.; Zou, X.; Zheng, H.; Jin, Z.; Xie, Y.; Ji,
C.; Mao, Y.: A novel splice variant of human gene NPL, mainly expressed
in human liver, kidney and peripheral blood leukocyte. DNA Seq. 16:
137-142, 2005.
*FIELD* CD
Patricia A. Hartz: 9/7/2007
*FIELD* ED
wwang: 09/07/2007