ID   GNPAT_HUMAN             Reviewed;         680 AA.
AC   O15228; Q5TBH7; Q9BWC2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-NOV-2007, entry version 74.
DE   Dihydroxyacetone phosphate acyltransferase (EC 2.3.1.42) (DHAP-AT)
DE   (DAP-AT) (Glycerone-phosphate O-acyltransferase) (Acyl-
DE   CoA:dihydroxyacetonephosphateacyltransferase).
GN   Name=GNPAT; Synonyms=DAPAT, DHAPAT;
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].
RC   TISSUE=Brain;
RX   MEDLINE=98119399; PubMed=9459311; DOI=10.1016/S0014-5793(97)01495-6;
RA   Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K.,
RA   Just W.W.;
RT   "Ether lipid biosynthesis: isolation and molecular characterization of
RT   human dihydroxyacetonephosphate acyltransferase.";
RL   FEBS Lett. 420:205-211(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-33, AND VARIANTS
RP   RCDP2 CYS-211 AND HIS-211.
RX   MEDLINE=98204809; PubMed=9536089; DOI=10.1093/hmg/7.5.847;
RA   Ofman R., Hettema E.H., Hogenhout E.M., Caruso U., Muijsers A.O.,
RA   Wanders R.J.A.;
RT   "Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the
RT   human cDNA and resolution of the molecular basis in rhizomelic
RT   chondrodysplasia punctata type 2.";
RL   Hum. Mol. Genet. 7:847-853(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21134310; PubMed=11237722; DOI=10.1006/bbrc.2001.4407;
RA   Ofman R., Lajmir S., Wanders R.J.A.;
RT   "Etherphospholipid biosynthesis and dihydroxyactetone-phosphate
RT   acyltransferase: resolution of the genomic organization of the human
RT   GNPAT gene and its use in the identification of novel mutations.";
RL   Biochem. Biophys. Res. Commun. 281:754-760(2001).
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], AND VARIANT HIS-586.
RC   TISSUE=Lung;
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   VARIANTS RCDP2 HIS-211 AND GLY-519, AND CHARACTERIZATION OF VARIANTS
RP   RCDP2 HIS-211 AND GLY-519.
RX   PubMed=11152660; DOI=10.1093/hmg/10.2.127;
RA   Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K.,
RA   Just W.W.;
RT   "Impaired membrane traffic in defective ether lipid biosynthesis.";
RL   Hum. Mol. Genet. 10:127-136(2001).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + glycerone phosphate = CoA +
CC       acylglycerone phosphate.
CC   -!- PATHWAY: Lipid metabolism; glycerophospholipid metabolism.
CC   -!- SUBUNIT: May be part of an heterotrimeric complex composed of DAP-
CC       AT, ADAP-S and a modified form of DAP-AT.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Matrix side (By
CC       similarity). Note=Exclusively localized to the lumenal side of the
CC       peroxisomal membrane (By similarity).
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- DISEASE: Defects in GNPAT are the cause of rhizomelic
CC       chondrodysplasia punctata type 2 (RCDP2) [MIM:222765]. RDCP2 is
CC       characterized by rhizomelic shortening of femur and humerus,
CC       vertebral disorders, cataract, cutaneous lesions and severe mental
CC       retardation.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=GNPAT";
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DR   EMBL; AJ002190; CAA05242.1; -; mRNA.
DR   EMBL; AF043937; AAC24505.1; -; mRNA.
DR   EMBL; AF218233; AAG17547.1; -; Genomic_DNA.
DR   EMBL; AF218223; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218224; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218225; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218226; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218227; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218228; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218229; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218230; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218231; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AF218232; AAG17547.1; JOINED; Genomic_DNA.
DR   EMBL; AL137801; CAI21988.1; -; Genomic_DNA.
DR   EMBL; AL117352; CAI21988.1; JOINED; Genomic_DNA.
DR   EMBL; AL117352; CAI23094.1; -; Genomic_DNA.
DR   EMBL; AL137801; CAI23094.1; JOINED; Genomic_DNA.
DR   EMBL; BC000450; AAH00450.1; -; mRNA.
DR   RefSeq; NP_055051.1; -.
DR   UniGene; Hs.498028; -.
DR   Ensembl; ENSG00000116906; Homo sapiens.
DR   GeneID; 8443; -.
DR   KEGG; hsa:8443; -.
DR   H-InvDB; HIX0001692; -.
DR   HGNC; HGNC:4416; GNPAT.
DR   MIM; 222765; phenotype.
DR   MIM; 602744; gene.
DR   Orphanet; 177; Chondrodysplasia punctata, rhizomelic type.
DR   PharmGKB; PA28795; -.
DR   Reactome; REACT_602; Lipid and lipoprotein metabolism.
DR   LinkHub; O15228; -.
DR   ArrayExpress; O15228; -.
DR   CleanEx; HS_GNPAT; -.
DR   GermOnline; ENSG00000116906; Homo sapiens.
DR   GO; GO:0005777; C:peroxisome; TAS:ProtInc.
DR   GO; GO:0008415; F:acyltransferase activity; TAS:ProtInc.
DR   GO; GO:0006631; P:fatty acid metabolic process; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   InterPro; IPR002123; Acyltransferase.
DR   InterPro; IPR012123; DHAPAT.
DR   InterPro; IPR012082; G3P_DHAP-acetyltrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   PIRSF; PIRSF500063; DHAPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cataract; Direct protein sequencing;
KW   Disease mutation; Dwarfism; Membrane; Peroxisome;
KW   Rhizomelic chondrodysplasia punctata; Transferase.
FT   CHAIN         1    680       Dihydroxyacetone phosphate
FT                                acyltransferase.
FT                                /FTId=PRO_0000195246.
FT   MOTIF       162    167       HXXXXD motif.
FT   MOTIF       678    680       Microbody targeting signal (Potential).
FT   COMPBIAS      3      9       Poly-Ser.
FT   VARIANT     211    211       R -> C (in RCDP2).
FT                                /FTId=VAR_006357.
FT   VARIANT     211    211       R -> H (in RCDP2; complete loss of
FT                                activity).
FT                                /FTId=VAR_006358.
FT   VARIANT     495    495       V -> I (in dbSNP:rs11122266).
FT                                /FTId=VAR_030696.
FT   VARIANT     519    519       D -> G (in RCDP2; 70% reduction in
FT                                activity; dbSNP:rs11558492).
FT                                /FTId=VAR_025897.
FT   VARIANT     586    586       Y -> H (in dbSNP:rs17849315).
FT                                /FTId=VAR_030697.
FT   CONFLICT     26     26       S -> K (in Ref. 2; AA sequence).
FT   CONFLICT     31     31       K -> N (in Ref. 2; AA sequence).
SQ   SEQUENCE   680 AA;  77188 MW;  BDF624CCD4D92477 CRC64;
     MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF AMKCYTPLVY
     KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR EEVSEILDEM SHKLRLGAIR
     FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL
     PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF
     FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV
     PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE
     DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL WLKGLTQAFG
     GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG DSEVVDGLML QHITLLMCSA
     YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC
     YLLCKSEAIQ VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY
     LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC IFNVNEPATT
     KLEEMLGCKT PIGKPATAKL
//