PPA6_HUMAN
ID PPA6_HUMAN Reviewed; 428 AA.
AC Q9NPH0; Q59G61; Q5T490; Q6IAQ3; Q7LG81; Q9UIG6; X5D289;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Lysophosphatidic acid phosphatase type 6;
DE EC=3.1.3.2 {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:23807634};
DE AltName: Full=Acid phosphatase 6, lysophosphatidic;
DE AltName: Full=Acid phosphatase-like protein 1;
DE AltName: Full=PACPL1;
DE Flags: Precursor;
GN Name=ACP6; Synonyms=ACPL1, LPAP; ORFNames=UNQ205/PRO231;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-59, INDUCTION, CATALYTIC ACTIVITY,
RP AND SUBSTRATE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10506173; DOI=10.1074/jbc.274.41.29172;
RA Hiroyama M., Takenawa T.;
RT "Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that
RT is involved in the regulation of mitochondrial lipid biosynthesis.";
RL J. Biol. Chem. 274:29172-29180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12010880; DOI=10.1136/gut.50.6.790;
RA Takayama I., Daigo Y., Ward S.M., Sanders K.M., Walker R.L., Horowitz B.,
RA Yamanaka T., Fujino M.A.;
RT "Novel human and mouse genes encoding an acid phosphatase family member and
RT its downregulation in W/W(V) mouse jejunum.";
RL Gut 50:790-796(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=24722188; DOI=10.1038/ncomms4650;
RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT "Protein interaction network of alternatively spliced isoforms from brain
RT links genetic risk factors for autism.";
RL Nat. Commun. 5:3650-3650(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-316.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Pancreas;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-428 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 33-47.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 33-428 IN COMPLEXES WITH MALONATE
RP AND TARTRATE, ACTIVE SITE, PROBABLE SUBSTRATE-BINDING SITES, CATALYTIC
RP ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-58; HIS-59; ARG-62;
RP TYR-106; ARG-168; ALA-257; SER-285; LEU-289; HIS-334 AND ASP-335.
RX PubMed=23807634; DOI=10.1007/s13238-013-3031-z;
RA Li J., Dong Y., Lu X., Wang L., Peng W., Zhang X.C., Rao Z.;
RT "Crystal structures and biochemical studies of human lysophosphatidic acid
RT phosphatase type 6.";
RL Protein Cell 4:548-561(2013).
CC -!- FUNCTION: Hydrolyzes lysophosphatidic acid (LPA) containing a medium
CC length fatty acid chain to the corresponding monoacylglycerol. Has
CC highest activity with lysophosphatidic acid containing myristate
CC (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower
CC activity with C18:0 and C6:0 lysophosphatidic acid.
CC {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:23807634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:23807634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000305|PubMed:10506173};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000269|PubMed:10506173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000305|PubMed:10506173};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23807634}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10506173}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPH0-2; Sequence=VSP_014121, VSP_014122;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, heart, small intestine,
CC muscle, liver, prostate, testis, ovary and weakly expressed in thymus
CC and colon. {ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:12010880}.
CC -!- INDUCTION: Induced with the differentiation from myoblast to myotube.
CC {ECO:0000269|PubMed:10506173}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally reported to be located in the mitochondrion,
CC but the evidence seems to be weak and contradictory with the presence
CC of a cleaved signal sequence. {ECO:0000305|PubMed:10506173}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA89311.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92485.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB031478; BAA89311.1; ALT_INIT; mRNA.
DR EMBL; AB030039; BAA94309.2; -; mRNA.
DR EMBL; KJ534759; AHW56399.1; -; mRNA.
DR EMBL; AY358552; AAQ88916.1; -; mRNA.
DR EMBL; AK000657; BAA91310.1; -; mRNA.
DR EMBL; AB209248; BAD92485.1; ALT_INIT; mRNA.
DR EMBL; AC241644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC242628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359207; CAI15199.1; -; Genomic_DNA.
DR EMBL; CH471223; EAW50931.1; -; Genomic_DNA.
DR EMBL; BC009965; AAH09965.1; -; mRNA.
DR EMBL; BC034686; AAH34686.1; -; mRNA.
DR EMBL; CR457101; CAG33382.1; -; mRNA.
DR CCDS; CCDS928.1; -. [Q9NPH0-1]
DR RefSeq; NP_057445.4; NM_016361.4. [Q9NPH0-1]
DR PDB; 4JOB; X-ray; 2.17 A; A=33-428.
DR PDB; 4JOC; X-ray; 2.21 A; A=33-428.
DR PDB; 4JOD; X-ray; 2.21 A; A=33-428.
DR PDBsum; 4JOB; -.
DR PDBsum; 4JOC; -.
DR PDBsum; 4JOD; -.
DR AlphaFoldDB; Q9NPH0; -.
DR SMR; Q9NPH0; -.
DR BioGRID; 119378; 30.
DR IntAct; Q9NPH0; 16.
DR STRING; 9606.ENSP00000463574; -.
DR SwissLipids; SLP:000001294; -.
DR DEPOD; ACP6; -.
DR iPTMnet; Q9NPH0; -.
DR PhosphoSitePlus; Q9NPH0; -.
DR BioMuta; ACP6; -.
DR DMDM; 317373268; -.
DR EPD; Q9NPH0; -.
DR jPOST; Q9NPH0; -.
DR MassIVE; Q9NPH0; -.
DR PaxDb; Q9NPH0; -.
DR PeptideAtlas; Q9NPH0; -.
DR PRIDE; Q9NPH0; -.
DR ProteomicsDB; 81995; -. [Q9NPH0-1]
DR ProteomicsDB; 81996; -. [Q9NPH0-2]
DR Antibodypedia; 33980; 181 antibodies from 22 providers.
DR DNASU; 51205; -.
DR Ensembl; ENST00000487562.5; ENSP00000481777.1; ENSG00000162836.12. [Q9NPH0-2]
DR Ensembl; ENST00000583509.7; ENSP00000463574.1; ENSG00000162836.12. [Q9NPH0-1]
DR GeneID; 51205; -.
DR KEGG; hsa:51205; -.
DR MANE-Select; ENST00000583509.7; ENSP00000463574.1; NM_016361.5; NP_057445.4.
DR UCSC; uc001epr.3; human.
DR CTD; 51205; -.
DR DisGeNET; 51205; -.
DR GeneCards; ACP6; -.
DR HGNC; HGNC:29609; ACP6.
DR HPA; ENSG00000162836; Low tissue specificity.
DR MIM; 611471; gene.
DR neXtProt; NX_Q9NPH0; -.
DR OpenTargets; ENSG00000162836; -.
DR PharmGKB; PA134930830; -.
DR VEuPathDB; HostDB:ENSG00000162836; -.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000158408; -.
DR HOGENOM; CLU_030431_5_1_1; -.
DR InParanoid; Q9NPH0; -.
DR OMA; SWPPFTS; -.
DR OrthoDB; 1221585at2759; -.
DR PhylomeDB; Q9NPH0; -.
DR TreeFam; TF318821; -.
DR BRENDA; 3.1.3.106; 2681.
DR PathwayCommons; Q9NPH0; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q9NPH0; -.
DR BioGRID-ORCS; 51205; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; ACP6; human.
DR GeneWiki; ACP6; -.
DR GenomeRNAi; 51205; -.
DR Pharos; Q9NPH0; Tbio.
DR PRO; PR:Q9NPH0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NPH0; protein.
DR Bgee; ENSG00000162836; Expressed in right uterine tube and 172 other tissues.
DR ExpressionAtlas; Q9NPH0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Hydrolase;
KW Lipid metabolism; Mitochondrion; Phospholipid metabolism;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 33..428
FT /note="Lysophosphatidic acid phosphatase type 6"
FT /id="PRO_0000023965"
FT REGION 58..168
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23807634"
FT ACT_SITE 335
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:23807634"
FT VAR_SEQ 261..271
FT /note="AHNLPSCPMLK -> EKMGSCRFHGS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_014121"
FT VAR_SEQ 272..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_014122"
FT VARIANT 316
FT /note="M -> V (in dbSNP:rs6593795)"
FT /id="VAR_022678"
FT MUTAGEN 58
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 59
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10506173,
FT ECO:0000269|PubMed:23807634"
FT MUTAGEN 62
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 106
FT /note="Y->F: Decreases enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 110
FT /note="Y->F: Decreases enzyme activity."
FT MUTAGEN 168
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 257
FT /note="A->F,L: Decreases enzyme activity by interfering
FT with water access to the active site cavity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 257
FT /note="A->W: Abolishes enzyme activity by interfering with
FT water access to the active site cavity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 285
FT /note="S->W: Decreases activity toward substrates with
FT medium and long aliphatic chains, but not toward substrates
FT with short aliphatic chains."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 289
FT /note="L->W: Decreases activity toward substrates with
FT medium and long aliphatic chains, but not toward substrates
FT with short aliphatic chains."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 334
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT MUTAGEN 335
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:23807634"
FT CONFLICT 428
FT /note="E -> D (in Ref. 10; CAG33382)"
FT /evidence="ECO:0000305"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:4JOD"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4JOC"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4JOC"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 294..314
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4JOD"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:4JOD"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:4JOB"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4JOC"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:4JOB"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:4JOB"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:4JOB"
SQ SEQUENCE 428 AA; 48886 MW; 3CA08CFD1BB44BFA CRC64;
MITGVFSMRL WTPVGVLTSL AYCLHQRRVA LAELQEADGQ CPVDRSLLKL KMVQVVFRHG
ARSPLKPLPL EEQVEWNPQL LEVPPQTQFD YTVTNLAGGP KPYSPYDSQY HETTLKGGMF
AGQLTKVGMQ QMFALGERLR KNYVEDIPFL SPTFNPQEVF IRSTNIFRNL ESTRCLLAGL
FQCQKEGPII IHTDEADSEV LYPNYQSCWS LRQRTRGRRQ TASLQPGISE DLKKVKDRMG
IDSSDKVDFF ILLDNVAAEQ AHNLPSCPML KRFARMIEQR AVDTSLYILP KEDRESLQMA
VGPFLHILES NLLKAMDSAT APDKIRKLYL YAAHDVTFIP LLMTLGIFDH KWPPFAVDLT
MELYQHLESK EWFVQLYYHG KEQVPRGCPD GLCPLDMFLN AMSVYTLSPE KYHALCSQTQ
VMEVGNEE
