ID   LIPF_HUMAN              Reviewed;         398 AA.
AC   P07098; B7Z723; F5H1P4; Q2M1P6; Q5VXI7; Q5VXI8; Q658L8;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-SEP-2026, entry version 224.
DE   RecName: Full=Gastric triacylglycerol lipase;
DE            Short=GL;
DE            Short=Gastric lipase;
DE            EC=3.1.1.3 {ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091};
DE   Flags: Precursor;
GN   Name=LIPF;
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).
RX   PubMed=3304425; DOI=10.1016/0167-4781(87)90083-2;
RA   Bodmer M.W., Angal S., Yarranton G.T., Harris T.J.R., Lyons A., King D.J.,
RA   Pieroni G., Riviere C., Verger R., Lowe P.A.;
RT   "Molecular cloning of a human gastric lipase and expression of the enzyme
RT   in yeast.";
RL   Biochim. Biophys. Acta 909:237-244(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Stomach;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Stomach;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-161; ILE-224 AND
RP   THR-348.
RG   NIEHS SNPs program;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-161.
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   [8]
RP   PROTEIN SEQUENCE OF 20-45.
RX   PubMed=2753032; DOI=10.1111/j.1432-1033.1989.tb14855.x;
RA   Bernbaeck S., Blaeckberg L.;
RT   "Human gastric lipase. The N-terminal tetrapeptide is essential for lipid
RT   binding and lipase activity.";
RL   Eur. J. Biochem. 182:495-499(1989).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2243091; DOI=10.1016/s0021-9258(17)30500-8;
RA   Rogalska E., Ransac S., Verger R.;
RT   "Stereoselectivity of lipases. II. Stereoselective hydrolysis of
RT   triglycerides by gastric and pancreatic lipases.";
RL   J. Biol. Chem. 265:20271-20276(1990).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, ACTIVE
RP   SITES, GLYCOSYLATION AT ASN-34; ASN-99; ASN-271 AND ASN-327, AND DISULFIDE
RP   BOND.
RX   PubMed=10358049; DOI=10.1074/jbc.274.24.16995;
RA   Roussel A., Canaan S., Egloff M.P., Riviere M., Dupuis L., Verger R.,
RA   Cambillau C.;
RT   "Crystal structure of human gastric lipase and model of lysosomal acid
RT   lipase, two lipolytic enzymes of medical interest.";
RL   J. Biol. Chem. 274:16995-17002(1999).
CC   -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free
CC       fatty acids, diacylglycerol, monoacylglycerol, and glycerol
CC       (PubMed:10358049, PubMed:2243091). Shows a preferential hydrolysis at
CC       the sn-3 position of triacylglycerol (PubMed:2243091).
CC       {ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC         Evidence={ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = 1,2-di-(9Z-
CC         octadecenoyl)-sn-glycerol + (9Z)-octadecenoate + H(+);
CC         Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753;
CC         Evidence={ECO:0000269|PubMed:2243091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932;
CC         Evidence={ECO:0000305|PubMed:2243091};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol +
CC         octanoate + H(+); Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC         ChEBI:CHEBI:76979; Evidence={ECO:0000269|PubMed:2243091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048;
CC         Evidence={ECO:0000305|PubMed:2243091};
CC   -!- INTERACTION:
CC       P07098; Q6UWE0: LRSAM1; NbExp=2; IntAct=EBI-3386192, EBI-720984;
CC       P07098-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11979889, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P07098-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P07098-2; Sequence=VSP_047296;
CC       Name=3;
CC         IsoId=P07098-3; Sequence=VSP_047295;
CC       Name=4;
CC         IsoId=P07098-4; Sequence=VSP_047295, VSP_047296;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA29414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X05997; CAA29413.1; -; mRNA.
DR   EMBL; X05997; CAA29414.1; ALT_INIT; mRNA.
DR   EMBL; AK301310; BAH13457.1; -; mRNA.
DR   EMBL; AK301320; BAH13459.1; -; mRNA.
DR   EMBL; AK312940; BAG35782.1; -; mRNA.
DR   EMBL; AL833751; CAH56244.1; -; mRNA.
DR   EMBL; AY631869; AAT38115.1; -; Genomic_DNA.
DR   EMBL; AL358532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW50162.1; -; Genomic_DNA.
DR   EMBL; BC112272; AAI12273.1; -; mRNA.
DR   EMBL; BC113711; AAI13712.1; -; mRNA.
DR   CCDS; CCDS55718.1; -. [P07098-3]
DR   CCDS; CCDS55719.1; -. [P07098-2]
DR   CCDS; CCDS65896.1; -. [P07098-4]
DR   CCDS; CCDS7389.1; -. [P07098-1]
DR   PIR; S07145; S07145.
DR   RefSeq; NP_001185757.1; NM_001198828.2. [P07098-2]
DR   RefSeq; NP_001185758.1; NM_001198829.2. [P07098-3]
DR   RefSeq; NP_001185759.1; NM_001198830.2. [P07098-4]
DR   RefSeq; NP_004181.1; NM_004190.4. [P07098-1]
DR   RefSeq; XP_011538613.1; XM_011540311.2. [P07098-1]
DR   RefSeq; XP_054223025.1; XM_054367050.1. [P07098-1]
DR   PDB; 1HLG; X-ray; 3.00 A; A/B=28-398.
DR   AlphaFoldDB; P07098; -.
DR   SMR; P07098; -.
DR   BioGRID; 114085; 18.
DR   CORUM; P07098; -.
DR   FunCoup; P07098; 105.
DR   IntAct; P07098; 10.
DR   NDEx; IQUERY-CP-LIPF; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000377900; -.
DR   ChEMBL; CHEMBL1796; -.
DR   DrugBank; DB06586; Cetilistat.
DR   DrugBank; DB01083; Orlistat.
DR   DrugBank; DB02457; Undecyl-Phosphinic Acid Butyl Ester.
DR   DrugCentral; P07098; -.
DR   SwissLipids; SLP:000000524; -.
DR   ESTHER; human-LIPF; Acidic_Lipase.
DR   GlyCosmos; P07098; 4 sites, No reported glycans.
DR   GlyGen; P07098; 4 sites.
DR   iPTMnet; P07098; -.
DR   PhosphoSitePlus; P07098; -.
DR   BioMuta; LIPF; -.
DR   DMDM; 126306; -.
DR   MassIVE; P07098; -.
DR   PaxDb; 9606-ENSP00000377900; -.
DR   PeptideAtlas; P07098; -.
DR   ProteomicsDB; 25718; -.
DR   ProteomicsDB; 51948; -. [P07098-1]
DR   ProteomicsDB; 65595; -.
DR   Antibodypedia; 30193; 214 antibodies from 29 providers.
DR   DNASU; 8513; -.
DR   Ensembl; ENST00000238983.9; ENSP00000238983.5; ENSG00000182333.15. [P07098-1]
DR   Ensembl; ENST00000355843.2; ENSP00000348101.3; ENSG00000182333.15. [P07098-4]
DR   Ensembl; ENST00000394375.7; ENSP00000377900.3; ENSG00000182333.15. [P07098-3]
DR   Ensembl; ENST00000608620.5; ENSP00000477140.1; ENSG00000182333.15. [P07098-2]
DR   GeneID; 8513; -.
DR   KEGG; hsa:8513; -.
DR   MANE-Select; ENST00000238983.9; ENSP00000238983.5; NM_004190.4; NP_004181.1.
DR   UCSC; uc001kfg.3; human. [P07098-1]
DR   AGR; HGNC:6622; -.
DR   ClinPGx; PA30394; -.
DR   CTD; 8513; -.
DR   DisGeNET; 8513; -.
DR   GeneCards; LIPF; -.
DR   HGNC; HGNC:6622; LIPF.
DR   HPA; ENSG00000182333; Tissue enriched (stomach).
DR   MIM; 601980; gene.
DR   OpenTargets; ENSG00000182333; -.
DR   VEuPathDB; HostDB:ENSG00000182333; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   GeneTree; ENSGT00940000161066; -.
DR   HOGENOM; CLU_010974_0_0_1; -.
DR   InParanoid; P07098; -.
DR   OMA; WSRRNLY; -.
DR   OrthoDB; 9974421at2759; -.
DR   PAN-GO; P07098; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P07098; -.
DR   PathwayCommons; P07098; -.
DR   Reactome; R-HSA-192456; Digestion of dietary lipid.
DR   SignaLink; P07098; -.
DR   Agora; ENSG00000182333; -.
DR   BioGRID-ORCS; 8513; 8 hits in 1152 CRISPR screens.
DR   ChiTaRS; LIPF; human.
DR   EvolutionaryTrace; P07098; -.
DR   GenomeRNAi; 8513; -.
DR   Pharos; P07098; Tclin.
DR   PRO; PR:P07098; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P07098; protein.
DR   Bgee; ENSG00000182333; Expressed in cardia of stomach and 97 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0008289; F:lipid binding; NAS:UniProtKB.
DR   GO; GO:0016615; F:malate dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0006641; P:triglyceride metabolic process; NAS:UniProtKB.
DR   FunFam; 3.40.50.1820:FF:000012; Lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PDBsum; 1HLG; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Proteomics identification; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:2753032"
FT   CHAIN           20..398
FT                   /note="Gastric triacylglycerol lipase"
FT                   /id="PRO_0000017766"
FT   DOMAIN          78..377
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   ACT_SITE        372
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   DISULFID        246..255
FT                   /evidence="ECO:0000269|PubMed:10358049"
FT   VAR_SEQ         1
FT                   /note="M -> MFSNANSRSKM (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_047295"
FT   VAR_SEQ         75..107
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_047296"
FT   VARIANT         161
FT                   /note="T -> A (in dbSNP:rs814628)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT                   /id="VAR_011947"
FT   VARIANT         224
FT                   /note="F -> I (in dbSNP:rs6586145)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020565"
FT   VARIANT         348
FT                   /note="P -> T (in dbSNP:rs17333991)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020566"
FT   CONFLICT        350
FT                   /note="D -> N (in Ref. 2; BAH13459)"
FT                   /evidence="ECO:0000305"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           35..41
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           90..94
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           102..108
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           150..161
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           173..184
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          192..199
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   TURN            234..239
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           241..249
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           258..263
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           275..279
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           288..300
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           311..318
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          335..340
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           348..357
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   STRAND          361..367
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           382..386
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   HELIX           387..393
FT                   /evidence="ECO:0007829|PDB:1HLG"
FT   TURN            394..397
FT                   /evidence="ECO:0007829|PDB:1HLG"
SQ   SEQUENCE   398 AA;  45238 MW;  CD3EE1621C014F0F CRC64;
     MWLLLTMASL ISVLGTTHGL FGKLHPGSPE VTMNISQMIT YWGYPNEEYE VVTEDGYILE
     VNRIPYGKKN SGNTGQRPVV FLQHGLLASA TNWISNLPNN SLAFILADAG YDVWLGNSRG
     NTWARRNLYY SPDSVEFWAF SFDEMAKYDL PATIDFIVKK TGQKQLHYVG HSQGTTIGFI
     AFSTNPSLAK RIKTFYALAP VATVKYTKSL INKLRFVPQS LFKFIFGDKI FYPHNFFDQF
     LATEVCSREM LNLLCSNALF IICGFDSKNF NTSRLDVYLS HNPAGTSVQN MFHWTQAVKS
     GKFQAYDWGS PVQNRMHYDQ SQPPYYNVTA MNVPIAVWNG GKDLLADPQD VGLLLPKLPN
     LIYHKEIPFY NHLDFIWAMD APQEVYNDIV SMISEDKK
//