LIPG_HUMAN
ID LIPG_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 03-AUG-2022, entry version 206.
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:2243091, PubMed:10358049). 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 = (9Z)-
CC octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + 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 H(+) + octanoate; 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 P07098-3; 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; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/lipf/";
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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_001198828.1. [P07098-2]
DR RefSeq; NP_001185758.1; NM_001198829.1. [P07098-3]
DR RefSeq; NP_001185759.1; NM_001198830.1. [P07098-4]
DR RefSeq; NP_004181.1; NM_004190.3. [P07098-1]
DR RefSeq; XP_011538613.1; XM_011540311.1. [P07098-1]
DR PDB; 1HLG; X-ray; 3.00 A; A/B=28-398.
DR PDBsum; 1HLG; -.
DR AlphaFoldDB; P07098; -.
DR SMR; P07098; -.
DR BioGRID; 114085; 14.
DR IntAct; P07098; 8.
DR STRING; 9606.ENSP00000377900; -.
DR ChEMBL; CHEMBL1796; -.
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 GlyGen; P07098; 4 sites.
DR iPTMnet; P07098; -.
DR PhosphoSitePlus; P07098; -.
DR BioMuta; LIPF; -.
DR DMDM; 126306; -.
DR MassIVE; P07098; -.
DR PaxDb; P07098; -.
DR PeptideAtlas; P07098; -.
DR PRIDE; P07098; -.
DR ProteomicsDB; 25718; -.
DR ProteomicsDB; 51948; -. [P07098-1]
DR ProteomicsDB; 65595; -.
DR Antibodypedia; 30193; 211 antibodies from 28 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 CTD; 8513; -.
DR DisGeNET; 8513; -.
DR GeneCards; LIPF; -.
DR HGNC; HGNC:6622; LIPF.
DR HPA; ENSG00000182333; Tissue enriched (stomach).
DR MIM; 601980; gene.
DR neXtProt; NX_P07098; -.
DR OpenTargets; ENSG00000182333; -.
DR PharmGKB; PA30394; -.
DR VEuPathDB; HostDB:ENSG00000182333; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000161066; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; P07098; -.
DR OMA; HKYWPTY; -.
DR OrthoDB; 1387662at2759; -.
DR PhylomeDB; P07098; -.
DR TreeFam; TF315485; -.
DR PathwayCommons; P07098; -.
DR Reactome; R-HSA-192456; Digestion of dietary lipid.
DR SignaLink; P07098; -.
DR BioGRID-ORCS; 8513; 7 hits in 1066 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 95 other tissues.
DR Genevisible; P07098; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; NAS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR039097; Gastric_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF15; PTHR11005:SF15; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; 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 142..147
FT /evidence="ECO:0007829|PDB:1HLG"
FT HELIX 149..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 381..384
FT /evidence="ECO:0007829|PDB:1HLG"
FT HELIX 386..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
