ID   GPD1L_HUMAN             Reviewed;         351 AA.
AC   Q8N335; A8K9U3; Q14702; Q9BRM5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            Short=GPD1-L;
DE            EC=1.1.1.8 {ECO:0000269|PubMed:19666841};
GN   Name=GPD1L {ECO:0000312|HGNC:HGNC:28956}; Synonyms=KIAA0089;
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 [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA   Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III. The
RT   coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
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   [5]
RP   FUNCTION, CHARACTERIZATION OF VARIANTS BRGDA2 LYS-83 AND VAL-280,
RP   INTERACTION WITH SCN5A, AND CATALYTIC ACTIVITY.
RX   PubMed=19666841; DOI=10.1152/ajpheart.00513.2009;
RA   Valdivia C.R., Ueda K., Ackerman M.J., Makielski J.C.;
RT   "GPD1L links redox state to cardiac excitability by PKC-dependent
RT   phosphorylation of the sodium channel SCN5A.";
RL   Am. J. Physiol. 297:H1446-H1452(2009).
RN   [6]
RP   FUNCTION, AND CHARACTERIZATION OF VARIANT BRGDA2 VAL-280.
RX   PubMed=19745168; DOI=10.1161/circresaha.109.197277;
RA   Liu M., Sanyal S., Gao G., Gurung I.S., Zhu X., Gaconnet G., Kerchner L.J.,
RA   Shang L.L., Huang C.L., Grace A., London B., Dudley S.C. Jr.;
RT   "Cardiac Na+ current regulation by pyridine nucleotides.";
RL   Circ. Res. 105:737-745(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-349 IN COMPLEX WITH NAD AND
RP   PHOSPHATE IONS.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human glycerol-3-phosphate dehydrogenase 1-like
RT   protein.";
RL   Submitted (MAY-2007) to the PDB data bank.
RN   [9]
RP   VARIANTS BRGDA2 LYS-83; VAL-124 AND CYS-273, AND CHARACTERIZATION OF
RP   VARIANTS BRGDA2 LYS-83; VAL-124 AND CYS-273.
RX   PubMed=17967976; DOI=10.1161/circulationaha.107.704627;
RA   Van Norstrand D.W., Valdivia C.R., Tester D.J., Ueda K., London B.,
RA   Makielski J.C., Ackerman M.J.;
RT   "Molecular and functional characterization of novel glycerol-3-phosphate
RT   dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death
RT   syndrome.";
RL   Circulation 116:2253-2259(2007).
RN   [10]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT BRGDA2 VAL-280, AND
RP   CHARACTERIZATION OF VARIANT BRGDA2 VAL-280.
RX   PubMed=17967977; DOI=10.1161/circulationaha.107.703330;
RA   London B., Michalec M., Mehdi H., Zhu X., Kerchner L., Sanyal S.,
RA   Viswanathan P.C., Pfahnl A.E., Shang L.L., Madhusudanan M., Baty C.J.,
RA   Lagana S., Aleong R., Gutmann R., Ackerman M.J., McNamara D.M., Weiss R.,
RA   Dudley S.C. Jr.;
RT   "Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L)
RT   decreases cardiac Na+ current and causes inherited arrhythmias.";
RL   Circulation 116:2260-2268(2007).
CC   -!- FUNCTION: Plays a role in regulating cardiac sodium current; decreased
CC       enzymatic activity with resulting increased levels of glycerol 3-
CC       phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway,
CC       may ultimately lead to decreased sodium current; cardiac sodium current
CC       may also be reduced due to alterations of NAD(H) balance induced by
CC       DPD1L. {ECO:0000269|PubMed:19666841, ECO:0000269|PubMed:19745168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC         Evidence={ECO:0000269|PubMed:19666841};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC         Evidence={ECO:0000269|PubMed:19666841};
CC   -!- SUBUNIT: Interacts with SCN5A. {ECO:0000269|PubMed:19666841,
CC       ECO:0000269|Ref.8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17967977}.
CC       Note=Localized to the region of the plasma membrane.
CC   -!- TISSUE SPECIFICITY: Most highly expressed in heart tissue, with lower
CC       levels in the skeletal muscle, kidney, lung and other organs.
CC       {ECO:0000269|PubMed:17967977}.
CC   -!- DISEASE: Brugada syndrome 2 (BRGDA2) [MIM:611777]: A tachyarrhythmia
CC       characterized by right bundle branch block and ST segment elevation on
CC       an electrocardiogram (ECG). It can cause the ventricles to beat so fast
CC       that the blood is prevented from circulating efficiently in the body.
CC       When this situation occurs, the individual will faint and may die in a
CC       few minutes if the heart is not reset. {ECO:0000269|PubMed:17967976,
CC       ECO:0000269|PubMed:17967977, ECO:0000269|PubMed:19666841,
CC       ECO:0000269|PubMed:19745168}. Note=The gene represented in this entry
CC       may be involved in disease pathogenesis.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA07648.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D42047; BAA07648.1; ALT_INIT; mRNA.
DR   EMBL; AK292808; BAF85497.1; -; mRNA.
DR   EMBL; CH471055; EAW64422.1; -; Genomic_DNA.
DR   EMBL; BC006168; AAH06168.1; -; mRNA.
DR   EMBL; BC028726; AAH28726.1; -; mRNA.
DR   CCDS; CCDS33729.1; -.
DR   RefSeq; NP_055956.1; NM_015141.3.
DR   PDB; 2PLA; X-ray; 2.51 A; A/B=1-349.
DR   PDBsum; 2PLA; -.
DR   AlphaFoldDB; Q8N335; -.
DR   SMR; Q8N335; -.
DR   BioGRID; 116783; 58.
DR   IntAct; Q8N335; 12.
DR   MINT; Q8N335; -.
DR   STRING; 9606.ENSP00000282541; -.
DR   SwissLipids; SLP:000000146; -.
DR   GlyGen; Q8N335; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N335; -.
DR   MetOSite; Q8N335; -.
DR   PhosphoSitePlus; Q8N335; -.
DR   SwissPalm; Q8N335; -.
DR   BioMuta; GPD1L; -.
DR   DMDM; 74750945; -.
DR   EPD; Q8N335; -.
DR   jPOST; Q8N335; -.
DR   MassIVE; Q8N335; -.
DR   MaxQB; Q8N335; -.
DR   PaxDb; 9606-ENSP00000282541; -.
DR   PeptideAtlas; Q8N335; -.
DR   ProteomicsDB; 71759; -.
DR   Pumba; Q8N335; -.
DR   Antibodypedia; 27707; 189 antibodies from 25 providers.
DR   DNASU; 23171; -.
DR   Ensembl; ENST00000282541.10; ENSP00000282541.6; ENSG00000152642.11.
DR   GeneID; 23171; -.
DR   KEGG; hsa:23171; -.
DR   MANE-Select; ENST00000282541.10; ENSP00000282541.6; NM_015141.4; NP_055956.1.
DR   UCSC; uc003cew.4; human.
DR   AGR; HGNC:28956; -.
DR   CTD; 23171; -.
DR   DisGeNET; 23171; -.
DR   GeneCards; GPD1L; -.
DR   GeneReviews; GPD1L; -.
DR   HGNC; HGNC:28956; GPD1L.
DR   HPA; ENSG00000152642; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; GPD1L; -.
DR   MIM; 611777; phenotype.
DR   MIM; 611778; gene.
DR   neXtProt; NX_Q8N335; -.
DR   OpenTargets; ENSG00000152642; -.
DR   Orphanet; 130; Brugada syndrome.
DR   PharmGKB; PA134986345; -.
DR   VEuPathDB; HostDB:ENSG00000152642; -.
DR   eggNOG; KOG2711; Eukaryota.
DR   GeneTree; ENSGT00390000003114; -.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q8N335; -.
DR   OMA; YDTPPMD; -.
DR   OrthoDB; 3675564at2759; -.
DR   PhylomeDB; Q8N335; -.
DR   TreeFam; TF300836; -.
DR   PathwayCommons; Q8N335; -.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   SignaLink; Q8N335; -.
DR   BioGRID-ORCS; 23171; 10 hits in 1152 CRISPR screens.
DR   ChiTaRS; GPD1L; human.
DR   EvolutionaryTrace; Q8N335; -.
DR   GenomeRNAi; 23171; -.
DR   Pharos; Q8N335; Tbio.
DR   PRO; PR:Q8N335; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8N335; Protein.
DR   Bgee; ENSG00000152642; Expressed in biceps brachii and 209 other cell types or tissues.
DR   ExpressionAtlas; Q8N335; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0019674; P:NAD metabolic process; IMP:BHF-UCL.
DR   GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:BHF-UCL.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:BHF-UCL.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:BHF-UCL.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IMP:BHF-UCL.
DR   GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IMP:BHF-UCL.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF7; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1-LIKE PROTEIN; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; Q8N335; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Brugada syndrome; Cytoplasm; Disease variant; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Glycerol-3-phosphate dehydrogenase 1-like protein"
FT                   /id="PRO_0000286511"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT   BINDING         12..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         271..272
FT                   /ligand="substrate"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|Ref.8"
FT   BINDING         300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   VARIANT         83
FT                   /note="E -> K (in BRGDA2; uncertain significance; decreased
FT                   enzymatic activity and significant reduction of sodium
FT                   current when coexpressed with SCN5A in HEK cells;
FT                   dbSNP:rs72552292)"
FT                   /evidence="ECO:0000269|PubMed:17967976,
FT                   ECO:0000269|PubMed:19666841"
FT                   /id="VAR_044044"
FT   VARIANT         124
FT                   /note="I -> V (in BRGDA2; uncertain significance;
FT                   significant reduction of sodium current when coexpressed
FT                   with SCN5A in HEK cells; dbSNP:rs72552293)"
FT                   /evidence="ECO:0000269|PubMed:17967976"
FT                   /id="VAR_044045"
FT   VARIANT         178
FT                   /note="L -> F (in dbSNP:rs35447795)"
FT                   /id="VAR_032114"
FT   VARIANT         273
FT                   /note="R -> C (in BRGDA2; uncertain significance;
FT                   significant reduction of sodium current when coexpressed
FT                   with SCN5A in HEK cells; dbSNP:rs72552294)"
FT                   /evidence="ECO:0000269|PubMed:17967976"
FT                   /id="VAR_044046"
FT   VARIANT         280
FT                   /note="A -> V (in BRGDA2; uncertain significance; decreased
FT                   enzymatic activity; affects SCN5A membrane expression;
FT                   reduction of sodium current when coexpressed with SCN5A in
FT                   HEK cells; dbSNP:rs72552291)"
FT                   /evidence="ECO:0000269|PubMed:17967977,
FT                   ECO:0000269|PubMed:19666841, ECO:0000269|PubMed:19745168"
FT                   /id="VAR_044047"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           52..59
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           81..85
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           100..107
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           155..159
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           173..183
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           196..218
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           223..244
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           260..269
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           271..282
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           286..294
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           301..315
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           322..332
FT                   /evidence="ECO:0007829|PDB:2PLA"
FT   HELIX           339..345
FT                   /evidence="ECO:0007829|PDB:2PLA"
SQ   SEQUENCE   351 AA;  38419 MW;  74C3B27EEB41DE89 CRC64;
     MAAAPLKVCI VGSGNWGSAV AKIIGNNVKK LQKFASTVKM WVFEETVNGR KLTDIINNDH
     ENVKYLPGHK LPENVVAMSN LSEAVQDADL LVFVIPHQFI HRICDEITGR VPKKALGITL
     IKGIDEGPEG LKLISDIIRE KMGIDISVLM GANIANEVAA EKFCETTIGS KVMENGLLFK
     ELLQTPNFRI TVVDDADTVE LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF
     ARIFCKGQVS TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KEMLNGQKLQ
     GPQTSAEVYR ILKQKGLLDK FPLFTAVYQI CYESRPVQEM LSCLQSHPEH T
//