GPD1L_HUMAN
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 03-AUG-2022, entry version 164.
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; 54.
DR IntAct; Q8N335; 11.
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 BioMuta; GPD1L; -.
DR DMDM; 74750945; -.
DR EPD; Q8N335; -.
DR jPOST; Q8N335; -.
DR MassIVE; Q8N335; -.
DR MaxQB; Q8N335; -.
DR PaxDb; Q8N335; -.
DR PeptideAtlas; Q8N335; -.
DR PRIDE; Q8N335; -.
DR ProteomicsDB; 71759; -.
DR Antibodypedia; 27707; 166 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 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; FIHKVCD; -.
DR OrthoDB; 476066at2759; -.
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 1074 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 207 other tissues.
DR ExpressionAtlas; Q8N335; baseline and differential.
DR Genevisible; Q8N335; HS.
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:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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; 1.10.1040.10; -; 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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
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; unknown pathological
FT significance; decreased enzymatic activity and significant
FT reduction of sodium current when coexpressed with SCN5A in
FT HEK cells; 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; unknown pathological
FT significance; significant reduction of sodium current when
FT coexpressed 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; unknown pathological
FT significance; significant reduction of sodium current when
FT coexpressed 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; unknown pathological
FT significance; decreased enzymatic activity; affects SCN5A
FT membrane expression; reduction of sodium current when
FT coexpressed with SCN5A in 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
