G3PT_HUMAN
ID G3PT_HUMAN Reviewed; 408 AA.
AC O14556; B2RC82; O60823; Q6JTT9; Q9HCU6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific;
DE EC=1.2.1.12;
DE AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2;
DE Short=GAPDH-2;
DE AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase;
GN Name=GAPDHS; Synonyms=GAPD2, GAPDH2, GAPDS; ORFNames=HSD-35, HSD35;
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].
RC TISSUE=Testis;
RA McLaughlin E.A., Hall L.;
RT "Nucleotide sequence of human testis-specific glyceraldehyde-3-phosphate
RT dehydrogenase (GAPDH-2) cDNA.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10714828;
RA Welch J.E., Brown P.L., O'Brien D.A., Magyar P.L., Bunch D.O., Mori C.,
RA Eddy E.M.;
RT "Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed
RT specifically in spermatogenic cells.";
RL J. Androl. 21:328-338(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Zhao H., Miao S.Y., Zhang X.D., Liang G., Qiao Y., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP INTERACTION WITH ARRB2.
RX PubMed=16820410; DOI=10.1242/jcs.03046;
RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
RT "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa.";
RL J. Cell Sci. 119:3047-3056(2006).
RN [8]
RP DOMAIN N-TERMINAL EXTENSION, AND SUBUNIT.
RX PubMed=18298375; DOI=10.1134/s0006297908020107;
RA Shchutskaya Y.Y., Elkina Y.L., Kuravsky M.L., Bragina E.E.,
RA Schmalhausen E.V.;
RT "Investigation of glyceraldehyde-3-phosphate dehydrogenase from human
RT sperms.";
RL Biochemistry (Mosc.) 73:185-191(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 69-407 IN COMPLEX WITH NAD AND
RP GLYCEROL, ACTIVE SITE, AND SUBUNIT.
RX PubMed=21269272; DOI=10.1042/bj20101442;
RA Chaikuad A., Shafqat N., Al-Mokhtar R., Cameron G., Clarke A.R.,
RA Brady R.L., Oppermann U., Frayne J., Yue W.W.;
RT "Structure and kinetic characterization of human sperm-specific
RT glyceraldehyde-3-phosphate dehydrogenase, GAPDS.";
RL Biochem. J. 435:401-409(2011).
CC -!- FUNCTION: May play an important role in regulating the switch between
CC different pathways for energy production during spermiogenesis and in
CC the spermatozoon. Required for sperm motility and male fertility (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. Interacts with ARRB2; the interaction is
CC detected in the nucleus upon OR1D2 stimulation.
CC {ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:18298375,
CC ECO:0000269|PubMed:21269272}.
CC -!- INTERACTION:
CC O14556; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1057431, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- DOMAIN: The testis-specific N-terminal extension mediates tight
CC association with the cytoskeletal fibrous sheath of the spermatozoa
CC flagellum, possibly via interchain disulfide-bonding of Cys-21 with
CC sheath components. {ECO:0000269|PubMed:18298375}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ005371; CAA06501.1; -; mRNA.
DR EMBL; AF216641; AAF87970.1; -; Genomic_DNA.
DR EMBL; AF216631; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216632; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216633; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216634; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216635; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216636; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216637; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216638; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216639; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AF216640; AAF87970.1; JOINED; Genomic_DNA.
DR EMBL; AY306129; AAQ75383.1; -; mRNA.
DR EMBL; AK314980; BAG37479.1; -; mRNA.
DR EMBL; AC002389; AAB64181.1; -; Genomic_DNA.
DR EMBL; BC036373; AAH36373.1; -; mRNA.
DR CCDS; CCDS12465.1; -.
DR RefSeq; NP_055179.1; NM_014364.4.
DR PDB; 3H9E; X-ray; 1.72 A; O/P=69-407.
DR PDB; 3PFW; X-ray; 2.15 A; O/P=69-407.
DR PDB; 5C7L; X-ray; 1.86 A; O/R=74-407.
DR PDB; 5C7O; X-ray; 1.73 A; O/P=74-407.
DR PDBsum; 3H9E; -.
DR PDBsum; 3PFW; -.
DR PDBsum; 5C7L; -.
DR PDBsum; 5C7O; -.
DR AlphaFoldDB; O14556; -.
DR SMR; O14556; -.
DR BioGRID; 117681; 234.
DR IntAct; O14556; 54.
DR MINT; O14556; -.
DR STRING; 9606.ENSP00000222286; -.
DR DrugBank; DB02205; (+)-Rutamarin alcohol.
DR DrugBank; DB04477; 2'-Deoxy-2'-[(3,5-dimethoxybenzoyl)amino]-N-[(1R)-1,2,3,4-tetrahydro-1-naphthalenyl]adenosine.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB03331; N-naphthalen-1-ylmethyl-2'-[3,5-dimethoxybenzamido]-2'-deoxy-adenosine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; O14556; -.
DR MetOSite; O14556; -.
DR PhosphoSitePlus; O14556; -.
DR BioMuta; GAPDHS; -.
DR EPD; O14556; -.
DR jPOST; O14556; -.
DR MassIVE; O14556; -.
DR MaxQB; O14556; -.
DR PaxDb; O14556; -.
DR PeptideAtlas; O14556; -.
DR PRIDE; O14556; -.
DR ProteomicsDB; 48082; -.
DR Antibodypedia; 29443; 323 antibodies from 36 providers.
DR DNASU; 26330; -.
DR Ensembl; ENST00000222286.9; ENSP00000222286.3; ENSG00000105679.9.
DR GeneID; 26330; -.
DR KEGG; hsa:26330; -.
DR MANE-Select; ENST00000222286.9; ENSP00000222286.3; NM_014364.5; NP_055179.1.
DR UCSC; uc002oaf.2; human.
DR CTD; 26330; -.
DR DisGeNET; 26330; -.
DR GeneCards; GAPDHS; -.
DR HGNC; HGNC:24864; GAPDHS.
DR HPA; ENSG00000105679; Tissue enriched (testis).
DR MIM; 609169; gene.
DR neXtProt; NX_O14556; -.
DR OpenTargets; ENSG00000105679; -.
DR PharmGKB; PA134934259; -.
DR VEuPathDB; HostDB:ENSG00000105679; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000160272; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; O14556; -.
DR OMA; NAKVLAW; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; O14556; -.
DR TreeFam; TF300533; -.
DR BioCyc; MetaCyc:HS02793-MON; -.
DR BRENDA; 1.2.1.12; 2681.
DR PathwayCommons; O14556; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SignaLink; O14556; -.
DR SIGNOR; O14556; -.
DR UniPathway; UPA00109; UER00184.
DR BioGRID-ORCS; 26330; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; GAPDHS; human.
DR EvolutionaryTrace; O14556; -.
DR GeneWiki; GAPDHS; -.
DR GenomeRNAi; 26330; -.
DR Pharos; O14556; Tbio.
DR PRO; PR:O14556; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14556; protein.
DR Bgee; ENSG00000105679; Expressed in left testis and 108 other tissues.
DR ExpressionAtlas; O14556; baseline and differential.
DR Genevisible; O14556; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0045821; P:positive regulation of glycolytic process; TAS:UniProtKB.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..408
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, testis-
FT specific"
FT /id="PRO_0000145502"
FT REGION 1..73
FT /note="Testis-specific N-terminal extension"
FT REGION 19..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009,
FT ECO:0000269|PubMed:21269272"
FT BINDING 85..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT BINDING 223..225
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 283..284
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21269272"
FT SITE 251
FT /note="Activates thiol group during catalysis"
FT VARIANT 110
FT /note="D -> N (in dbSNP:rs2285514)"
FT /id="VAR_049219"
FT CONFLICT 220
FT /note="S -> SVRAHLGCFS (in Ref. 5; AAB64181)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="G -> V (in Ref. 3; AAQ75383)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> R (in Ref. 2; AAF87970)"
FT /evidence="ECO:0000305"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 340..345
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:3H9E"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3H9E"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:3H9E"
FT HELIX 390..407
FT /evidence="ECO:0007829|PDB:3H9E"
SQ SEQUENCE 408 AA; 44501 MW; 301F71C768CD95D8 CRC64;
MSKRDIVLTN VTVVQLLRQP CPVTRAPPPP EPKAEVEPQP QPEPTPVREE IKPPPPPLPP
HPATPPPKMV SVARELTVGI NGFGRIGRLV LRACMEKGVK VVAVNDPFID PEYMVYMFKY
DSTHGRYKGS VEFRNGQLVV DNHEISVYQC KEPKQIPWRA VGSPYVVEST GVYLSIQAAS
DHISAGAQRV VISAPSPDAP MFVMGVNEND YNPGSMNIVS NASCTTNCLA PLAKVIHERF
GIVEGLMTTV HSYTATQKTV DGPSRKAWRD GRGAHQNIIP ASTGAAKAVT KVIPELKGKL
TGMAFRVPTP DVSVVDLTCR LAQPAPYSAI KEAVKAAAKG PMAGILAYTE DEVVSTDFLG
DTHSSIFDAK AGIALNDNFV KLISWYDNEY GYSHRVVDLL RYMFSRDK
