ID NOCT_HUMAN Reviewed; 431 AA. AC Q9UK39; D3DNY5; Q14D51; Q9HD93; Q9HD94; Q9HD95; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 10-JUN-2026, entry version 181. DE RecName: Full=Nocturnin {ECO:0000312|HGNC:HGNC:14254}; DE EC=3.1.3.108 {ECO:0000269|PubMed:31147539}; DE AltName: Full=Carbon catabolite repression 4-like protein; DE Flags: Precursor; GN Name=NOCT {ECO:0000312|HGNC:HGNC:14254}; Synonyms=CCR4, CCRN4L, NOC; 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]. RX PubMed=10521507; DOI=10.1074/jbc.274.43.31068; RA Dupressoir A., Barbot W., Loireau M.-P., Heidmann T.; RT "Characterization of a mammalian gene related to the yeast CCR4 general RT transcription factor and revealed by transposon insertion."; RL J. Biol. Chem. 274:31068-31075(1999). RN [2] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 67-431. RA Wang Y., Osterbur D.L., Green C.B., Besharse J.C.; RT "Mammalian homologs of Xenopus nocturnin: conservation of structure and RT circadian regulation."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY. RX PubMed=22331129; DOI=10.1038/oby.2012.37; RA Hee S.W., Tsai S.H., Chang Y.C., Chang C.J., Yu I.S., Lee P.C., Lee W.J., RA Yun-Chia Chang E., Chuang L.M.; RT "The role of nocturnin in early adipogenesis and modulation of systemic RT insulin resistance in human."; RL Obesity 20:1558-1565(2012). RN [6] RP REVIEW. RX PubMed=22608110; DOI=10.1016/j.tem.2012.03.007; RA Stubblefield J.J., Terrien J., Green C.B.; RT "Nocturnin: at the crossroads of clocks and metabolism."; RL Trends Endocrinol. Metab. 23:326-333(2012). RN [7] {ECO:0007744|PDB:6BT1, ECO:0007744|PDB:6BT2} RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 120-431 IN COMPLEX WITH RP MAGNESIUM, FUNCTION, COFACTOR, LACK OF ADENYLASE ACTIVITY, AND MUTAGENESIS RP OF ASN-149; GLU-195; HIS-286; ASP-324; ASN-326; ASP-377 AND HIS-414. RX PubMed=29860338; DOI=10.1093/nar/gky412; RA Abshire E.T., Chasseur J., Bohn J.A., Del Rizzo P.A., Freddolino P.L., RA Goldstrohm A.C., Trievel R.C.; RT "The structure of human Nocturnin reveals a conserved ribonuclease domain RT that represses target transcript translation and abundance in cells."; RL Nucleic Acids Res. 46:6257-6270(2018). RN [8] {ECO:0007744|PDB:6MAL} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 122-431 IN COMPLEX WITH RP MAGNESIUM, AND LACK OF ADENYLASE ACTIVITY. RX PubMed=30389976; DOI=10.1038/s41598-018-34615-0; RA Estrella M.A., Du J., Korennykh A.; RT "Crystal Structure of Human Nocturnin Catalytic Domain."; RL Sci. Rep. 8:16294-16294(2018). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 122-431 IN COMPLEX WITH METAL AND RP NADPH, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ASP-160; GLU-195; LYS-219; HIS-286; LYS-288; ARG-290; RP LYS-365 AND ARG-367. RX PubMed=31147539; DOI=10.1038/s41467-019-10125-z; RA Estrella M.A., Du J., Chen L., Rath S., Prangley E., Chitrakar A., Aoki T., RA Schedl P., Rabinowitz J., Korennykh A.; RT "The metabolites NADP+ and NADPH are the targets of the circadian protein RT Nocturnin (Curled)."; RL Nat. Commun. 10:2367-2367(2019). CC -!- FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to CC NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference CC for NADPH over NADP(+) (PubMed:31147539). Represses translation and CC promotes degradation of target mRNA molecules (PubMed:29860338). Plays CC an important role in post-transcriptional regulation of metabolic genes CC under circadian control (By similarity). Exerts a rhythmic post- CC transcriptional control of genes necessary for metabolic functions CC including nutrient absorption, glucose/insulin sensitivity, lipid CC metabolism, adipogenesis, inflammation and osteogenesis (By CC similarity). Plays an important role in favoring adipogenesis over CC osteoblastogenesis and acts as a key regulator of the CC adipogenesis/osteogenesis balance (By similarity). Promotes CC adipogenesis by facilitating PPARG nuclear translocation which CC activates its transcriptional activity (By similarity). Regulates CC circadian expression of NOS2 in the liver and negatively regulates the CC circadian expression of IGF1 in the bone (By similarity). Critical for CC proper development of early embryos (By similarity). CC {ECO:0000250|UniProtKB:O35710, ECO:0000269|PubMed:29860338, CC ECO:0000269|PubMed:31147539}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + H2O = phosphate + NAD(+); Xref=Rhea:RHEA:28050, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:58349; EC=3.1.3.108; CC Evidence={ECO:0000269|PubMed:31147539}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051; CC Evidence={ECO:0000269|PubMed:31147539}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADPH + H2O = phosphate + NADH; Xref=Rhea:RHEA:60664, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:57945; EC=3.1.3.108; CC Evidence={ECO:0000269|PubMed:31147539}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665; CC Evidence={ECO:0000269|PubMed:31147539}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:30389976}; CC Note=Binds 2 magnesium ions, but the ions are only loosely bound to the CC protein. {ECO:0000269|PubMed:29860338}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=173 uM for NADPH {ECO:0000269|PubMed:31147539}; CC -!- SUBUNIT: Interacts with PPARG. {ECO:0000250|UniProtKB:O35710}. CC -!- INTERACTION: CC Q9UK39; Q8TEM1: NUP210; NbExp=2; IntAct=EBI-5655962, EBI-372826; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus CC {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:O35710}. Mitochondrion CC {ECO:0000269|PubMed:31147539}. CC -!- TISSUE SPECIFICITY: Adipose tissue. Expression is higher in CC subcutaneous adipose tissue as compared to visceral adipose tissue. CC {ECO:0000269|PubMed:22331129}. CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}. CC -!- CAUTION: Was initially shown to have low deadenylase activity that was CC lost when the metal-binding Glu was mutated (By similarity). Later CC studies showed that the purified protein lacked deadenylase activity CC (PubMed:29860338, PubMed:30389976). Was subsequently shown to act as a CC phosphatase (PubMed:31147539). {ECO:0000250|UniProtKB:O35710, CC ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:30389976, CC ECO:0000269|PubMed:31147539}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF183961; AAD56548.1; -; mRNA. DR EMBL; CH471056; EAX05129.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05131.1; -; Genomic_DNA. DR EMBL; BC113494; AAI13495.1; -; mRNA. DR EMBL; BC113500; AAI13501.1; -; mRNA. DR EMBL; AF199492; AAG01387.1; -; Genomic_DNA. DR EMBL; AF199493; AAG01388.1; -; mRNA. DR EMBL; AF199494; AAG01389.1; -; Transcribed_RNA. DR CCDS; CCDS3743.1; -. DR RefSeq; NP_036250.2; NM_012118.3. DR PDB; 6BT1; X-ray; 1.48 A; A=120-431. DR PDB; 6BT2; X-ray; 2.41 A; A/B=120-431. DR PDB; 6MAL; X-ray; 2.60 A; A=122-431. DR PDB; 6NF0; X-ray; 2.70 A; A=122-431. DR PDBsum; 6BT1; -. DR PDBsum; 6BT2; -. DR PDBsum; 6MAL; -. DR PDBsum; 6NF0; -. DR AlphaFoldDB; Q9UK39; -. DR SASBDB; Q9UK39; -. DR SMR; Q9UK39; -. DR BioGRID; 117347; 74. DR FunCoup; Q9UK39; 2186. DR IntAct; Q9UK39; 47. DR NDEx; IQUERY-CP-NOCT; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000280614; -. DR GlyGen; Q9UK39; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UK39; -. DR PhosphoSitePlus; Q9UK39; -. DR BioMuta; NOCT; -. DR DMDM; 212276446; -. DR jPOST; Q9UK39; -. DR MassIVE; Q9UK39; -. DR PaxDb; 9606-ENSP00000280614; -. DR PeptideAtlas; Q9UK39; -. DR ProteomicsDB; 84714; -. DR Pumba; Q9UK39; -. DR Antibodypedia; 16153; 125 antibodies from 30 providers. DR DNASU; 25819; -. DR Ensembl; ENST00000280614.4; ENSP00000280614.2; ENSG00000151014.7. DR GeneID; 25819; -. DR KEGG; hsa:25819; -. DR MANE-Select; ENST00000280614.4; ENSP00000280614.2; NM_012118.4; NP_036250.2. DR UCSC; uc003ihl.5; human. DR AGR; HGNC:14254; -. DR ClinPGx; PA26176; -. DR CTD; 25819; -. DR DisGeNET; 25819; -. DR GeneCards; NOCT; -. DR HGNC; HGNC:14254; NOCT. DR HPA; ENSG00000151014; Tissue enhanced (bone). DR MIM; 608468; gene. DR OpenTargets; ENSG00000151014; -. DR VEuPathDB; HostDB:ENSG00000151014; -. DR eggNOG; KOG0620; Eukaryota. DR GeneTree; ENSGT00940000155249; -. DR HOGENOM; CLU_016428_1_2_1; -. DR InParanoid; Q9UK39; -. DR OMA; RAACSMG; -. DR OrthoDB; 276515at2759; -. DR PAN-GO; Q9UK39; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9UK39; -. DR BioCyc; MetaCyc:ENSG00000151014-MONOMER; -. DR BRENDA; 3.1.3.108; 2681. DR PathwayCommons; Q9UK39; -. DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian expression. DR SignaLink; Q9UK39; -. DR Agora; ENSG00000151014; -. DR BioGRID-ORCS; 25819; 19 hits in 1140 CRISPR screens. DR ChiTaRS; NOCT; human. DR GenomeRNAi; 25819; -. DR Pharos; Q9UK39; Tbio. DR PRO; PR:Q9UK39; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9UK39; protein. DR Bgee; ENSG00000151014; Expressed in buccal mucosa cell and 117 other cell types or tissues. DR ExpressionAtlas; Q9UK39; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000932; C:P-body; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB. DR GO; GO:0019178; F:NADP phosphatase activity; IDA:UniProtKB. DR GO; GO:0102757; F:NADPH phosphatase activity; IDA:UniProtKB. DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB. DR GO; GO:0006739; P:NADP+ metabolic process; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd09096; Deadenylase_nocturnin; 1. DR FunFam; 3.60.10.10:FF:000012; nocturnin isoform X2; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR050410; CCR4/nocturin_mRNA_transcr. DR InterPro; IPR034965; Deadenylase_nocturnin. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR PANTHER; PTHR12121; CARBON CATABOLITE REPRESSOR PROTEIN 4; 1. DR PANTHER; PTHR12121:SF45; NOCTURNIN; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; DNase I-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Biological rhythms; Cytoplasm; Hydrolase; Magnesium; KW Metal-binding; Mitochondrion; Nucleus; Proteomics identification; KW Reference proteome; Repressor; RNA-binding; Transit peptide. FT TRANSIT 1..75 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 76..431 FT /note="Nocturnin" FT /evidence="ECO:0000255" FT /id="PRO_0000218568" FT REGION 20..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 343..353 FT /note="Interaction with PPARG" FT /evidence="ECO:0000250|UniProtKB:O35710" FT COMPBIAS 20..31 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..41 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 195 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:29860338, FT ECO:0000269|PubMed:30389976, ECO:0000269|PubMed:31147539, FT ECO:0007744|PDB:6BT1, ECO:0007744|PDB:6BT2, FT ECO:0007744|PDB:6MAL, ECO:0007744|PDB:6NF0" FT BINDING 195 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT BINDING 219..221 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT BINDING 286..289 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT BINDING 324..326 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31147539" FT VARIANT 140 FT /note="H -> Y (in dbSNP:rs2271777)" FT /id="VAR_047096" FT MUTAGEN 149 FT /note="N->A: Slightly decreased activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT MUTAGEN 160 FT /note="D->A: Lack of catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 195 FT /note="E->A: Slightly increased activity as transcriptional FT repressor. Lack of catalytic activity." FT /evidence="ECO:0000269|PubMed:29860338, FT ECO:0000269|PubMed:31147539" FT MUTAGEN 219 FT /note="K->A: Reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 286 FT /note="H->A: No effect on activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT MUTAGEN 286 FT /note="H->N: Lack of catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 288 FT /note="K->A: Reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 290 FT /note="R->A: Lack of catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 324 FT /note="D->A: No effect on activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT MUTAGEN 326 FT /note="N->A: No effect on activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT MUTAGEN 365 FT /note="K->A: No effect on catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 367 FT /note="R->A: Reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:31147539" FT MUTAGEN 377 FT /note="D->A: Slightly decreased activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT MUTAGEN 414 FT /note="H->A,N: Decreased activity as transcriptional FT repressor." FT /evidence="ECO:0000269|PubMed:29860338" FT CONFLICT 16 FT /note="D -> G (in Ref. 1; AAD56548)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="T -> N (in Ref. 4; AAG01387)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="A -> G (in Ref. 1; AAD56548)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="A -> T (in Ref. 4; AAG01389)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="S -> N (in Ref. 1; AAD56548)" FT /evidence="ECO:0000305" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:6MAL" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 189..195 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 204..209 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 223..226 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:6BT1" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 245..257 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 260..273 FT /evidence="ECO:0007829|PDB:6BT1" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 279..286 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 294..311 FT /evidence="ECO:0007829|PDB:6BT1" FT TURN 312..316 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 319..324 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 332..339 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 347..351 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 370..374 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:6BT1" FT TURN 383..385 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 386..392 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 393..396 FT /evidence="ECO:0007829|PDB:6BT1" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:6BT1" FT STRAND 411..414 FT /evidence="ECO:0007829|PDB:6BT2" FT STRAND 417..423 FT /evidence="ECO:0007829|PDB:6BT1" SQ SEQUENCE 431 AA; 48196 MW; 5BDEFC43173B2D0C CRC64; MFHSPRRLCS ALLQRDAPGL RRLPAPGLRR PLSPPAAVPR PASPRLLAAA SAASGAARSC SRTVCSMGTG TSRLYSALAK TLNSSAASQH PEYLVSPDPE HLEPIDPKEL LEECRAVLHT RPPRFQRDFV DLRTDCPSTH PPIRVMQWNI LAQALGEGKD NFVQCPVEAL KWEERKCLIL EEILAYQPDI LCLQEVDHYF DTFQPLLSRL GYQGTFFPKP WSPCLDVEHN NGPDGCALFF LQNRFKLVNS ANIRLTAMTL KTNQVAIAQT LECKESGRQF CIAVTHLKAR TGWERFRSAQ GCDLLQNLQN ITQGAKIPLI VCGDFNAEPT EEVYKHFASS SLNLNSAYKL LSADGQSEPP YTTWKIRTSG ECRHTLDYIW YSKHALNVRS ALDLLTEEQI GPNRLPSFNY PSDHLSLVCD FSFTEESDGL S //