CNOT3_HUMAN
ID CNOT3_HUMAN Reviewed; 753 AA.
AC O75175; Q9NZN7; Q9UF76;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CCR4-NOT transcription complex subunit 3 {ECO:0000305};
DE AltName: Full=CCR4-associated factor 3;
DE AltName: Full=Leukocyte receptor cluster member 2;
GN Name=CNOT3 {ECO:0000312|HGNC:HGNC:7879}; Synonyms=KIAA0691, LENG2, NOT3;
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=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-607, INTERACTION WITH CNOT8, AND TISSUE
RP SPECIFICITY.
RX PubMed=10637334; DOI=10.1093/nar/28.3.809;
RA Albert T.K., Lemaire M., van Berkum N.L., Gentz R., Collart M.A.,
RA Timmers H.T.M.;
RT "Isolation and characterization of human orthologs of yeast CCR4-NOT
RT complex subunits.";
RL Nucleic Acids Res. 28:809-817(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-161.
RC TISSUE=Testis;
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 [5]
RP INTERACTION WITH TIP120B.
RX PubMed=12207886; DOI=10.1016/s0006-291x(02)02031-4;
RA Aoki T., Okada N., Wakamatsu T., Tamura T.-A.;
RT "TBP-interacting protein 120B, which is induced in relation to myogenesis,
RT binds to NOT3.";
RL Biochem. Biophys. Res. Commun. 296:1097-1103(2002).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=14707134; DOI=10.1074/jbc.m311747200;
RA Zwartjes C.G., Jayne S., van den Berg D.L., Timmers H.T.;
RT "Repression of promoter activity by CNOT2, a subunit of the transcription
RT regulatory Ccr4-not complex.";
RL J. Biol. Chem. 279:10848-10854(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE CCR4-NOT
RP COMPLEX.
RX PubMed=19558367; DOI=10.1042/bj20090500;
RA Lau N.C., Kolkman A., van Schaik F.M., Mulder K.W., Pijnappel W.W.,
RA Heck A.J., Timmers H.T.;
RT "Human Ccr4-Not complexes contain variable deadenylase subunits.";
RL Biochem. J. 422:443-453(2009).
RN [10]
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 [11]
RP INTERACTION WITH CNOT2.
RX PubMed=21299754; DOI=10.1111/j.1365-2443.2011.01492.x;
RA Ito K., Inoue T., Yokoyama K., Morita M., Suzuki T., Yamamoto T.;
RT "CNOT2 depletion disrupts and inhibits the CCR4-NOT deadenylase complex and
RT induces apoptotic cell death.";
RL Genes Cells 16:368-379(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP FUNCTION.
RX PubMed=22342980; DOI=10.1016/j.bbrc.2012.02.007;
RA Takahashi A., Kikuguchi C., Morita M., Shimodaira T., Tokai-Nishizumi N.,
RA Yokoyama K., Ohsugi M., Suzuki T., Yamamoto T.;
RT "Involvement of CNOT3 in mitotic progression through inhibition of MAD1
RT expression.";
RL Biochem. Biophys. Res. Commun. 419:268-273(2012).
RN [14]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22367759; DOI=10.1002/stem.1070;
RA Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P.,
RA Archer T.K., Jothi R., Hu G.;
RT "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit
RT extraembryonic differentiation.";
RL Stem Cells 30:910-922(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP INTERACTION WITH EBF1.
RX PubMed=27807034; DOI=10.1101/gad.285452.116;
RA Yang C.Y., Ramamoorthy S., Boller S., Rosenbaum M., Rodriguez Gil A.,
RA Mittler G., Imai Y., Kuba K., Grosschedl R.;
RT "Interaction of CCR4-NOT with EBF1 regulates gene-specific transcription
RT and mRNA stability in B lymphopoiesis.";
RL Genes Dev. 30:2310-2324(2016).
RN [17]
RP INVOLVEMENT IN IDDSADF, AND VARIANTS IDDSADF GLN-20; VAL-48; GLU-119;
RP LYS-147; CYS-188; HIS-188; 622-TRP--GLN-753 DEL; 694-GLN--GLN-753 DEL AND
RP GLN-697.
RX PubMed=31201375; DOI=10.1038/s41431-019-0413-6;
RA Martin R., Splitt M., Genevieve D., Aten E., Collins A., de Bie C.I.,
RA Faivre L., Foulds N., Giltay J., Ibitoye R., Joss S., Kennedy J., Kerr B.,
RA Kivuva E., Koopmans M., Newbury-Ecob R., Jean-Marcais N., Peeters E.A.J.,
RA Smithson S., Tomkins S., Tranmauthem F., Piton A., van Haeringen A.;
RT "De novo variants in CNOT3 cause a variable neurodevelopmental disorder.";
RL Eur. J. Hum. Genet. 27:1677-1682(2019).
CC -!- FUNCTION: Component of the CCR4-NOT complex which is one of the major
CC cellular mRNA deadenylases and is linked to various cellular processes
CC including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. May be involved in
CC metabolic regulation; may be involved in recruitment of the CCR4-NOT
CC complex to deadenylation target mRNAs involved in energy metabolism.
CC Involved in mitotic progression and regulation of the spindle assembly
CC checkpoint by regulating the stability of MAD1L1 mRNA. Can repress
CC transcription and may link the CCR4-NOT complex to transcriptional
CC regulation; the repressive function may involve histone deacetylases.
CC Involved in the maintenance of embryonic stem (ES) cell identity.
CC {ECO:0000269|PubMed:14707134, ECO:0000269|PubMed:22342980,
CC ECO:0000269|PubMed:22367759}.
CC -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to
CC exist that differ in the participation of probably mutually exclusive
CC catalytic subunits. In the complex interacts directly with CNOT2.
CC Interacts with TIP120B and NANOS2. Interacts with EBF1.
CC {ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:12207886,
CC ECO:0000269|PubMed:19558367, ECO:0000269|PubMed:21299754,
CC ECO:0000269|PubMed:27807034}.
CC -!- INTERACTION:
CC O75175; P27797: CALR; NbExp=3; IntAct=EBI-743073, EBI-1049597;
CC O75175; A5YKK6: CNOT1; NbExp=2; IntAct=EBI-743073, EBI-1222758;
CC O75175; Q9NZN8: CNOT2; NbExp=10; IntAct=EBI-743073, EBI-743033;
CC O75175; Q96LI5: CNOT6L; NbExp=2; IntAct=EBI-743073, EBI-1046635;
CC O75175; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-743073, EBI-742299;
CC O75175; P36957: DLST; NbExp=3; IntAct=EBI-743073, EBI-351007;
CC O75175; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-743073, EBI-1055945;
CC O75175; P16284: PECAM1; NbExp=3; IntAct=EBI-743073, EBI-716404;
CC O75175; Q9HCJ0: TNRC6C; NbExp=10; IntAct=EBI-743073, EBI-6507625;
CC O75175; P50616: TOB1; NbExp=3; IntAct=EBI-743073, EBI-723281;
CC O75175; P55072: VCP; NbExp=3; IntAct=EBI-743073, EBI-355164;
CC O75175; Q6ZQ73: Cand2; Xeno; NbExp=3; IntAct=EBI-743073, EBI-6504831;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC Cytoplasm, P-body {ECO:0000250}. Note=NANOS2 promotes its localization
CC to P-body. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart,
CC thymus, spleen, kidney, liver, small intestine, lung and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:10637334}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells.
CC {ECO:0000269|PubMed:22367759}.
CC -!- DISEASE: Intellectual developmental disorder with speech delay, autism
CC and dysmorphic facies (IDDSADF) [MIM:618672]: An autosomal dominant
CC disorder characterized by mild to severe intellectual disability,
CC developmental delay, delayed or absent speech, hypotonia, short
CC stature, autistic features, and highly variable dysmorphic facial
CC features. {ECO:0000269|PubMed:31201375}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CNOT2/3/5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29828.1; Type=Miscellaneous discrepancy; Note=Seems to have an artifactual loop-out at the 3'-end deleting 2 full exons and part of 2 others.; Evidence={ECO:0000305};
CC Sequence=BAA31666.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB63766.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AB014591; BAA31666.2; ALT_INIT; mRNA.
DR EMBL; BC016474; AAH16474.1; -; mRNA.
DR EMBL; AF180474; AAF29828.1; ALT_SEQ; mRNA.
DR EMBL; AL133647; CAB63766.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12880.1; -.
DR PIR; T43456; T43456.
DR RefSeq; NP_055331.1; NM_014516.3.
DR PDB; 4C0D; X-ray; 3.20 A; C=607-753.
DR PDB; 4C0G; X-ray; 2.40 A; A/B/C/D/E/F=656-753.
DR PDB; 5FU6; X-ray; 2.90 A; C/F=607-748.
DR PDB; 5FU7; X-ray; 3.10 A; C/G=607-748.
DR PDBsum; 4C0D; -.
DR PDBsum; 4C0G; -.
DR PDBsum; 5FU6; -.
DR PDBsum; 5FU7; -.
DR AlphaFoldDB; O75175; -.
DR SMR; O75175; -.
DR BioGRID; 110911; 149.
DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant.
DR ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant.
DR ComplexPortal; CPX-2849; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant.
DR ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant.
DR CORUM; O75175; -.
DR DIP; DIP-40297N; -.
DR IntAct; O75175; 57.
DR MINT; O75175; -.
DR STRING; 9606.ENSP00000351159; -.
DR ChEMBL; CHEMBL4105769; -.
DR iPTMnet; O75175; -.
DR PhosphoSitePlus; O75175; -.
DR BioMuta; CNOT3; -.
DR EPD; O75175; -.
DR jPOST; O75175; -.
DR MassIVE; O75175; -.
DR MaxQB; O75175; -.
DR PaxDb; O75175; -.
DR PeptideAtlas; O75175; -.
DR PRIDE; O75175; -.
DR Antibodypedia; 1756; 260 antibodies from 29 providers.
DR DNASU; 4849; -.
DR Ensembl; ENST00000221232.11; ENSP00000221232.5; ENSG00000088038.19.
DR Ensembl; ENST00000358389.7; ENSP00000351159.4; ENSG00000088038.19.
DR Ensembl; ENST00000610883.4; ENSP00000480258.1; ENSG00000274941.4.
DR Ensembl; ENST00000611252.4; ENSP00000483968.1; ENSG00000275979.4.
DR Ensembl; ENST00000612924.4; ENSP00000480585.1; ENSG00000274176.4.
DR Ensembl; ENST00000613528.4; ENSP00000483604.1; ENSG00000277615.4.
DR Ensembl; ENST00000613752.4; ENSP00000481681.1; ENSG00000273943.4.
DR Ensembl; ENST00000614649.4; ENSP00000484794.1; ENSG00000274176.4.
DR Ensembl; ENST00000615030.2; ENSP00000480697.1; ENSG00000274616.4.
DR Ensembl; ENST00000616359.3; ENSP00000484040.1; ENSG00000274616.4.
DR Ensembl; ENST00000616910.4; ENSP00000480876.1; ENSG00000277615.4.
DR Ensembl; ENST00000617982.4; ENSP00000479987.1; ENSG00000277600.4.
DR Ensembl; ENST00000618405.4; ENSP00000481924.1; ENSG00000277114.4.
DR Ensembl; ENST00000619567.4; ENSP00000483882.1; ENSG00000275979.4.
DR Ensembl; ENST00000619854.4; ENSP00000483431.1; ENSG00000273943.4.
DR Ensembl; ENST00000620060.1; ENSP00000483036.1; ENSG00000277114.4.
DR Ensembl; ENST00000620419.4; ENSP00000478956.1; ENSG00000276082.4.
DR Ensembl; ENST00000620573.4; ENSP00000480988.1; ENSG00000276082.4.
DR Ensembl; ENST00000620970.4; ENSP00000483692.1; ENSG00000277600.4.
DR Ensembl; ENST00000622131.4; ENSP00000478280.1; ENSG00000274941.4.
DR GeneID; 4849; -.
DR KEGG; hsa:4849; -.
DR MANE-Select; ENST00000221232.11; ENSP00000221232.5; NM_014516.4; NP_055331.1.
DR UCSC; uc002qdj.3; human.
DR CTD; 4849; -.
DR DisGeNET; 4849; -.
DR GeneCards; CNOT3; -.
DR HGNC; HGNC:7879; CNOT3.
DR HPA; ENSG00000088038; Low tissue specificity.
DR MalaCards; CNOT3; -.
DR MIM; 604910; gene.
DR MIM; 618672; phenotype.
DR neXtProt; NX_O75175; -.
DR OpenTargets; ENSG00000088038; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA26674; -.
DR VEuPathDB; HostDB:ENSG00000088038; -.
DR eggNOG; KOG2150; Eukaryota.
DR GeneTree; ENSGT00390000014743; -.
DR HOGENOM; CLU_013819_1_1_1; -.
DR InParanoid; O75175; -.
DR OrthoDB; 1109812at2759; -.
DR PhylomeDB; O75175; -.
DR TreeFam; TF321963; -.
DR PathwayCommons; O75175; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR SignaLink; O75175; -.
DR SIGNOR; O75175; -.
DR BioGRID-ORCS; 4849; 713 hits in 1082 CRISPR screens.
DR ChiTaRS; CNOT3; human.
DR GeneWiki; CNOT3; -.
DR GenomeRNAi; 4849; -.
DR Pharos; O75175; Tbio.
DR PRO; PR:O75175; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75175; protein.
DR Bgee; ENSG00000088038; Expressed in sural nerve and 93 other tissues.
DR ExpressionAtlas; O75175; baseline and differential.
DR Genevisible; O75175; HS.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR Gene3D; 2.30.30.1020; -; 1.
DR IDEAL; IID00434; -.
DR InterPro; IPR038635; CCR4-NOT_su2/3/5_N_sf.
DR InterPro; IPR012270; CCR4-NOT_su3/5.
DR InterPro; IPR040168; Not2/3/5.
DR InterPro; IPR007282; NOT2/3/5_C.
DR InterPro; IPR007207; Not_N.
DR PANTHER; PTHR23326; PTHR23326; 2.
DR Pfam; PF04153; NOT2_3_5; 1.
DR Pfam; PF04065; Not3; 1.
DR PIRSF; PIRSF005290; NOT_su_3_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Disease variant;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..753
FT /note="CCR4-NOT transcription complex subunit 3"
FT /id="PRO_0000198333"
FT REGION 240..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..753
FT /note="Repressor domain"
FT COMPBIAS 240..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 20
FT /note="E -> Q (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083405"
FT VARIANT 48
FT /note="L -> V (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083406"
FT VARIANT 119
FT /note="K -> E (in IDDSADF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083407"
FT VARIANT 147
FT /note="E -> K (in IDDSADF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083408"
FT VARIANT 188
FT /note="R -> C (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083409"
FT VARIANT 188
FT /note="R -> H (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083410"
FT VARIANT 622..753
FT /note="Missing (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083411"
FT VARIANT 694..753
FT /note="Missing (in IDDSADF)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083412"
FT VARIANT 697
FT /note="R -> Q (in IDDSADF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31201375"
FT /id="VAR_083413"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:5FU6"
FT HELIX 628..631
FT /evidence="ECO:0007829|PDB:5FU6"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:5FU6"
FT TURN 655..658
FT /evidence="ECO:0007829|PDB:5FU6"
FT HELIX 660..665
FT /evidence="ECO:0007829|PDB:4C0G"
FT HELIX 668..677
FT /evidence="ECO:0007829|PDB:4C0G"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:5FU6"
FT HELIX 682..693
FT /evidence="ECO:0007829|PDB:4C0G"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:4C0G"
FT TURN 700..703
FT /evidence="ECO:0007829|PDB:4C0G"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:4C0G"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:4C0G"
FT STRAND 717..728
FT /evidence="ECO:0007829|PDB:4C0G"
FT TURN 729..732
FT /evidence="ECO:0007829|PDB:4C0G"
FT STRAND 733..743
FT /evidence="ECO:0007829|PDB:4C0G"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:4C0G"
SQ SEQUENCE 753 AA; 81872 MW; C9D4F8B9FEF6CD90 CRC64;
MADKRKLQGE IDRCLKKVSE GVEQFEDIWQ KLHNAANANQ KEKYEADLKK EIKKLQRLRD
QIKTWVASNE IKDKRQLIDN RKLIETQMER FKVVERETKT KAYSKEGLGL AQKVDPAQKE
KEEVGQWLTN TIDTLNMQVD QFESEVESLS VQTRKKKGDK DKQDRIEGLK RHIEKHRYHV
RMLETILRML DNDSILVDAI RKIKDDVEYY VDSSQDPDFE ENEFLYDDLD LEDIPQALVA
TSPPSHSHME DEIFNQSSST PTSTTSSSPI PPSPANCTTE NSEDDKKRGR STDSEVSQSP
AKNGSKPVHS NQHPQSPAVP PTYPSGPPPA ASALSTTPGN NGVPAPAAPP SALGPKASPA
PSHNSGTPAP YAQAVAPPAP SGPSTTQPRP PSVQPSGGGG GGSGGGGSSS SSNSSAGGGA
GKQNGATSYS SVVADSPAEV ALSSSGGNNA SSQALGPPSG PHNPPPSTSK EPSAAAPTGA
GGVAPGSGNN SGGPSLLVPL PVNPPSSPTP SFSDAKAAGA LLNGPPQFST APEIKAPEPL
SSLKSMAERA AISSGIEDPV PTLHLTERDI ILSSTSAPPA SAQPPLQLSE VNIPLSLGVC
PLGPVPLTKE QLYQQAMEEA AWHHMPHPSD SERIRQYLPR NPCPTPPYHH QMPPPHSDTV
EFYQRLSTET LFFIFYYLEG TKAQYLAAKA LKKQSWRFHT KYMMWFQRHE EPKTITDEFE
QGTYIYFDYE KWGQRKKEGF TFEYRYLEDR DLQ
