NACC1_HUMAN
ID NACC1_HUMAN Reviewed; 527 AA.
AC Q96RE7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nucleus accumbens-associated protein 1;
DE Short=NAC-1;
DE AltName: Full=BTB/POZ domain-containing protein 14B;
GN Name=NACC1; Synonyms=BTBD14B, NAC1;
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=Keratinocyte;
RA Cha X.Y., Fakharzadeh S.S.;
RT "Human NAC1 protein, a gene transcriptional repressor.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 FUNCTION, HOMOOLIGOMERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=17130457; DOI=10.1073/pnas.0604083103;
RA Nakayama K., Nakayama N., Davidson B., Sheu J.-J.C., Jinawath N.,
RA Santillan A., Salani R., Bristow R.E., Morin P.J., Kurman R.J., Wang T.-L.,
RA Shih I.-M.;
RT "A BTB/POZ protein, NAC-1, is related to tumor recurrence and is essential
RT for tumor growth and survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18739-18744(2006).
RN [4]
RP FUNCTION.
RX PubMed=17804717; DOI=10.1158/0008-5472.can-07-1357;
RA Nakayama K., Nakayama N., Wang T.-L., Shih I.-M.;
RT "NAC-1 controls cell growth and survival by repressing transcription of
RT Gadd45GIP1, a candidate tumor suppressor.";
RL Cancer Res. 67:8058-8064(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17391728; DOI=10.1016/j.humpath.2006.12.009;
RA Davidson B., Berner A., Trope' C.G., Wang T.-L., Shih I.-M.;
RT "Expression and clinical role of the bric-a-brac tramtrack broad
RT complex/poxvirus and zinc protein NAC-1 in ovarian carcinoma effusions.";
RL Hum. Pathol. 38:1030-1036(2007).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP INVOLVEMENT IN NECFM, AND VARIANT NECFM TRP-298.
RX PubMed=28132692; DOI=10.1016/j.ajhg.2016.12.013;
RG UCLA Clinical Genomics Center;
RG Undiagnosed Diseases Network;
RA Schoch K., Meng L., Szelinger S., Bearden D.R., Stray-Pedersen A.,
RA Busk O.L., Stong N., Liston E., Cohn R.D., Scaglia F., Rosenfeld J.A.,
RA Tarpinian J., Skraban C.M., Deardorff M.A., Friedman J.N., Akdemir Z.C.,
RA Walley N., Mikati M.A., Kranz P.G., Jasien J., McConkie-Rosell A.,
RA McDonald M., Wechsler S.B., Freemark M., Kansagra S., Freedman S., Bali D.,
RA Millan F., Bale S., Nelson S.F., Lee H., Dorrani N., Goldstein D.B.,
RA Xiao R., Yang Y., Posey J.E., Martinez-Agosto J.A., Lupski J.R.,
RA Wangler M.F., Shashi V.;
RT "A recurrent de novo variant in NACC1 causes a syndrome characterized by
RT infantile epilepsy, cataracts, and profound developmental delay.";
RL Am. J. Hum. Genet. 100:343-351(2017).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-183; LYS-318; LYS-452;
RP LYS-480; LYS-483 AND LYS-498, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-125.
RX PubMed=19407373; DOI=10.1107/s1744309109012214;
RA Stead M.A., Carr S.B., Wright S.C.;
RT "Structure of the human Nac1 POZ domain.";
RL Acta Crystallogr. F 65:445-449(2009).
CC -!- FUNCTION: Functions as a transcriptional repressor. Seems to function
CC as a transcriptional corepressor in neuronal cells through recruitment
CC of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell
CC proliferation and survival. This may be mediated at least in part
CC through repressing transcriptional activity of GADD45GIP1. Required for
CC recruiting the proteasome from the nucleus to the cytoplasm and
CC dendritic spines. {ECO:0000269|PubMed:17130457,
CC ECO:0000269|PubMed:17804717}.
CC -!- SUBUNIT: Homooligomer; mediated by the BTB domain. Interacts with HDAC3
CC and HDAC4. Interacts (via BTB domain) with CUL3, PSMD7 AND RCOR1.
CC -!- INTERACTION:
CC Q96RE7; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-7950997, EBI-715389;
CC Q96RE7; Q08426: EHHADH; NbExp=3; IntAct=EBI-7950997, EBI-2339219;
CC Q96RE7; Q14241: ELOA; NbExp=3; IntAct=EBI-7950997, EBI-742350;
CC Q96RE7; O00214-2: LGALS8; NbExp=3; IntAct=EBI-7950997, EBI-12069522;
CC Q96RE7; P62310: LSM3; NbExp=3; IntAct=EBI-7950997, EBI-348239;
CC Q96RE7; P62875: POLR2L; NbExp=3; IntAct=EBI-7950997, EBI-359527;
CC Q96RE7; P41743: PRKCI; NbExp=3; IntAct=EBI-7950997, EBI-286199;
CC Q96RE7; Q99633: PRPF18; NbExp=3; IntAct=EBI-7950997, EBI-2798416;
CC Q96RE7; O43395: PRPF3; NbExp=3; IntAct=EBI-7950997, EBI-744322;
CC Q96RE7; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-7950997, EBI-17208936;
CC Q96RE7; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-7950997, EBI-1049952;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Distribution in the
CC cytoplasm is dependent on phosphorylation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Overexpressed in several types of carcinomas
CC including ovarian serous carcinomas. Expression levels positively
CC correlate with tumor recurrence in ovarian serous carcinomas, and
CC intense immunoreactivity in primary ovarian tumors predicts early
CC recurrence. Up-regulated in ovarian carcinomas after chemotherapy,
CC suggesting a role in development of chemotherapy resistance in ovarian
CC cancer. {ECO:0000269|PubMed:17130457, ECO:0000269|PubMed:17391728}.
CC -!- DISEASE: Neurodevelopmental disorder with epilepsy, cataracts, feeding
CC difficulties, and delayed brain myelination (NECFM) [MIM:617393]: A
CC neurodevelopmental disorder characterized by microcephaly, profound
CC developmental delay, intellectual disability, cataracts, severe
CC epilepsy including infantile spasms, irritability, failure to thrive,
CC and stereotypic hand movements. Brain imaging reveals delayed
CC myelination and cerebral atrophy. {ECO:0000269|PubMed:28132692}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NACC1ID44511ch19p13.html";
CC -!- WEB RESOURCE: Name=Undiagnosed Disease Network; Note=NACC1;
CC URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/nacc1-gene/";
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DR EMBL; AF395817; AAK83885.1; -; mRNA.
DR EMBL; BC055396; AAH55396.1; -; mRNA.
DR CCDS; CCDS12294.1; -.
DR RefSeq; NP_443108.1; NM_052876.3.
DR RefSeq; XP_005259778.1; XM_005259721.3.
DR PDB; 3GA1; X-ray; 2.10 A; A/B=2-125.
DR PDB; 4U2N; X-ray; 2.30 A; A/B=2-125.
DR PDB; 7BV9; NMR; -; A=322-485.
DR PDBsum; 3GA1; -.
DR PDBsum; 4U2N; -.
DR PDBsum; 7BV9; -.
DR AlphaFoldDB; Q96RE7; -.
DR SMR; Q96RE7; -.
DR BioGRID; 125217; 79.
DR IntAct; Q96RE7; 29.
DR MINT; Q96RE7; -.
DR STRING; 9606.ENSP00000292431; -.
DR GlyGen; Q96RE7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96RE7; -.
DR MetOSite; Q96RE7; -.
DR PhosphoSitePlus; Q96RE7; -.
DR SwissPalm; Q96RE7; -.
DR BioMuta; NACC1; -.
DR DMDM; 74732694; -.
DR EPD; Q96RE7; -.
DR jPOST; Q96RE7; -.
DR MassIVE; Q96RE7; -.
DR MaxQB; Q96RE7; -.
DR PaxDb; Q96RE7; -.
DR PeptideAtlas; Q96RE7; -.
DR PRIDE; Q96RE7; -.
DR ProteomicsDB; 77953; -.
DR Antibodypedia; 13525; 319 antibodies from 38 providers.
DR DNASU; 112939; -.
DR Ensembl; ENST00000292431.5; ENSP00000292431.3; ENSG00000160877.6.
DR GeneID; 112939; -.
DR KEGG; hsa:112939; -.
DR MANE-Select; ENST00000292431.5; ENSP00000292431.3; NM_052876.4; NP_443108.1.
DR UCSC; uc002mwm.5; human.
DR CTD; 112939; -.
DR DisGeNET; 112939; -.
DR GeneCards; NACC1; -.
DR HGNC; HGNC:20967; NACC1.
DR HPA; ENSG00000160877; Low tissue specificity.
DR MalaCards; NACC1; -.
DR MIM; 610672; gene.
DR MIM; 617393; phenotype.
DR neXtProt; NX_Q96RE7; -.
DR OpenTargets; ENSG00000160877; -.
DR Orphanet; 500545; Severe neurodevelopmental disorder with feeding difficulties-stereotypic hand movement-bilateral cataract.
DR PharmGKB; PA164723404; -.
DR VEuPathDB; HostDB:ENSG00000160877; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159327; -.
DR HOGENOM; CLU_029038_1_0_1; -.
DR InParanoid; Q96RE7; -.
DR OMA; GKMEPDM; -.
DR OrthoDB; 567120at2759; -.
DR PhylomeDB; Q96RE7; -.
DR TreeFam; TF331184; -.
DR PathwayCommons; Q96RE7; -.
DR SignaLink; Q96RE7; -.
DR SIGNOR; Q96RE7; -.
DR BioGRID-ORCS; 112939; 34 hits in 1115 CRISPR screens.
DR ChiTaRS; NACC1; human.
DR EvolutionaryTrace; Q96RE7; -.
DR GeneWiki; BTBD14B; -.
DR GenomeRNAi; 112939; -.
DR Pharos; Q96RE7; Tbio.
DR PRO; PR:Q96RE7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96RE7; protein.
DR Bgee; ENSG00000160877; Expressed in pancreatic ductal cell and 190 other tissues.
DR ExpressionAtlas; Q96RE7; baseline and differential.
DR Genevisible; Q96RE7; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR018379; BEN_domain.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF10523; BEN; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM01025; BEN; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS51457; BEN; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..527
FT /note="Nucleus accumbens-associated protein 1"
FT /id="PRO_0000274041"
FT DOMAIN 30..94
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 374..471
FT /note="BEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 259
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:O35260"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 318
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 298
FT /note="R -> W (in NECFM; dbSNP:rs1060505041)"
FT /evidence="ECO:0000269|PubMed:28132692"
FT /id="VAR_078808"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3GA1"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:4U2N"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3GA1"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:3GA1"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:3GA1"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3GA1"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:3GA1"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4U2N"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7BV9"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:7BV9"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:7BV9"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:7BV9"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:7BV9"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:7BV9"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:7BV9"
SQ SEQUENCE 527 AA; 57258 MW; 00BEA89D2DC3DAD2 CRC64;
MAQTLQMEIP NFGNSILECL NEQRLQGLYC DVSVVVKGHA FKAHRAVLAA SSSYFRDLFN
NSRSAVVELP AAVQPQSFQQ ILSFCYTGRL SMNVGDQFLL MYTAGFLQIQ EIMEKGTEFF
LKVSSPSCDS QGLHAEEAPS SEPQSPVAQT SGWPACSTPL PLVSRVKTEQ QESDSVQCMP
VAKRLWDSGQ KEAGGGGNGS RKMAKFSTPD LAANRPHQPP PPQQAPVVAA AQPAVAAGAG
QPAGGVAAAG GVVSGPSTSE RTSPGTSSAY TSDSPGSYHN EEDEEEDGGE EGMDEQYRQI
CNMYTMYSMM NVGQTAEKVE ALPEQVAPES RNRIRVRQDL ASLPAELINQ IGNRCHPKLY
DEGDPSEKLE LVTGTNVYIT RAQLMNCHVS AGTRHKVLLR RLLASFFDRN TLANSCGTGI
RSSTNDPRRK PLDSRVLHAV KYYCQNFAPN FKESEMNAIA ADMCTNARRV VRKSWMPKVK
VLKAEDDAYT TFISETGKIE PDMMGVEHGF ETASHEGEAG PSAEALQ
