MED27_HUMAN
ID MED27_HUMAN Reviewed; 311 AA.
AC Q6P2C8; O95401; Q4F964; Q5VTA4; Q5VTA5; Q9BU57; Q9NYR4; V9GYV9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 27;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 8;
DE Short=CRSP complex subunit 8;
DE AltName: Full=Mediator complex subunit 27;
DE AltName: Full=P37 TRAP/SMCC/PC2 subunit;
DE AltName: Full=Transcriptional coactivator CRSP34;
GN Name=MED27; Synonyms=CRSP34 {ECO:0000312|EMBL:AAD12721.1}, CRSP8;
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] (ISOFORM 3).
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH64608.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung {ECO:0000312|EMBL:AAH02878.1}, and
RC Skin {ECO:0000312|EMBL:AAH64608.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD12721.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-311 (ISOFORM 1), FUNCTION, IDENTIFICATION
RP IN CRSP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9989412; DOI=10.1038/17141;
RA Ryu S., Zhou S., Ladurner A.G., Tjian R.;
RT "The transcriptional cofactor complex CRSP is required for activity of the
RT enhancer-binding protein Sp1.";
RL Nature 397:446-450(1999).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAF37290.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-311 (ISOFORM 1), FUNCTION, IDENTIFICATION
RP IN CRSP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=10882111; DOI=10.1016/s1097-2765(00)80254-3;
RA Malik S., Gu W., Wu W., Qin J., Roeder R.G.;
RT "The USA-derived transcriptional coactivator PC2 is a submodule of
RT TRAP/SMCC and acts synergistically with other PCs.";
RL Mol. Cell 5:753-760(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-311 (ISOFORM 2).
RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Huang B., Li H., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP 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 METHYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP INVOLVEMENT IN NEDSCAC, AND VARIANTS NEDSCAC GLY-63; PHE-232; ALA-242;
RP LEU-259; LEU-280; SER-291 AND LEU-293.
RX PubMed=33443317; DOI=10.1002/ana.26019;
RA Meng L., Isohanni P., Shao Y., Graham B.H., Hickey S.E., Brooks S.,
RA Suomalainen A., Joset P., Steindl K., Rauch A., Hackenberg A., High F.A.,
RA Armstrong-Javors A., Mencacci N.E., Gonzalez-Latapi P., Kamel W.A.,
RA Al-Hashel J.Y., Bustos B.I., Hernandez A.V., Krainc D., Lubbe S.J.,
RA Van Esch H., De Luca C., Ballon K., Ravelli C., Burglen L., Qebibo L.,
RA Calame D.G., Mitani T., Marafi D., Pehlivan D., Saadi N.W., Sahin Y.,
RA Maroofian R., Efthymiou S., Houlden H., Maqbool S., Rahman F., Gu S.,
RA Posey J.E., Lupski J.R., Hunter J.V., Wangler M.F., Carroll C.J., Yang Y.;
RT "MED27 variants cause developmental delay, dystonia, and cerebellar
RT hypoplasia.";
RL Ann. Neurol. 89:828-833(2021).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. {ECO:0000269|PubMed:10882111,
CC ECO:0000269|PubMed:9989412}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.
CC {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:9989412}.
CC -!- INTERACTION:
CC Q6P2C8; Q9NVC6: MED17; NbExp=3; IntAct=EBI-394603, EBI-394562;
CC Q6P2C8; Q15528: MED22; NbExp=3; IntAct=EBI-394603, EBI-394687;
CC Q6P2C8; O75586: MED6; NbExp=2; IntAct=EBI-394603, EBI-394624;
CC Q6P2C8; Q9R0X0: Med20; Xeno; NbExp=2; IntAct=EBI-394603, EBI-398698;
CC Q6P2C8; Q9CQI9: Med30; Xeno; NbExp=2; IntAct=EBI-394603, EBI-309220;
CC Q6P2C8; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-394603, EBI-7990252;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882111,
CC ECO:0000269|PubMed:9989412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:9989412,
CC ECO:0000303|PubMed:15164053, ECO:0000305};
CC IsoId=Q6P2C8-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:15164053};
CC IsoId=Q6P2C8-2; Sequence=VSP_051869;
CC Name=3;
CC IsoId=Q6P2C8-4; Sequence=VSP_055411, VSP_055412;
CC -!- DISEASE: Neurodevelopmental disorder with spasticity, cataracts, and
CC cerebellar hypoplasia (NEDSCAC) [MIM:619286]: An autosomal recessive
CC disorder characterized by global developmental delay, impaired
CC intellectual development, and poor or absent speech. More severely
CC affected individuals do not achieve independent ambulation, whereas
CC others develop some speech and can walk, or show regression later in
CC childhood. Additional features include axial hypotonia, peripheral
CC spasticity, dystonia, cataracts, and seizures. Brain imaging usually
CC shows cerebellar hypoplasia, thin corpus callosum, cerebral atrophy,
CC and hypomyelination. {ECO:0000269|PubMed:33443317}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 27 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02878.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH02878.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BQ189678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002878; AAH02878.1; ALT_SEQ; mRNA.
DR EMBL; BC064608; AAH64608.1; -; mRNA.
DR EMBL; AF104252; AAD12721.1; -; mRNA.
DR EMBL; AF230382; AAF37290.1; -; mRNA.
DR EMBL; DQ099387; AAZ13763.1; -; mRNA.
DR CCDS; CCDS59153.1; -. [Q6P2C8-2]
DR CCDS; CCDS6945.1; -. [Q6P2C8-1]
DR CCDS; CCDS69689.1; -. [Q6P2C8-4]
DR RefSeq; NP_001240810.1; NM_001253881.1. [Q6P2C8-2]
DR RefSeq; NP_001240811.1; NM_001253882.1. [Q6P2C8-4]
DR RefSeq; NP_004260.2; NM_004269.3. [Q6P2C8-1]
DR PDB; 7EMF; EM; 3.50 A; 0=1-311.
DR PDB; 7ENA; EM; 4.07 A; c=1-311.
DR PDB; 7ENC; EM; 4.13 A; c=1-311.
DR PDB; 7ENJ; EM; 4.40 A; 0=1-311.
DR PDB; 7LBM; EM; 4.80 A; n=1-311.
DR PDB; 7NVR; EM; 4.50 A; p=1-311.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q6P2C8; -.
DR SMR; Q6P2C8; -.
DR BioGRID; 114832; 77.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q6P2C8; -.
DR DIP; DIP-31465N; -.
DR IntAct; Q6P2C8; 46.
DR MINT; Q6P2C8; -.
DR STRING; 9606.ENSP00000292035; -.
DR iPTMnet; Q6P2C8; -.
DR PhosphoSitePlus; Q6P2C8; -.
DR BioMuta; MED27; -.
DR DMDM; 74737195; -.
DR EPD; Q6P2C8; -.
DR jPOST; Q6P2C8; -.
DR MassIVE; Q6P2C8; -.
DR MaxQB; Q6P2C8; -.
DR PaxDb; Q6P2C8; -.
DR PeptideAtlas; Q6P2C8; -.
DR PRIDE; Q6P2C8; -.
DR ProteomicsDB; 66886; -. [Q6P2C8-1]
DR ProteomicsDB; 66887; -. [Q6P2C8-2]
DR Antibodypedia; 1810; 162 antibodies from 27 providers.
DR DNASU; 9442; -.
DR Ensembl; ENST00000292035.10; ENSP00000292035.5; ENSG00000160563.14. [Q6P2C8-1]
DR Ensembl; ENST00000357028.6; ENSP00000349530.3; ENSG00000160563.14. [Q6P2C8-2]
DR Ensembl; ENST00000474263.1; ENSP00000477136.1; ENSG00000160563.14. [Q6P2C8-4]
DR GeneID; 9442; -.
DR KEGG; hsa:9442; -.
DR MANE-Select; ENST00000292035.10; ENSP00000292035.5; NM_004269.4; NP_004260.2.
DR UCSC; uc004cbe.3; human. [Q6P2C8-1]
DR CTD; 9442; -.
DR DisGeNET; 9442; -.
DR GeneCards; MED27; -.
DR HGNC; HGNC:2377; MED27.
DR HPA; ENSG00000160563; Low tissue specificity.
DR MIM; 605044; gene.
DR MIM; 619286; phenotype.
DR neXtProt; NX_Q6P2C8; -.
DR OpenTargets; ENSG00000160563; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA162395634; -.
DR VEuPathDB; HostDB:ENSG00000160563; -.
DR eggNOG; ENOG502QS6H; Eukaryota.
DR GeneTree; ENSGT00390000012207; -.
DR HOGENOM; CLU_056015_0_0_1; -.
DR InParanoid; Q6P2C8; -.
DR OMA; HAAMLHF; -.
DR OrthoDB; 1256412at2759; -.
DR PhylomeDB; Q6P2C8; -.
DR TreeFam; TF323728; -.
DR PathwayCommons; Q6P2C8; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q6P2C8; -.
DR SIGNOR; Q6P2C8; -.
DR BioGRID-ORCS; 9442; 509 hits in 1075 CRISPR screens.
DR ChiTaRS; MED27; human.
DR GeneWiki; MED27; -.
DR GenomeRNAi; 9442; -.
DR Pharos; Q6P2C8; Tbio.
DR PRO; PR:Q6P2C8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6P2C8; protein.
DR Bgee; ENSG00000160563; Expressed in oocyte and 182 other tissues.
DR ExpressionAtlas; Q6P2C8; baseline and differential.
DR Genevisible; Q6P2C8; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR021627; Mediator_Med27.
DR PANTHER; PTHR13130; PTHR13130; 1.
DR Pfam; PF11571; Med27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cataract;
KW Intellectual disability; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..311
FT /note="Mediator of RNA polymerase II transcription subunit
FT 27"
FT /id="PRO_0000079361"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 117..130
FT /note="LQYHAGLASGLLNQ -> KEQLSIPRIFHWKV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8889548"
FT /id="VSP_055411"
FT VAR_SEQ 131..311
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8889548"
FT /id="VSP_055412"
FT VAR_SEQ 192..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15164053,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_051869"
FT VARIANT 63
FT /note="V -> G (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs774752053)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085606"
FT VARIANT 232
FT /note="S -> F (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs1056298725)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085607"
FT VARIANT 242
FT /note="V -> A (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs1589166413)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085608"
FT VARIANT 259
FT /note="P -> L (in NEDSCAC; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085609"
FT VARIANT 280
FT /note="P -> L (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs778593272)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085610"
FT VARIANT 291
FT /note="G -> S (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs774276967)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085611"
FT VARIANT 293
FT /note="P -> L (in NEDSCAC; unknown pathological
FT significance; dbSNP:rs1218659650)"
FT /evidence="ECO:0000269|PubMed:33443317"
FT /id="VAR_085612"
FT CONFLICT 64
FT /note="N -> D (in Ref. 6; AAZ13763)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> E (in Ref. 6; AAZ13763)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> S (in Ref. 4; AAD12721)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> C (in Ref. 4; AAD12721)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="N -> D (in Ref. 6; AAZ13763)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="A -> G (in Ref. 4; AAD12721)"
FT /evidence="ECO:0000305"
FT HELIX 8..37
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 45..76
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 104..130
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 198..219
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 311 AA; 35432 MW; 996D675993E393CB CRC64;
MADVINVSVN LEAFSQAISA IQALRSSVSR VFDCLKDGMR NKETLEGREK AFIAHFQDNL
HSVNRDLNEL ERLSNLVGKP SENHPLHNSG LLSLDPVQDK TPLYSQLLQA YKWSNKLQYH
AGLASGLLNQ QSLKRSANQM GVSAKRRPKA QPTTLVLPPQ YVDDVISRID RMFPEMSIHL
SRPNGTSAML LVTLGKVLKV IVVMRSLFID RTIVKGYNEN VYTEDGKLDI WSKSNYQVFQ
KVTDHATTAL LHYQLPQMPD VVVRSFMTWL RSYIKLFQAP CQRCGKFLQD GLPPTWRDFR
TLEAFHDTCR Q
