MED16_HUMAN
ID MED16_HUMAN Reviewed; 877 AA.
AC Q9Y2X0; Q6PJT2; Q96AD4; Q96I35; Q9Y652;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 16;
DE AltName: Full=Mediator complex subunit 16;
DE AltName: Full=Thyroid hormone receptor-associated protein 5;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 95 kDa component;
DE Short=Trap95;
DE AltName: Full=Vitamin D3 receptor-interacting protein complex 92 kDa component;
DE Short=DRIP92;
GN Name=MED16; Synonyms=DRIP92 {ECO:0000312|EMBL:AAD31087.1}, THRAP5;
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] {ECO:0000305, ECO:0000312|EMBL:AAD30032.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 277-283,
RP IDENTIFICATION IN TRAP COMPLEX, AND FUNCTION OF TRAP COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=10198638; DOI=10.1016/s1097-2765(00)80463-3;
RA Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y.,
RA Zhang X., Qin J., Roeder R.G.;
RT "Identity between TRAP and SMCC complexes indicates novel pathways for the
RT function of nuclear receptors and diverse mammalian activators.";
RL Mol. Cell 3:361-370(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD31087.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF 27-42 AND
RP 755-772, IDENTIFICATION IN ARC COMPLEX, AND FUNCTION OF ARC COMPLEX.
RC TISSUE=B-cell {ECO:0000269|PubMed:10235266};
RX PubMed=10235266; DOI=10.1038/19783;
RA Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
RA Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT "Ligand-dependent transcription activation by nuclear receptors requires
RT the DRIP complex.";
RL Nature 398:824-828(1999).
RN [3] {ECO:0000312|EMBL:AAH11841.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 248-877 (ISOFORM 4).
RC TISSUE=Skin {ECO:0000312|EMBL:AAH17282.1}, and
RC Uterus {ECO:0000312|EMBL:AAH11841.1};
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]
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 [5]
RP INTERACTION WITH MED1; MED10; MED21 AND MED30, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND ASSOCIATION OF
RP 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).
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:10198638,
CC ECO:0000269|PubMed:10235266}.
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:10198638, ECO:0000269|PubMed:10235266,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q9Y2X0; O60244: MED14; NbExp=2; IntAct=EBI-394541, EBI-394489;
CC Q9Y2X0; Q9ULK4: MED23; NbExp=4; IntAct=EBI-394541, EBI-311161;
CC Q9Y2X0; O75448: MED24; NbExp=2; IntAct=EBI-394541, EBI-394523;
CC Q9Y2X0; Q71SY5: MED25; NbExp=3; IntAct=EBI-394541, EBI-394558;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:10198638};
CC IsoId=Q9Y2X0-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9Y2X0-2; Sequence=VSP_051724;
CC Name=3 {ECO:0000305};
CC IsoId=Q9Y2X0-3; Sequence=VSP_051722, VSP_051724;
CC Name=4 {ECO:0000305};
CC IsoId=Q9Y2X0-4; Sequence=VSP_051721, VSP_051723;
CC Name=5;
CC IsoId=Q9Y2X0-5; Sequence=VSP_028749, VSP_028750;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 16 family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-13 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31087.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF121228; AAD30032.1; -; mRNA.
DR EMBL; AF106934; AAD31087.1; ALT_FRAME; mRNA.
DR EMBL; BC004554; AAH04554.1; -; mRNA.
DR EMBL; BC007853; AAH07853.2; -; mRNA.
DR EMBL; BC011841; AAH11841.1; -; mRNA.
DR EMBL; BC017282; AAH17282.1; -; mRNA.
DR CCDS; CCDS12047.1; -. [Q9Y2X0-1]
DR RefSeq; NP_005472.2; NM_005481.2. [Q9Y2X0-1]
DR PDB; 7EMF; EM; 3.50 A; P=1-828.
DR PDB; 7ENA; EM; 4.07 A; p=1-828.
DR PDB; 7ENC; EM; 4.13 A; p=1-828.
DR PDB; 7ENJ; EM; 4.40 A; P=1-877.
DR PDB; 7LBM; EM; 4.80 A; 0=1-828.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; Q9Y2X0; -.
DR SMR; Q9Y2X0; -.
DR BioGRID; 115342; 102.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9Y2X0; -.
DR DIP; DIP-31463N; -.
DR IntAct; Q9Y2X0; 45.
DR MINT; Q9Y2X0; -.
DR STRING; 9606.ENSP00000325612; -.
DR iPTMnet; Q9Y2X0; -.
DR PhosphoSitePlus; Q9Y2X0; -.
DR BioMuta; MED16; -.
DR DMDM; 62511180; -.
DR EPD; Q9Y2X0; -.
DR jPOST; Q9Y2X0; -.
DR MassIVE; Q9Y2X0; -.
DR MaxQB; Q9Y2X0; -.
DR PaxDb; Q9Y2X0; -.
DR PeptideAtlas; Q9Y2X0; -.
DR PRIDE; Q9Y2X0; -.
DR ProteomicsDB; 85922; -. [Q9Y2X0-1]
DR ProteomicsDB; 85923; -. [Q9Y2X0-2]
DR ProteomicsDB; 85924; -. [Q9Y2X0-3]
DR ProteomicsDB; 85925; -. [Q9Y2X0-4]
DR ProteomicsDB; 85926; -. [Q9Y2X0-5]
DR Antibodypedia; 10226; 191 antibodies from 24 providers.
DR DNASU; 10025; -.
DR Ensembl; ENST00000312090.10; ENSP00000308528.4; ENSG00000175221.16. [Q9Y2X0-3]
DR Ensembl; ENST00000325464.6; ENSP00000325612.1; ENSG00000175221.16. [Q9Y2X0-1]
DR Ensembl; ENST00000395808.7; ENSP00000379153.1; ENSG00000175221.16. [Q9Y2X0-2]
DR GeneID; 10025; -.
DR KEGG; hsa:10025; -.
DR MANE-Select; ENST00000325464.6; ENSP00000325612.1; NM_005481.3; NP_005472.2.
DR UCSC; uc002lqd.2; human. [Q9Y2X0-1]
DR CTD; 10025; -.
DR DisGeNET; 10025; -.
DR GeneCards; MED16; -.
DR HGNC; HGNC:17556; MED16.
DR HPA; ENSG00000175221; Low tissue specificity.
DR MIM; 604062; gene.
DR neXtProt; NX_Q9Y2X0; -.
DR OpenTargets; ENSG00000175221; -.
DR PharmGKB; PA162395406; -.
DR VEuPathDB; HostDB:ENSG00000175221; -.
DR eggNOG; ENOG502QQ3H; Eukaryota.
DR GeneTree; ENSGT00390000003821; -.
DR HOGENOM; CLU_018773_0_0_1; -.
DR InParanoid; Q9Y2X0; -.
DR OMA; DSHAQLH; -.
DR OrthoDB; 493637at2759; -.
DR PhylomeDB; Q9Y2X0; -.
DR PathwayCommons; Q9Y2X0; -.
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; Q9Y2X0; -.
DR SIGNOR; Q9Y2X0; -.
DR BioGRID-ORCS; 10025; 148 hits in 1104 CRISPR screens.
DR ChiTaRS; MED16; human.
DR GeneWiki; MED16; -.
DR GenomeRNAi; 10025; -.
DR Pharos; Q9Y2X0; Tbio.
DR PRO; PR:Q9Y2X0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2X0; protein.
DR Bgee; ENSG00000175221; Expressed in lower esophagus mucosa and 93 other tissues.
DR ExpressionAtlas; Q9Y2X0; baseline and differential.
DR Genevisible; Q9Y2X0; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021665; Mediator_Med16.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13224; PTHR13224; 1.
DR Pfam; PF11635; Med16; 1.
DR SMART; SM00320; WD40; 1.
DR SUPFAM; SSF50952; SSF50952; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..877
FT /note="Mediator of RNA polymerase II transcription subunit
FT 16"
FT /id="PRO_0000051292"
FT REPEAT 21..71
FT /note="WD 1"
FT REPEAT 72..119
FT /note="WD 2"
FT REPEAT 120..165
FT /note="WD 3"
FT REPEAT 166..203
FT /note="WD 4"
FT REPEAT 204..257
FT /note="WD 5"
FT REPEAT 258..334
FT /note="WD 6"
FT REPEAT 335..415
FT /note="WD 7"
FT REPEAT 416..460
FT /note="WD 8"
FT REPEAT 461..495
FT /note="WD 9"
FT REGION 848..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 636..751
FT /note="GSLLRPGHSFLRDGTSLGMLRELMVVIRIWGLLKPSCLPVYTATSDTQDSMS
FT LLFRLLTKLWICCRDEGPASEPDEALVDECCLLPSQLLIPSLDWLPASDGLVSRLQPKQ
FT PLRLQ -> VAMRAQRASRTRRWWMNAACCPASCLSPAWTGCQPATAWLAACSPSSPFV
FT CSLAGRPRCLAVLPPCSSTASPGPQASPRSTTCGGCTLALAPRRNARPAPGAAVSPCSS
FT RPTEPRR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051721"
FT VAR_SEQ 636..663
FT /note="GSLLRPGHSFLRDGTSLGMLRELMVVIR -> PCPTSEPCPTSEPSPTSEPS
FT PTSEPSSP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10235266"
FT /id="VSP_028749"
FT VAR_SEQ 664..877
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10235266"
FT /id="VSP_028750"
FT VAR_SEQ 700
FT /note="C -> FPSTGPCSVWVLLGWQPLPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051722"
FT VAR_SEQ 752..877
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051723"
FT VAR_SEQ 829..877
FT /note="AVEGRGPDACVTSRASEEAPAFVQLGPQSTHHSPRTPRSLDHLHPEDRP ->
FT CGGLWWRVPLSYP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10235266,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051724"
FT VARIANT 770
FT /note="L -> F (in dbSNP:rs34859566)"
FT /id="VAR_053958"
FT VARIANT 874
FT /note="E -> K (in dbSNP:rs13090)"
FT /id="VAR_053959"
FT CONFLICT 46
FT /note="A -> T (in Ref. 1; AAD30032)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="G -> A (in Ref. 2; AAD31087)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="R -> K (in Ref. 1; AAD30032)"
FT /evidence="ECO:0000305"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 91..103
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 177..193
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 378..389
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 438..450
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 467..483
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 523..534
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 544..563
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 576..586
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 615..631
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 641..646
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 649..668
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 685..700
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 701..704
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 711..718
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 720..723
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 795..801
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 804..808
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 817..820
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 821..823
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 877 AA; 96793 MW; 15173F237A75D230 CRC64;
MCDLRRPAAG GMMDLAYVCE WEKWSKSTHC PSVPLACAWS CRNLIAFTMD LRSDDQDLTR
MIHILDTEHP WDLHSIPSEH HEAITCLEWD QSGSRLLSAD ADGQIKCWSM ADHLANSWES
SVGSLVEGDP IVALSWLHNG VKLALHVEKS GASSFGEKFS RVKFSPSLTL FGGKPMEGWI
AVTVSGLVTV SLLKPSGQVL TSTESLCRLR GRVALADIAF TGGGNIVVAT ADGSSASPVQ
FYKVCVSVVS EKCRIDTEIL PSLFMRCTTD LNRKDKFPAI THLKFLARDM SEQVLLCASS
QTSSIVECWS LRKEGLPVNN IFQQISPVVG DKQPTILKWR ILSATNDLDR VSAVALPKLP
ISLTNTDLKV ASDTQFYPGL GLALAFHDGS VHIVHRLSLQ TMAVFYSSAA PRPVDEPAMK
RPRTAGPAVH LKAMQLSWTS LALVGIDSHG KLSVLRLSPS MGHPLEVGLA LRHLLFLLEY
CMVTGYDWWD ILLHVQPSMV QSLVEKLHEE YTRQTAALQQ VLSTRILAMK ASLCKLSPCT
VTRVCDYHTK LFLIAISSTL KSLLRPHFLN TPDKSPGDRL TEICTKITDV DIDKVMINLK
TEEFVLDMNT LQALQQLLQW VGDFVLYLLA SLPNQGSLLR PGHSFLRDGT SLGMLRELMV
VIRIWGLLKP SCLPVYTATS DTQDSMSLLF RLLTKLWICC RDEGPASEPD EALVDECCLL
PSQLLIPSLD WLPASDGLVS RLQPKQPLRL QFGRAPTLPG SAATLQLDGL ARAPGQPKID
HLRRLHLGAC PTEECKACTR CGCVTMLKSP NRTTAVKQWE QRWIKNCLAV EGRGPDACVT
SRASEEAPAF VQLGPQSTHH SPRTPRSLDH LHPEDRP
