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 24-JAN-2024, entry version 175. 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 Uterus RC {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}; 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; 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 PDB; 8GXQ; EM; 5.04 A; p=1-828. DR PDB; 8GXS; EM; 4.16 A; p=1-828. DR PDBsum; 7EMF; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7ENJ; -. DR PDBsum; 7LBM; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR AlphaFoldDB; Q9Y2X0; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31191; -. DR EMDB; EMD-31211; -. DR SMR; Q9Y2X0; -. DR BioGRID; 115342; 105. DR ComplexPortal; CPX-3227; Core mediator complex. DR CORUM; Q9Y2X0; -. DR DIP; DIP-31463N; -. DR IntAct; Q9Y2X0; 46. DR MINT; Q9Y2X0; -. DR STRING; 9606.ENSP00000325612; -. DR GlyGen; Q9Y2X0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y2X0; -. DR PhosphoSitePlus; Q9Y2X0; -. DR SwissPalm; Q9Y2X0; -. DR BioMuta; MED16; -. DR DMDM; 62511180; -. DR EPD; Q9Y2X0; -. DR jPOST; Q9Y2X0; -. DR MassIVE; Q9Y2X0; -. DR MaxQB; Q9Y2X0; -. DR PaxDb; 9606-ENSP00000325612; -. DR PeptideAtlas; 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 Pumba; Q9Y2X0; -. DR Antibodypedia; 10226; 208 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 AGR; HGNC:17556; -. 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; EIWQPKE; -. DR OrthoDB; 2938982at2759; -. 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; 162 hits in 1188 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 95 other cell types or tissues. DR ExpressionAtlas; Q9Y2X0; baseline and differential. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; 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; NAS:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR048616; MED16_bridge. DR InterPro; IPR048338; Mediator_Med16. DR InterPro; IPR048339; Mediator_Med16_C. DR InterPro; IPR021665; Mediator_Med16_N. DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR13224:SF6; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 16; 1. DR PANTHER; PTHR13224; THYROID HORMONE RECEPTOR-ASSOCIATED PROTEIN-RELATED; 1. DR Pfam; PF20718; Med16_bridge; 1. DR Pfam; PF20719; Med16_C; 1. DR Pfam; PF11635; Med16_N; 1. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 1. DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q9Y2X0; HS. 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 //