SP20H_HUMAN
ID SP20H_HUMAN Reviewed; 779 AA.
AC Q8NEM7; E7ER46; Q71RF3; Q9Y6A6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcription factor SPT20 homolog;
DE AltName: Full=p38-interacting protein;
DE Short=p38IP;
GN Name=SUPT20H; Synonyms=C13orf19, FAM48A; ORFNames=FP757;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Prostate, and Testis;
RX PubMed=11340631; DOI=10.1002/pros.1051;
RA Schmidt U., Fiedler U., Pilarsky C.P., Ehlers W., Fuessel S., Haase M.,
RA Faller G., Sauter G., Wirth M.P.;
RT "Identification of a novel gene on chromosome 13 between BRCA2 and Rb1.";
RL Prostate 47:91-101(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH MAPK14.
RX PubMed=16751104; DOI=10.1016/j.cell.2006.03.048;
RA Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.;
RT "p38 and a p38-interacting protein are critical for downregulation of E-
RT cadherin during mouse gastrulation.";
RL Cell 125:957-969(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 445-779, AND VARIANT MET-773.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, AND IDENTIFICATION BY
RP 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 FUNCTION, INTERACTION WITH ATG9A, AND SUBCELLULAR LOCATION.
RX PubMed=19893488; DOI=10.1038/emboj.2009.321;
RA Webber J.L., Tooze S.A.;
RT "Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and
RT p38IP.";
RL EMBO J. 29:27-40(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or
CC MAPK14) activation during gastrulation. Required for down-regulation of
CC E-cadherin during gastrulation by regulating E-cadherin protein level
CC downstream from NCK-interacting kinase (NIK) and independently of the
CC regulation of transcription by FGF signaling and Snail (By similarity).
CC Required for starvation-induced ATG9A trafficking during autophagy.
CC {ECO:0000250, ECO:0000269|PubMed:19893488}.
CC -!- SUBUNIT: Interacts with MAPK14. Interacts with ATG9A.
CC {ECO:0000269|PubMed:16751104, ECO:0000269|PubMed:19893488}.
CC -!- INTERACTION:
CC Q8NEM7; P54253: ATXN1; NbExp=7; IntAct=EBI-946984, EBI-930964;
CC Q8NEM7; Q16539: MAPK14; NbExp=5; IntAct=EBI-946984, EBI-73946;
CC Q8NEM7-2; Q7Z3C6: ATG9A; NbExp=8; IntAct=EBI-7568679, EBI-727146;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19893488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NEM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEM7-2; Sequence=VSP_014877, VSP_014878, VSP_014879;
CC Name=3;
CC IsoId=Q8NEM7-3; Sequence=VSP_055621, VSP_014878, VSP_014879;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, moderately in brain and
CC pituitary gland. Expressed in several fetal tissues, including lung,
CC brain, thymus and kidney. Expression is down-regulated in malignant
CC prostate tissues. {ECO:0000269|PubMed:11340631}.
CC -!- SIMILARITY: Belongs to the SPT20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15220.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ15220.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AJ130894; CAB62207.1; -; mRNA.
DR EMBL; AF093250; AAD40550.1; -; mRNA.
DR EMBL; AK225376; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL138706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030686; AAH30686.1; -; mRNA.
DR EMBL; AF370384; AAQ15220.1; ALT_SEQ; mRNA.
DR CCDS; CCDS31959.1; -. [Q8NEM7-1]
DR CCDS; CCDS61311.1; -. [Q8NEM7-3]
DR CCDS; CCDS9362.1; -. [Q8NEM7-2]
DR RefSeq; NP_001014308.2; NM_001014286.2. [Q8NEM7-1]
DR RefSeq; NP_001265409.1; NM_001278480.1. [Q8NEM7-3]
DR RefSeq; NP_001265410.1; NM_001278481.1. [Q8NEM7-2]
DR RefSeq; NP_001265411.1; NM_001278482.1. [Q8NEM7-2]
DR RefSeq; NP_060039.1; NM_017569.3. [Q8NEM7-2]
DR PDB; 7KTR; EM; 2.93 A; C=1-728.
DR PDB; 7KTS; EM; 19.09 A; C=1-728.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; Q8NEM7; -.
DR SMR; Q8NEM7; -.
DR BioGRID; 120729; 73.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR CORUM; Q8NEM7; -.
DR IntAct; Q8NEM7; 34.
DR MINT; Q8NEM7; -.
DR GlyGen; Q8NEM7; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q8NEM7; -.
DR PhosphoSitePlus; Q8NEM7; -.
DR BioMuta; SUPT20H; -.
DR DMDM; 334302791; -.
DR EPD; Q8NEM7; -.
DR jPOST; Q8NEM7; -.
DR MassIVE; Q8NEM7; -.
DR MaxQB; Q8NEM7; -.
DR PaxDb; Q8NEM7; -.
DR PeptideAtlas; Q8NEM7; -.
DR PRIDE; Q8NEM7; -.
DR ProteomicsDB; 17715; -.
DR ProteomicsDB; 73182; -. [Q8NEM7-1]
DR ProteomicsDB; 73183; -. [Q8NEM7-2]
DR Antibodypedia; 49228; 89 antibodies from 20 providers.
DR DNASU; 55578; -.
DR Ensembl; ENST00000350612.11; ENSP00000218894.10; ENSG00000102710.21. [Q8NEM7-1]
DR Ensembl; ENST00000356185.7; ENSP00000348512.3; ENSG00000102710.21. [Q8NEM7-2]
DR Ensembl; ENST00000360252.8; ENSP00000353388.4; ENSG00000102710.21. [Q8NEM7-2]
DR Ensembl; ENST00000464744.5; ENSP00000419754.1; ENSG00000102710.21. [Q8NEM7-2]
DR Ensembl; ENST00000475892.5; ENSP00000417510.1; ENSG00000102710.21. [Q8NEM7-3]
DR GeneID; 55578; -.
DR KEGG; hsa:55578; -.
DR MANE-Select; ENST00000350612.11; ENSP00000218894.10; NM_001014286.3; NP_001014308.2.
DR UCSC; uc001uwg.4; human. [Q8NEM7-1]
DR CTD; 55578; -.
DR DisGeNET; 55578; -.
DR GeneCards; SUPT20H; -.
DR HGNC; HGNC:20596; SUPT20H.
DR HPA; ENSG00000102710; Tissue enhanced (testis).
DR MIM; 613417; gene.
DR neXtProt; NX_Q8NEM7; -.
DR OpenTargets; ENSG00000102710; -.
DR PharmGKB; PA134985241; -.
DR VEuPathDB; HostDB:ENSG00000102710; -.
DR GeneTree; ENSGT00390000013549; -.
DR HOGENOM; CLU_020200_1_0_1; -.
DR InParanoid; Q8NEM7; -.
DR OMA; XTTATQV; -.
DR OrthoDB; 369747at2759; -.
DR TreeFam; TF329155; -.
DR PathwayCommons; Q8NEM7; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q8NEM7; -.
DR BioGRID-ORCS; 55578; 120 hits in 1092 CRISPR screens.
DR ChiTaRS; SUPT20H; human.
DR GeneWiki; FAM48A; -.
DR GenomeRNAi; 55578; -.
DR Pharos; Q8NEM7; Tbio.
DR PRO; PR:Q8NEM7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8NEM7; protein.
DR Bgee; ENSG00000102710; Expressed in left testis and 202 other tissues.
DR ExpressionAtlas; Q8NEM7; baseline and differential.
DR Genevisible; Q8NEM7; HS.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0070461; C:SAGA-type complex; IDA:BHF-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IC:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR021950; Spt20.
DR PANTHER; PTHR13526; PTHR13526; 2.
DR Pfam; PF12090; Spt20; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Developmental protein;
KW Gastrulation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..779
FT /note="Transcription factor SPT20 homolog"
FT /id="PRO_0000187039"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT00"
FT MOD_RES 494
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT00"
FT VAR_SEQ 55
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11340631,
FT ECO:0000303|PubMed:16751104"
FT /id="VSP_014877"
FT VAR_SEQ 531
FT /note="R -> RSGTPKPSTPTPTPSSTPHPPDAQSSTPSTPSATPTPQDSGFTPQPT
FT LLTQFAQQQRSLSQAMPVTTIPLSTMVTSITPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055621"
FT VAR_SEQ 700..732
FT /note="VLSQLGSAENRPEQSLPQQRFQLSSAFQQQQQQ -> AVAILAASNGYGSSS
FT STNSSATSSSAYRQPVKK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11340631,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16751104"
FT /id="VSP_014878"
FT VAR_SEQ 733..779
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11340631,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16751104"
FT /id="VSP_014879"
FT VARIANT 154
FT /note="M -> V (in dbSNP:rs7324275)"
FT /id="VAR_055798"
FT VARIANT 773
FT /note="T -> M (in dbSNP:rs9469)"
FT /evidence="ECO:0000269|PubMed:15498874"
FT /id="VAR_055799"
FT CONFLICT 707
FT /note="A -> V (in Ref. 5; AAH30686)"
FT /evidence="ECO:0000305"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 399..417
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 779 AA; 85789 MW; 4CD7DFD8719F621C CRC64;
MQQALELALD RAEYVIESAR QRPPKRKYLS SGRKSVFQKL YDLYIEECEK EPEVKKLRRN
VNLLEKLVMQ ETLSCLVVNL YPGNEGYSLM LRGKNGSDSE TIRLPYEEGE LLEYLDAEEL
PPILVDLLEK SQVNIFHCGC VIAEIRDYRQ SSNMKSPGYQ SRHILLRPTM QTLICDVHSI
TSDNHKWTQE DKLLLESQLI LATAEPLCLD PSIAVTCTAN RLLYNKQKMN TRPMKRCFKR
YSRSSLNRQQ DLSHCPPPPQ LRLLDFLQKR KERKAGQHYD LKISKAGNCV DMWKRSPCNL
AIPSEVDVEK YAKVEKSIKS DDSQPTVWPA HDVKDDYVFE CEAGTQYQKT KLTILQSLGD
PLYYGKIQPC KADEESDSQM SPSHSSTDDH SNWFIIGSKT DAERVVNQYQ ELVQNEAKCP
VKMSHSSSGS ASLSQVSPGK ETDQTETVSV QSSVLGKGVK HRPPPIKLPS SSGNSSSGNY
FTPQQTSSFL KSPTPPPSSK PSSIPRKSSV DLNQVSMLSP AALSPASSSQ RTTATQVMAN
SAGLNFINVV GSVCGAQALM SGSNPMLGCN TGAITPAGIN LSGLLPSGGL LPNALPSAMQ
AASQAGVPFG LKNTSSLRPL NLLQLPGGSL IFNTLQQQQQ QLSQFTPQQP QQPTTCSPQQ
PGEQGSEQGS TSQEQALSAQ QAAVINLTGV GSFMQSQAAV LSQLGSAENR PEQSLPQQRF
QLSSAFQQQQ QQIQQLRFLQ HQMAMAAAAA QTAQLHHHRH TGSQSKSKMK RGTPTTPKF
