ST65G_HUMAN
ID ST65G_HUMAN Reviewed; 414 AA.
AC O94864; B4E3W3; Q6IB21; Q9H2T6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=STAGA complex 65 subunit gamma;
DE AltName: Full=Adenocarcinoma antigen ART1;
DE AltName: Full=SPTF-associated factor 65 gamma;
DE Short=STAF65gamma;
DE AltName: Full=Suppressor of Ty 7-like;
GN Name=SUPT7L; Synonyms=KIAA0764;
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] (ISOFORMS 1 AND 2).
RX PubMed=10987294;
RA Nishizaka S., Gomi S., Harada K., Oizumi K., Itoh K., Shichijo S.;
RT "A new tumor-rejection antigen recognized by cytotoxic T lymphocytes
RT infiltrating into a lung adenocarcinoma.";
RL Cancer Res. 60:4830-4837(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [7]
RP SUBCELLULAR LOCATION, IDENTIFICATION AS PART OF THE STAGA COMPLEX WITH
RP SUPT3H; GCN5L2; TRRAP; TAF5L; TAF6L; TADA3L; TAF10; TAF12 AND TAF9, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [8]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [9]
RP IDENTIFICATION IN THE TFTC COMPLEX.
RX PubMed=17375202; DOI=10.1371/journal.pone.0000316;
RA Demeny M.A., Soutoglou E., Nagy Z., Scheer E., Janoshazi A., Richardot M.,
RA Argentini M., Kessler P., Tora L.;
RT "Identification of a small TAF complex and its role in the assembly of TAF-
RT containing complexes.";
RL PLoS ONE 2:E316-E316(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-334, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271, AND IDENTIFICATION BY MASS
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271, AND IDENTIFICATION BY MASS
RP 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
CC -!- SUBUNIT: Component of the STAGA transcription coactivator-HAT complex,
CC at least composed of SUPT3H, SUPT7L, GCN5L2, TAF5L, TAF6L, TADA3L,
CC TAD1L, TAF10, TAF12 and TAF9. {ECO:0000269|PubMed:17375202}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94864-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94864-2; Sequence=VSP_003974;
CC Name=3;
CC IsoId=O94864-4; Sequence=VSP_054839;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in adenocarcinomas and
CC gliomas and low in esophageal cancers and malignant hematological
CC disease. Also expressed at high level in the thymus, low in peripheral
CC blood mononuclear cells, and lowest in the stomach, small intestine,
CC and skeletal muscle.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34484.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF197954; AAG28523.1; -; mRNA.
DR EMBL; AF224759; AAG47636.1; -; mRNA.
DR EMBL; AB018307; BAA34484.2; ALT_INIT; mRNA.
DR EMBL; AK304889; BAG65625.1; -; mRNA.
DR EMBL; CR456983; CAG33264.1; -; mRNA.
DR EMBL; AC074091; AAX93202.1; -; Genomic_DNA.
DR EMBL; BC074000; AAH74000.1; -; mRNA.
DR CCDS; CCDS42667.1; -. [O94864-1]
DR CCDS; CCDS62885.1; -. [O94864-2]
DR CCDS; CCDS62886.1; -. [O94864-4]
DR RefSeq; NP_001269658.1; NM_001282729.1. [O94864-1]
DR RefSeq; NP_001269659.1; NM_001282730.1. [O94864-2]
DR RefSeq; NP_001269660.1; NM_001282731.1. [O94864-2]
DR RefSeq; NP_001269661.1; NM_001282732.1. [O94864-4]
DR RefSeq; NP_055675.1; NM_014860.2. [O94864-1]
DR RefSeq; XP_005264729.1; XM_005264672.4. [O94864-2]
DR PDB; 7KTR; EM; 2.93 A; D=51-414.
DR PDB; 7KTS; EM; 19.09 A; D=1-414.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; O94864; -.
DR SMR; O94864; -.
DR BioGRID; 115242; 65.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR CORUM; O94864; -.
DR IntAct; O94864; 21.
DR MINT; O94864; -.
DR STRING; 9606.ENSP00000336750; -.
DR GlyGen; O94864; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94864; -.
DR PhosphoSitePlus; O94864; -.
DR BioMuta; SUPT7L; -.
DR EPD; O94864; -.
DR jPOST; O94864; -.
DR MassIVE; O94864; -.
DR MaxQB; O94864; -.
DR PaxDb; O94864; -.
DR PeptideAtlas; O94864; -.
DR PRIDE; O94864; -.
DR ProteomicsDB; 50503; -. [O94864-1]
DR ProteomicsDB; 50504; -. [O94864-2]
DR Antibodypedia; 50579; 99 antibodies from 18 providers.
DR DNASU; 9913; -.
DR Ensembl; ENST00000337768.10; ENSP00000336750.5; ENSG00000119760.16. [O94864-1]
DR Ensembl; ENST00000404798.6; ENSP00000385218.2; ENSG00000119760.16. [O94864-4]
DR Ensembl; ENST00000405491.5; ENSP00000384469.1; ENSG00000119760.16. [O94864-2]
DR Ensembl; ENST00000406540.5; ENSP00000385436.1; ENSG00000119760.16. [O94864-2]
DR Ensembl; ENST00000464789.2; ENSP00000441110.1; ENSG00000119760.16. [O94864-2]
DR GeneID; 9913; -.
DR KEGG; hsa:9913; -.
DR MANE-Select; ENST00000337768.10; ENSP00000336750.5; NM_014860.3; NP_055675.1.
DR UCSC; uc002rli.3; human. [O94864-1]
DR CTD; 9913; -.
DR DisGeNET; 9913; -.
DR GeneCards; SUPT7L; -.
DR HGNC; HGNC:30632; SUPT7L.
DR HPA; ENSG00000119760; Low tissue specificity.
DR MIM; 612762; gene.
DR neXtProt; NX_O94864; -.
DR OpenTargets; ENSG00000119760; -.
DR PharmGKB; PA142670854; -.
DR VEuPathDB; HostDB:ENSG00000119760; -.
DR eggNOG; ENOG502QQTJ; Eukaryota.
DR GeneTree; ENSGT00390000005572; -.
DR HOGENOM; CLU_055453_1_0_1; -.
DR InParanoid; O94864; -.
DR OMA; YEKIVNP; -.
DR OrthoDB; 1243197at2759; -.
DR PhylomeDB; O94864; -.
DR TreeFam; TF328615; -.
DR PathwayCommons; O94864; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O94864; -.
DR BioGRID-ORCS; 9913; 72 hits in 1092 CRISPR screens.
DR ChiTaRS; SUPT7L; human.
DR GeneWiki; SUPT7L; -.
DR GenomeRNAi; 9913; -.
DR Pharos; O94864; Tdark.
DR PRO; PR:O94864; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O94864; protein.
DR Bgee; ENSG00000119760; Expressed in middle temporal gyrus and 197 other tissues.
DR Genevisible; O94864; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:HGNC-UCL.
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 Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR039460; SUPT7L.
DR PANTHER; PTHR28598; PTHR28598; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR SMART; SM00576; BTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..414
FT /note="STAGA complex 65 subunit gamma"
FT /id="PRO_0000072233"
FT REGION 87..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 271
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:28112733"
FT VAR_SEQ 1..4
FT /note="MNLQ -> ML (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10987294"
FT /id="VSP_003974"
FT VAR_SEQ 5..140
FT /note="RYWGEIPISSSQTNRSSFDLLPREFRLVEVHDPPLHQPSANKPKPPTMLDIP
FT SEPCSLTIHTIQLIQHNRRLRNLIATAQAQNQQQTEGVKTEESEPLPSCPGSPPLPDDL
FT LPLDCKNPNAPFQIRHSDPESDFYR -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054839"
FT HELIX 58..86
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 151..169
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 176..207
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 240..261
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 414 AA; 46193 MW; 59724A96353D44D5 CRC64;
MNLQRYWGEI PISSSQTNRS SFDLLPREFR LVEVHDPPLH QPSANKPKPP TMLDIPSEPC
SLTIHTIQLI QHNRRLRNLI ATAQAQNQQQ TEGVKTEESE PLPSCPGSPP LPDDLLPLDC
KNPNAPFQIR HSDPESDFYR GKGEPVTELS WHSCRQLLYQ AVATILAHAG FDCANESVLE
TLTDVAHEYC LKFTKLLRFA VDREARLGQT PFPDVMEQVF HEVGIGSVLS LQKFWQHRIK
DYHSYMLQIS KQLSEEYERI VNPEKATEDA KPVKIKEEPV SDITFPVSEE LEADLASGDQ
SLPMGVLGAQ SERFPSNLEV EASPQASSAE VNASPLWNLA HVKMEPQESE EGNVSGHGVL
GSDVFEEPMS GMSEAGIPQS PDDSDSSYGS HSTDSLMGSS PVFNQRCKKR MRKI
