SYF1_HUMAN
ID SYF1_HUMAN Reviewed; 855 AA.
AC Q9HCS7; Q8TET6; Q96HB0; Q96IW0; Q9NRG6; Q9ULP3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Pre-mRNA-splicing factor SYF1;
DE AltName: Full=Protein HCNP;
DE AltName: Full=XPA-binding protein 2;
GN Name=XAB2; Synonyms=HCNP, KIAA1177, SYF1; ORFNames=PP3898;
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 {ECO:0000312|EMBL:BAB15807.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=10944529; DOI=10.1074/jbc.m004936200;
RA Nakatsu Y., Asahina H., Citterio E., Rademakers S., Vermeulen W.,
RA Kamiuchi S., Yeo J.-P., Khaw M.-C., Saijo M., Kodo N., Matsuda T.,
RA Hoeijmakers J.H.J., Tanaka K.;
RT "XAB2, a novel tetratricopeptide repeat protein, involved in transcription-
RT coupled DNA repair and transcription.";
RL J. Biol. Chem. 275:34931-34937(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF86951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF86951.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-126; GLN-454 AND
RP THR-702.
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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] {ECO:0000305, ECO:0000312|EMBL:AAF86951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-855.
RC TISSUE=Spleen;
RA Ohara O., Nagase T., Kikuno R., Okumura K.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-855.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP FUNCTION, AND IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
RX PubMed=17981804; DOI=10.1074/jbc.m706647200;
RA Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y.,
RA Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.;
RT "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription,
RT and transcription-coupled repair.";
RL J. Biol. Chem. 283:940-950(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-420, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851, 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).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE IB COMPLEX,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25599396; DOI=10.1038/nsmb.2951;
RA De I., Bessonov S., Hofele R., dos Santos K., Will C.L., Urlaub H.,
RA Luhrmann R., Pena V.;
RT "The RNA helicase Aquarius exhibits structural adaptations mediating its
RT recruitment to spliceosomes.";
RL Nat. Struct. Mol. Biol. 22:138-144(2015).
RN [16] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [17] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:11991638, PubMed:28502770, PubMed:28076346). Involved in
CC transcription-coupled repair (TCR), transcription and pre-mRNA splicing
CC (PubMed:10944529, PubMed:17981804). {ECO:0000269|PubMed:10944529,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17981804,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- SUBUNIT: Associates with RNA polymerase II, the TCR-specific proteins
CC CKN1/CSA and ERCC6/CSB, and XPA (PubMed:10944529). Identified in the
CC spliceosome C complex (PubMed:11991638, PubMed:28502770,
CC PubMed:28076346). Component of the XAB2 complex, a multimeric protein
CC complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE
CC (PubMed:17981804). Identified in a pentameric intron-binding (IB)
CC complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is
CC incorporated into the spliceosome as a preassembled complex
CC (PubMed:25599396). The IB complex does not contain PRPF19
CC (PubMed:25599396). {ECO:0000269|PubMed:10944529,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17981804,
CC ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770}.
CC -!- INTERACTION:
CC Q9HCS7; O60306: AQR; NbExp=6; IntAct=EBI-295232, EBI-2512328;
CC Q9HCS7; O60231: DHX16; NbExp=2; IntAct=EBI-295232, EBI-311446;
CC Q9HCS7; Q13216: ERCC8; NbExp=3; IntAct=EBI-295232, EBI-295260;
CC Q9HCS7; P42858: HTT; NbExp=3; IntAct=EBI-295232, EBI-466029;
CC Q9HCS7; Q13123: IK; NbExp=2; IntAct=EBI-295232, EBI-713456;
CC Q9HCS7; Q9ULR0: ISY1; NbExp=7; IntAct=EBI-295232, EBI-2557660;
CC Q9HCS7; P24928: POLR2A; NbExp=2; IntAct=EBI-295232, EBI-295301;
CC Q9HCS7; Q9UNP9: PPIE; NbExp=12; IntAct=EBI-295232, EBI-591818;
CC Q9HCS7; Q13435: SF3B2; NbExp=2; IntAct=EBI-295232, EBI-749111;
CC Q9HCS7; P09661: SNRPA1; NbExp=2; IntAct=EBI-295232, EBI-876439;
CC Q9HCS7; Q13573: SNW1; NbExp=2; IntAct=EBI-295232, EBI-632715;
CC Q9HCS7; P23025: XPA; NbExp=2; IntAct=EBI-295232, EBI-295222;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:25599396, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770}. Note=Detected in the splicing complex
CC carrying pre-mRNA. {ECO:0000250|UniProtKB:Q99PK0}.
CC -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86951.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH08778.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84861.1; Type=Miscellaneous discrepancy; Note=Alternative splicing. Incomplete sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hcnp/";
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DR EMBL; AB026111; BAB15807.1; -; mRNA.
DR EMBL; AF226051; AAF86951.1; ALT_FRAME; mRNA.
DR EMBL; AF258567; AAG23770.1; -; mRNA.
DR EMBL; AF547265; AAN17847.1; -; Genomic_DNA.
DR EMBL; BC007208; AAH07208.1; -; mRNA.
DR EMBL; BC008778; AAH08778.1; ALT_INIT; mRNA.
DR EMBL; AK074035; BAB84861.1; ALT_SEQ; mRNA.
DR EMBL; AB033003; BAA86491.1; -; mRNA.
DR CCDS; CCDS32892.1; -.
DR RefSeq; NP_064581.2; NM_020196.2.
DR PDB; 5MQF; EM; 5.90 A; M=1-855.
DR PDB; 5XJC; EM; 3.60 A; I=1-855.
DR PDB; 5YZG; EM; 4.10 A; I=1-855.
DR PDB; 5Z56; EM; 5.10 A; I=1-855.
DR PDB; 5Z57; EM; 6.50 A; I=1-855.
DR PDB; 6FF7; EM; 4.50 A; M=1-855.
DR PDB; 6ICZ; EM; 3.00 A; I=1-855.
DR PDB; 6ID0; EM; 2.90 A; I=1-855.
DR PDB; 6ID1; EM; 2.86 A; I=1-855.
DR PDB; 6QDV; EM; 3.30 A; T=1-855.
DR PDB; 7A5P; EM; 5.00 A; M=1-855.
DR PDB; 7ABI; EM; 8.00 A; M=1-855.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; Q9HCS7; -.
DR SMR; Q9HCS7; -.
DR BioGRID; 121273; 164.
DR CORUM; Q9HCS7; -.
DR DIP; DIP-31646N; -.
DR IntAct; Q9HCS7; 64.
DR MINT; Q9HCS7; -.
DR STRING; 9606.ENSP00000351137; -.
DR GlyGen; Q9HCS7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCS7; -.
DR PhosphoSitePlus; Q9HCS7; -.
DR BioMuta; XAB2; -.
DR DMDM; 25091548; -.
DR EPD; Q9HCS7; -.
DR jPOST; Q9HCS7; -.
DR MassIVE; Q9HCS7; -.
DR MaxQB; Q9HCS7; -.
DR PaxDb; Q9HCS7; -.
DR PeptideAtlas; Q9HCS7; -.
DR PRIDE; Q9HCS7; -.
DR ProteomicsDB; 81796; -.
DR Antibodypedia; 12104; 304 antibodies from 35 providers.
DR DNASU; 56949; -.
DR Ensembl; ENST00000358368.5; ENSP00000351137.3; ENSG00000076924.12.
DR GeneID; 56949; -.
DR KEGG; hsa:56949; -.
DR MANE-Select; ENST00000358368.5; ENSP00000351137.3; NM_020196.3; NP_064581.2.
DR UCSC; uc002mgx.4; human.
DR CTD; 56949; -.
DR DisGeNET; 56949; -.
DR GeneCards; XAB2; -.
DR HGNC; HGNC:14089; XAB2.
DR HPA; ENSG00000076924; Low tissue specificity.
DR MIM; 610850; gene.
DR neXtProt; NX_Q9HCS7; -.
DR OpenTargets; ENSG00000076924; -.
DR PharmGKB; PA134905925; -.
DR VEuPathDB; HostDB:ENSG00000076924; -.
DR eggNOG; KOG2047; Eukaryota.
DR GeneTree; ENSGT00550000075140; -.
DR HOGENOM; CLU_007736_2_1_1; -.
DR InParanoid; Q9HCS7; -.
DR OMA; FLMQQPL; -.
DR OrthoDB; 370051at2759; -.
DR PhylomeDB; Q9HCS7; -.
DR TreeFam; TF300866; -.
DR PathwayCommons; Q9HCS7; -.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9HCS7; -.
DR BioGRID-ORCS; 56949; 796 hits in 1072 CRISPR screens.
DR ChiTaRS; XAB2; human.
DR GeneWiki; XAB2; -.
DR GenomeRNAi; 56949; -.
DR Pharos; Q9HCS7; Tbio.
DR PRO; PR:Q9HCS7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HCS7; protein.
DR Bgee; ENSG00000076924; Expressed in left ovary and 115 other tissues.
DR Genevisible; Q9HCS7; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11246; PTHR11246; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00386; HAT; 11.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA damage; DNA repair; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Spliceosome; Transcription.
FT CHAIN 1..855
FT /note="Pre-mRNA-splicing factor SYF1"
FT /id="PRO_0000106414"
FT REPEAT 15..47
FT /note="HAT 1"
FT /evidence="ECO:0000305"
FT REPEAT 48..80
FT /note="HAT 2"
FT /evidence="ECO:0000305"
FT REPEAT 90..122
FT /note="HAT 3"
FT /evidence="ECO:0000305"
FT REPEAT 124..158
FT /note="HAT 4"
FT /evidence="ECO:0000305"
FT REPEAT 160..192
FT /note="HAT 5"
FT /evidence="ECO:0000305"
FT REPEAT 198..230
FT /note="HAT 6"
FT REPEAT 235..268
FT /note="HAT 7"
FT REPEAT 270..305
FT /note="HAT 8"
FT REPEAT 369..407
FT /note="HAT 9"
FT REPEAT 498..530
FT /note="HAT 10"
FT REPEAT 532..566
FT /note="HAT 11"
FT REPEAT 571..605
FT /note="HAT 12"
FT REPEAT 643..677
FT /note="HAT 13"
FT REPEAT 679..713
FT /note="HAT 14"
FT REGION 810..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..834
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 420
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 126
FT /note="V -> I (in dbSNP:rs4134822)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016248"
FT VARIANT 454
FT /note="R -> Q (in dbSNP:rs4134850)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016249"
FT VARIANT 702
FT /note="A -> T (in dbSNP:rs4134865)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016250"
FT CONFLICT 68
FT /note="Y -> T (in Ref. 2; AAF86951)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="L -> M (in Ref. 1; BAB15807)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="E -> K (in Ref. 5; AAH08778)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="A -> V (in Ref. 2; AAF86951)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="E -> K (in Ref. 2; AAF86951)"
FT /evidence="ECO:0000305"
FT CONFLICT 751..753
FT /note="SAT -> IP (in Ref. 2; AAF86951)"
FT /evidence="ECO:0000305"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 405..417
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 424..438
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 465..476
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 508..523
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 528..541
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 570..579
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 587..597
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 602..635
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 641..652
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 664..675
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 707..719
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 723..733
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 741..755
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 761..772
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 780..791
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 793..798
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 799..817
FT /evidence="ECO:0007829|PDB:6ID1"
SQ SEQUENCE 855 AA; 100010 MW; CF766917CD65F6FD CRC64;
MVVMARLSRP ERPDLVFEEE DLPYEEEIMR NQFSVKCWLR YIEFKQGAPK PRLNQLYERA
LKLLPCSYKL WYRYLKARRA QVKHRCVTDP AYEDVNNCHE RAFVFMHKMP RLWLDYCQFL
MDQGRVTHTR RTFDRALRAL PITQHSRIWP LYLRFLRSHP LPETAVRGYR RFLKLSPESA
EEYIEYLKSS DRLDEAAQRL ATVVNDERFV SKAGKSNYQL WHELCDLISQ NPDKVQSLNV
DAIIRGGLTR FTDQLGKLWC SLADYYIRSG HFEKARDVYE EAIRTVMTVR DFTQVFDSYA
QFEESMIAAK METASELGRE EEDDVDLELR LARFEQLISR RPLLLNSVLL RQNPHHVHEW
HKRVALHQGR PREIINTYTE AVQTVDPFKA TGKPHTLWVA FAKFYEDNGQ LDDARVILEK
ATKVNFKQVD DLASVWCQCG ELELRHENYD EALRLLRKAT ALPARRAEYF DGSEPVQNRV
YKSLKVWSML ADLEESLGTF QSTKAVYDRI LDLRIATPQI VINYAMFLEE HKYFEESFKA
YERGISLFKW PNVSDIWSTY LTKFIARYGG RKLERARDLF EQALDGCPPK YAKTLYLLYA
QLEEEWGLAR HAMAVYERAT RAVEPAQQYD MFNIYIKRAA EIYGVTHTRG IYQKAIEVLS
DEHAREMCLR FADMECKLGE IDRARAIYSF CSQICDPRTT GAFWQTWKDF EVRHGNEDTI
KEMLRIRRSV QATYNTQVNF MASQMLKVSG SATGTVSDLA PGQSGMDDMK LLEQRAEQLA
AEAERDQPLR AQSKILFVRS DASREELAEL AQQVNPEEIQ LGEDEDEDEM DLEPNEVRLE
QQSVPAAVFG SLKED
