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Database: UniProt
Entry: Q9HCS7
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Original site: Q9HCS7 
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   29-SEP-2021, entry version 197.
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   SMR; Q9HCS7; -.
DR   BioGRID; 121273; 118.
DR   CORUM; Q9HCS7; -.
DR   DIP; DIP-31646N; -.
DR   IntAct; Q9HCS7; 62.
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; 297 antibodies.
DR   DNASU; 56949; -.
DR   Ensembl; ENST00000358368; ENSP00000351137; ENSG00000076924.
DR   GeneID; 56949; -.
DR   KEGG; hsa:56949; -.
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; KIWYNYL; -.
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   BioGRID-ORCS; 56949; 791 hits in 1019 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 lobe of thyroid gland and 177 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; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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
//
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