UVSSA_HUMAN
ID UVSSA_HUMAN Reviewed; 709 AA.
AC Q2YD98; A8K9E6; B2RU11; Q8WTX4; Q9P1Z8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=UV-stimulated scaffold protein A;
GN Name=UVSSA; Synonyms=KIAA1530;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-620.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-620.
RC TISSUE=Thymus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-620.
RC TISSUE=Duodenum, Lung, and Skin;
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 [5]
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-287, 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 [7]
RP FUNCTION, INVOLVEMENT IN UVSS3, MUTAGENESIS OF TRP-120 AND
RP 157-ARG--ARG-159, VARIANT UVSS3 ARG-32, AND CHARACTERIZATION OF VARIANT
RP UVSS3 ARG-32.
RX PubMed=22466610; DOI=10.1038/ng.2229;
RA Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M., Nardo T.,
RA Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M., Kinoshita A.,
RA Ono S., Takenaka K., Masuyama R., Kudo T., Slor H., Utani A., Tateishi S.,
RA Yamashita S., Stefanini M., Lehmann A.R., Yoshiura K.I., Ogi T.;
RT "Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase
RT IIo processing in transcription-coupled nucleotide-excision repair.";
RL Nat. Genet. 44:586-592(2012).
RN [8]
RP FUNCTION, INVOLVEMENT IN UVSS3, SUBCELLULAR LOCATION, UBIQUITINATION, AND
RP INTERACTION WITH USP7.
RX PubMed=22466611; DOI=10.1038/ng.2230;
RA Schwertman P., Lagarou A., Dekkers D.H., Raams A., van der Hoek A.C.,
RA Laffeber C., Hoeijmakers J.H., Demmers J.A., Fousteri M., Vermeulen W.,
RA Marteijn J.A.;
RT "UV-sensitive syndrome protein UVSSA recruits USP7 to regulate
RT transcription-coupled repair.";
RL Nat. Genet. 44:598-602(2012).
RN [9]
RP FUNCTION, INVOLVEMENT IN UVSS3, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ERCC6; ERCC8 AND USP7.
RX PubMed=22466612; DOI=10.1038/ng.2228;
RA Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I.,
RA Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.;
RT "Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in
RT transcription-coupled DNA repair.";
RL Nat. Genet. 44:593-597(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
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).
CC -!- FUNCTION: Factor involved in transcription-coupled nucleotide excision
CC repair (TC-NER) in response to UV damage. TC-NER allows RNA polymerase
CC II-blocking lesions to be rapidly removed from the transcribed strand
CC of active genes. Acts by promoting stabilization of ERCC6 by recruiting
CC deubiquitinating enzyme USP7 to TC-NER complexes, preventing UV-induced
CC degradation of ERCC6 by the proteasome. Interacts with the elongating
CC form of RNA polymerase II (RNA pol IIo) and facilitates its
CC ubiquitination at UV damage sites, leading to promote RNA pol IIo
CC backtracking to allow access to the nucleotide excision repair
CC machinery. Not involved in processing oxidative damage.
CC {ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611,
CC ECO:0000269|PubMed:22466612}.
CC -!- SUBUNIT: Interacts with the elongating form of RNA polymerase II (RNA
CC pol IIo). Interacts with ERCC6, ERCC8 and USP7.
CC {ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612}.
CC -!- INTERACTION:
CC Q2YD98; O00505: KPNA3; NbExp=3; IntAct=EBI-11153331, EBI-358297;
CC Q2YD98; P43358: MAGEA4; NbExp=3; IntAct=EBI-11153331, EBI-743122;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:22466611,
CC ECO:0000269|PubMed:22466612}. Note=Accumulates at UV DNA damage sites.
CC {ECO:0000269|PubMed:22466611}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2YD98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2YD98-2; Sequence=VSP_030932;
CC -!- PTM: Monoubiquitinated: ubiquitination does not increase in response to
CC UV. {ECO:0000269|PubMed:22466611}.
CC -!- DISEASE: UV-sensitive syndrome 3 (UVSS3) [MIM:614640]: An autosomal
CC recessive disorder characterized by cutaneous photosensitivity and
CC slight dyspigmentation, without an increased risk of skin tumors.
CC {ECO:0000269|PubMed:22466610, ECO:0000269|PubMed:22466611,
CC ECO:0000269|PubMed:22466612}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the UVSSA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96054.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB040963; BAA96054.1; ALT_INIT; mRNA.
DR EMBL; AK292661; BAF85350.1; -; mRNA.
DR EMBL; AC078852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021930; AAH21930.1; -; mRNA.
DR EMBL; BC110331; AAI10332.1; -; mRNA.
DR EMBL; BC140901; AAI40902.1; -; mRNA.
DR CCDS; CCDS33938.1; -. [Q2YD98-1]
DR RefSeq; NP_001304863.1; NM_001317934.1. [Q2YD98-1]
DR RefSeq; NP_001304864.1; NM_001317935.1. [Q2YD98-1]
DR RefSeq; NP_065945.2; NM_020894.3. [Q2YD98-1]
DR RefSeq; XP_016863979.1; XM_017008490.1. [Q2YD98-1]
DR RefSeq; XP_016863980.1; XM_017008491.1. [Q2YD98-1]
DR RefSeq; XP_016863981.1; XM_017008492.1. [Q2YD98-1]
DR RefSeq; XP_016863982.1; XM_017008493.1. [Q2YD98-1]
DR RefSeq; XP_016863983.1; XM_017008494.1. [Q2YD98-1]
DR PDB; 5XV8; NMR; -; A=390-434.
DR PDB; 7OO3; EM; 2.80 A; c=1-709.
DR PDB; 7OOP; EM; 2.90 A; c=1-709.
DR PDB; 7OPC; EM; 3.00 A; c=1-709.
DR PDB; 7OPD; EM; 3.00 A; c=1-709.
DR PDBsum; 5XV8; -.
DR PDBsum; 7OO3; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; Q2YD98; -.
DR SMR; Q2YD98; -.
DR BioGRID; 121689; 36.
DR IntAct; Q2YD98; 6.
DR MINT; Q2YD98; -.
DR STRING; 9606.ENSP00000374501; -.
DR iPTMnet; Q2YD98; -.
DR PhosphoSitePlus; Q2YD98; -.
DR BioMuta; UVSSA; -.
DR DMDM; 296434546; -.
DR EPD; Q2YD98; -.
DR jPOST; Q2YD98; -.
DR MassIVE; Q2YD98; -.
DR MaxQB; Q2YD98; -.
DR PaxDb; Q2YD98; -.
DR PeptideAtlas; Q2YD98; -.
DR PRIDE; Q2YD98; -.
DR ProteomicsDB; 61547; -. [Q2YD98-1]
DR ProteomicsDB; 61548; -. [Q2YD98-2]
DR Antibodypedia; 22237; 52 antibodies from 18 providers.
DR DNASU; 57654; -.
DR Ensembl; ENST00000389851.10; ENSP00000374501.4; ENSG00000163945.19. [Q2YD98-1]
DR Ensembl; ENST00000507531.5; ENSP00000421741.1; ENSG00000163945.19. [Q2YD98-1]
DR Ensembl; ENST00000511216.6; ENSP00000425130.1; ENSG00000163945.19. [Q2YD98-1]
DR Ensembl; ENST00000512728.5; ENSP00000427701.1; ENSG00000163945.19. [Q2YD98-2]
DR Ensembl; ENST00000677286.1; ENSP00000503948.1; ENSG00000163945.19. [Q2YD98-1]
DR Ensembl; ENST00000679192.1; ENSP00000504544.1; ENSG00000163945.19. [Q2YD98-1]
DR GeneID; 57654; -.
DR KEGG; hsa:57654; -.
DR MANE-Select; ENST00000389851.10; ENSP00000374501.4; NM_020894.4; NP_065945.2.
DR UCSC; uc003gde.5; human. [Q2YD98-1]
DR CTD; 57654; -.
DR DisGeNET; 57654; -.
DR GeneCards; UVSSA; -.
DR HGNC; HGNC:29304; UVSSA.
DR HPA; ENSG00000163945; Low tissue specificity.
DR MalaCards; UVSSA; -.
DR MIM; 614632; gene.
DR MIM; 614640; phenotype.
DR neXtProt; NX_Q2YD98; -.
DR OpenTargets; ENSG00000163945; -.
DR Orphanet; 178338; UV-sensitive syndrome.
DR PharmGKB; PA162393105; -.
DR VEuPathDB; HostDB:ENSG00000163945; -.
DR eggNOG; KOG2374; Eukaryota.
DR GeneTree; ENSGT00390000000377; -.
DR HOGENOM; CLU_023577_0_0_1; -.
DR InParanoid; Q2YD98; -.
DR OMA; TSEHRFW; -.
DR OrthoDB; 996127at2759; -.
DR PhylomeDB; Q2YD98; -.
DR TreeFam; TF321660; -.
DR PathwayCommons; Q2YD98; -.
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 SignaLink; Q2YD98; -.
DR BioGRID-ORCS; 57654; 26 hits in 1077 CRISPR screens.
DR ChiTaRS; UVSSA; human.
DR GeneWiki; KIAA1530; -.
DR GenomeRNAi; 57654; -.
DR Pharos; Q2YD98; Tbio.
DR PRO; PR:Q2YD98; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q2YD98; protein.
DR Bgee; ENSG00000163945; Expressed in oviduct epithelium and 181 other tissues.
DR ExpressionAtlas; Q2YD98; baseline and differential.
DR Genevisible; Q2YD98; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IMP:UniProtKB.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:UniProtKB.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR018610; UVSSA.
DR PANTHER; PTHR28670; PTHR28670; 1.
DR Pfam; PF09740; DUF2043; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Coiled coil;
KW Disease variant; DNA damage; DNA repair; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..709
FT /note="UV-stimulated scaffold protein A"
FT /id="PRO_0000317282"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..145
FT /note="VHS-like"
FT REGION 230..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..199
FT /evidence="ECO:0000255"
FT COMPBIAS 588..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..449
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030932"
FT VARIANT 32
FT /note="C -> R (in UVSS3; mild phenotype; impairs
FT transcription-coupled nucleotide excision repair ability;
FT dbSNP:rs387907164)"
FT /evidence="ECO:0000269|PubMed:22466610"
FT /id="VAR_067798"
FT VARIANT 391
FT /note="R -> H (in dbSNP:rs2276904)"
FT /id="VAR_038499"
FT VARIANT 620
FT /note="P -> L (in dbSNP:rs28522910)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_038500"
FT MUTAGEN 120
FT /note="W->A: Impairs transcription-coupled nucleotide
FT excision repair ability."
FT /evidence="ECO:0000269|PubMed:22466610"
FT MUTAGEN 157..159
FT /note="RKR->EEE: Impairs transcription-coupled nucleotide
FT excision repair ability."
FT /evidence="ECO:0000269|PubMed:22466610"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:7OO3"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:7OO3"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:7OO3"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:7OO3"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:7OO3"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:5XV8"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:5XV8"
SQ SEQUENCE 709 AA; 80591 MW; 34698BE37A43BF2F CRC64;
MDQKLSKLVE ELTTSGEPRL NPEKMKELKK ICKSSEEQLS RAYRLLIAQL TQEHAEIRLS
AFQIVEELFV RSHQFRMLVV SNFQEFLELT LGTDPAQPLP PPREAAQRLR QATTRAVEGW
NEKFGEAYKK LALGYHFLRH NKKVDFQDTN ARSLAERKRE EEKQKHLDKI YQERASQAER
EMQEMSGEIE SCLTEVESCF RLLVPFDFDP NPETESLGMA SGMSDALRSS CAGQVGPCRS
GTPDPRDGEQ PCCSRDLPAS AGHPRAGGGA QPSQTATGDP SDEDEDSDLE EFVRSHGLGS
HKYTLDVELC SEGLKVQENE DNLALIHAAR DTLKLIRNKF LPAVCSWIQR FTRVGTHGGC
LKRAIDLKAE LELVLRKYKE LDIEPEGGER RRTEALGDAE EDEDDEDFVE VPEKEGYEPH
IPDHLRPEYG LEAAPEKDTV VRCLRTRTRM DEEVSDPTSA AAQLRQLRDH LPPPSSASPS
RALPEPQEAQ KLAAERARAP VVPYGVDLHY WGQELPTAGK IVKSDSQHRF WKPSEVEEEV
VNADISEMLR SRHITFAGKF EPVQHWCRAP RPDGRLCERQ DRLKCPFHGK IVPRDDEGRP
LDPEDRAREQ RRQLQKQERP EWQDPELMRD VEAATGQDLG SSRYSGKGRG KKRRYPSLTN
LKAQADTARA RIGRKVFAKA AVRRVVAAMN RMDQKKHEKF SNQFNYALN
