RECQ4_HUMAN
ID RECQ4_HUMAN Reviewed; 1208 AA.
AC O94761; A0A087WZ30; Q3Y424; Q96DW2; Q96F55;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=ATP-dependent DNA helicase Q4;
DE EC=3.6.4.12;
DE AltName: Full=DNA helicase, RecQ-like type 4;
DE Short=RecQ4;
DE AltName: Full=RTS;
DE AltName: Full=RecQ protein-like 4;
GN Name=RECQL4; Synonyms=RECQ4;
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], TISSUE SPECIFICITY, AND VARIANT PRO-92.
RC TISSUE=Testis;
RX PubMed=9878247; DOI=10.1006/geno.1998.5595;
RA Kitao S., Ohsugi I., Ichikawa K., Goto M., Furuichi Y., Shimamoto A.;
RT "Cloning of two new human helicase genes of the RecQ family: biological
RT significance of multiple species in higher eukaryotes.";
RL Genomics 54:443-452(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND VARIANT
RP PRO-92.
RX PubMed=10552928; DOI=10.1006/geno.1999.5959;
RA Kitao S., Lindor N.M., Shiratori M., Furuichi Y., Shimamoto A.;
RT "Rothmund-Thomson syndrome responsible gene, RECQL4: genomic structure and
RT products.";
RL Genomics 61:268-276(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-54; GLY-71; PRO-92;
RP SER-189; ASP-267; THR-273; LYS-301; CYS-522; HIS-522; LEU-591; SER-793;
RP MET-799; THR-964; LYS-976; TRP-1004; GLN-1005; GLN-1021; THR-1045;
RP SER-1105; ASP-1105; HIS-1106; ARG-1113 AND PHE-1148.
RG NIEHS SNPs program;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 468-1208.
RC TISSUE=Lymph, and Placenta;
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 INVOLVEMENT IN RTS2, AND VARIANT RTS2 757-GLN--ARG-1208 DEL.
RX PubMed=10319867; DOI=10.1038/8788;
RA Kitao S., Shimamoto A., Goto M., Miller R.W., Smithson W.A., Lindor N.M.,
RA Furuichi Y.;
RT "Mutations in RECQL4 cause a subset of cases of Rothmund-Thomson
RT syndrome.";
RL Nat. Genet. 22:82-84(1999).
RN [7]
RP INDUCTION.
RX PubMed=11032027; DOI=10.1038/sj.onc.1203841;
RA Kawabe T., Tsuyama N., Kitao S., Nishikawa K., Shimamoto A., Shiratori M.,
RA Matsumoto T., Anno K., Sato T., Mitsui Y., Seki M., Enomoto T., Goto M.,
RA Ellis N.A., Ide T., Furuichi Y., Sugimoto M.;
RT "Differential regulation of human RecQ family helicases in cell
RT transformation and cell cycle.";
RL Oncogene 19:4764-4772(2000).
RN [8]
RP INVOLVEMENT IN RTS2.
RX PubMed=10678659;
RX DOI=10.1002/(sici)1096-8628(20000131)90:3<223::aid-ajmg7>3.0.co;2-z;
RA Lindor N.M., Furuichi Y., Kitao S., Shimamoto A., Arndt C., Jalal S.;
RT "Rothmund-Thomson syndrome due to RECQ4 helicase mutations: report and
RT clinical and molecular comparisons with Bloom syndrome and Werner
RT syndrome.";
RL Am. J. Med. Genet. 90:223-228(2000).
RN [9]
RP INVOLVEMENT IN RAPADILINOS.
RX PubMed=12952869; DOI=10.1093/hmg/ddg306;
RA Siitonen H.A., Kopra O., Kaeaeriaeinen H., Haravuori H., Winter R.M.,
RA Saeaemaenen A.-M., Peltonen L., Kestilae M.;
RT "Molecular defect of RAPADILINO syndrome expands the phenotype spectrum of
RT RECQL diseases.";
RL Hum. Mol. Genet. 12:2837-2844(2003).
RN [10]
RP INTERACTION WITH UBR1 AND UBR2, SUBCELLULAR LOCATION, FUNCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15317757; DOI=10.1093/hmg/ddh269;
RA Yin J., Kwon Y.T., Varshavsky A., Wang W.;
RT "RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes,
RT interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
RL Hum. Mol. Genet. 13:2421-2430(2004).
RN [11]
RP INTERACTION WITH MCM10.
RX PubMed=19696745; DOI=10.1038/emboj.2009.235;
RA Xu X., Rochette P.J., Feyissa E.A., Su T.V., Liu Y.;
RT "MCM10 mediates RECQ4 association with MCM2-7 helicase complex during DNA
RT replication.";
RL EMBO J. 28:3005-3014(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-178 AND SER-180, AND
RP IDENTIFICATION BY 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 [13]
RP VARIANTS ASP-267 AND GLN-1005.
RX PubMed=12601557; DOI=10.1007/s100380300016;
RA Roversi G., Beghini A., Zambruno G., Paradisi M., Larizza L.;
RT "Identification of two novel RECQL4exonic SNPs and genomic characterization
RT of the IVS12 minisatellite.";
RL J. Hum. Genet. 48:107-109(2003).
RN [14]
RP VARIANT RTS2 757-GLN--ARG-1208 DEL, AND VARIANTS GLY-71; LEU-103; CYS-522;
RP MET-799; GLN-1021 AND LEU-1170.
RX PubMed=12734318; DOI=10.1093/jnci/95.9.669;
RA Wang L.L., Gannavarapu A., Kozinetz C.A., Levy M.L., Lewis R.A.,
RA Chintagumpala M.M., Ruiz-Maldanado R., Contreras-Ruiz J., Cunniff C.,
RA Erickson R.P., Lev D., Rogers M., Zackai E.H., Plon S.E.;
RT "Association between osteosarcoma and deleterious mutations in the RECQL4
RT gene in Rothmund-Thomson syndrome.";
RL J. Natl. Cancer Inst. 95:669-674(2003).
RN [15]
RP VARIANTS GLN-355; SER-441 AND 857-CYS--THR-858 DEL.
RX PubMed=15221963; DOI=10.1002/ijc.20269;
RA Nishijo K., Nakayama T., Aoyama T., Okamoto T., Ishibe T., Yasura K.,
RA Shima Y., Shibata K.R., Tsuboyama T., Nakamura T., Toguchida J.;
RT "Mutation analysis of the RECQL4 gene in sporadic osteosarcomas.";
RL Int. J. Cancer 111:367-372(2004).
RN [16]
RP VARIANT BGS TRP-1021, AND VARIANT THR-523.
RX PubMed=15964893; DOI=10.1136/jmg.2005.031781;
RA Van Maldergem L., Siitonen H.A., Jalkh N., Chouery E., De Roy M.,
RA Delague V., Muenke M., Jabs E.W., Cai J., Wang L.L., Plon S.E.,
RA Fourneau C., Kestilae M., Gillerot Y., Megarbane A., Verloes A.;
RT "Revisiting the craniosynostosis-radial ray hypoplasia association: Baller-
RT Gerold syndrome caused by mutations in the RECQL4 gene.";
RL J. Med. Genet. 43:148-152(2006).
RN [17]
RP VARIANT RTS2 640-LEU--ALA-642 DELINS PRO.
RX PubMed=20503338; DOI=10.1002/ajmg.a.33427;
RA Simon T., Kohlhase J., Wilhelm C., Kochanek M., De Carolis B., Berthold F.;
RT "Multiple malignant diseases in a patient with Rothmund-Thomson syndrome
RT with RECQL4 mutations: Case report and literature review.";
RL Am. J. Med. Genet. A 152A:1575-1579(2010).
CC -!- FUNCTION: DNA-dependent ATPase. May modulate chromosome segregation.
CC {ECO:0000269|PubMed:15317757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with UBR1 and UBR2. Interacts with MCM10; this
CC interaction regulates RECQL4 unwinding activity.
CC {ECO:0000269|PubMed:15317757, ECO:0000269|PubMed:19696745}.
CC -!- INTERACTION:
CC O94761; P54274: TERF1; NbExp=2; IntAct=EBI-722861, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15317757}. Nucleus
CC {ECO:0000269|PubMed:10552928}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC thymus and testis. {ECO:0000269|PubMed:9878247}.
CC -!- INDUCTION: Up-regulated in actively dividing cells.
CC {ECO:0000269|PubMed:11032027}.
CC -!- DISEASE: RAPADILINO syndrome (RAPADILINOS) [MIM:266280]: Disease
CC characterized by radial and patellar aplasia or hypoplasia.
CC {ECO:0000269|PubMed:12952869}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Baller-Gerold syndrome (BGS) [MIM:218600]: An autosomal
CC recessive syndrome characterized by short stature, craniosynostosis,
CC absent or hypoplastic radii, short and curved ulna, fused carpal bones
CC and absent carpals, metacarpals and phalanges. Some patients manifest
CC poikiloderma. Cases reported as Baller-Gerold syndrome have phenotypic
CC overlap with several other disorders, including Saethre-Chotzen
CC syndrome. {ECO:0000269|PubMed:15964893}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Rothmund-Thomson syndrome 2 (RTS2) [MIM:268400]: An autosomal
CC recessive disorder characterized by dermatological features such as
CC skin atrophy, pigmentation abnormalities, and telangiectasia. It is
CC frequently accompanied by juvenile cataract, saddle nose, congenital
CC bone defects, disturbances of hair growth, hypogonadism, and an
CC increased risk of osteosarcoma in childhood and skin cancer later in
CC life. {ECO:0000269|PubMed:10319867, ECO:0000269|PubMed:10678659,
CC ECO:0000269|PubMed:12734318, ECO:0000269|PubMed:20503338}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13277.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RECQL4ID285.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/recql4/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006532; BAA74453.1; -; mRNA.
DR EMBL; AB026546; BAA86899.1; -; Genomic_DNA.
DR EMBL; DQ176868; AAZ85145.1; -; Genomic_DNA.
DR EMBL; AC084125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF495717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011602; AAH11602.2; -; mRNA.
DR EMBL; BC013277; AAH13277.2; ALT_INIT; mRNA.
DR CCDS; CCDS75804.1; -.
DR RefSeq; NP_004251.3; NM_004260.3.
DR PDB; 2KMU; NMR; -; A=1-54.
DR PDB; 5LST; X-ray; 2.75 A; A=427-1116.
DR PDBsum; 2KMU; -.
DR PDBsum; 5LST; -.
DR AlphaFoldDB; O94761; -.
DR BMRB; O94761; -.
DR SMR; O94761; -.
DR BioGRID; 114798; 1441.
DR DIP; DIP-48475N; -.
DR IntAct; O94761; 30.
DR STRING; 9606.ENSP00000482313; -.
DR iPTMnet; O94761; -.
DR PhosphoSitePlus; O94761; -.
DR BioMuta; RECQL4; -.
DR EPD; O94761; -.
DR jPOST; O94761; -.
DR MassIVE; O94761; -.
DR PeptideAtlas; O94761; -.
DR PRIDE; O94761; -.
DR ProteomicsDB; 50424; -.
DR Antibodypedia; 4498; 135 antibodies from 20 providers.
DR DNASU; 9401; -.
DR Ensembl; ENST00000617875.6; ENSP00000482313.2; ENSG00000160957.15.
DR GeneID; 9401; -.
DR KEGG; hsa:9401; -.
DR MANE-Select; ENST00000617875.6; ENSP00000482313.2; NM_004260.4; NP_004251.4.
DR CTD; 9401; -.
DR DisGeNET; 9401; -.
DR GeneCards; RECQL4; -.
DR GeneReviews; RECQL4; -.
DR HGNC; HGNC:9949; RECQL4.
DR HPA; ENSG00000160957; Tissue enhanced (bone marrow, testis).
DR MalaCards; RECQL4; -.
DR MIM; 218600; phenotype.
DR MIM; 266280; phenotype.
DR MIM; 268400; phenotype.
DR MIM; 603780; gene.
DR neXtProt; NX_O94761; -.
DR OpenTargets; ENSG00000160957; -.
DR Orphanet; 1225; Baller-Gerold syndrome.
DR Orphanet; 3021; RAPADILINO syndrome.
DR Orphanet; 221016; Rothmund-Thomson syndrome type 2.
DR PharmGKB; PA34316; -.
DR VEuPathDB; HostDB:ENSG00000160957; -.
DR eggNOG; KOG0351; Eukaryota.
DR GeneTree; ENSGT00940000160387; -.
DR InParanoid; O94761; -.
DR OMA; WQKKGEC; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; O94761; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; O94761; -.
DR SignaLink; O94761; -.
DR SIGNOR; O94761; -.
DR BioGRID-ORCS; 9401; 32 hits in 258 CRISPR screens.
DR ChiTaRS; RECQL4; human.
DR EvolutionaryTrace; O94761; -.
DR GeneWiki; RECQL4; -.
DR GenomeRNAi; 9401; -.
DR Pharos; O94761; Tbio.
DR PRO; PR:O94761; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O94761; protein.
DR Bgee; ENSG00000160957; Expressed in lower esophagus mucosa and 138 other tissues.
DR ExpressionAtlas; O94761; baseline and differential.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; TAS:BHF-UCL.
DR GO; GO:0032357; F:oxidized purine DNA binding; IDA:BHF-UCL.
DR GO; GO:0061821; F:telomeric D-loop binding; IDA:BHF-UCL.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IMP:BHF-UCL.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0061820; P:telomeric D-loop disassembly; IDA:BHF-UCL.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR021110; DNA_rep_checkpnt_protein.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF11719; Drc1-Sld2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cataract; Craniosynostosis; Cytoplasm;
KW Disease variant; Dwarfism; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1208
FT /note="ATP-dependent DNA helicase Q4"
FT /id="PRO_0000205053"
FT DOMAIN 489..662
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 683..850
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 17..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 605..608
FT /note="DEAH box"
FT COMPBIAS 17..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 54
FT /note="Q -> R (in dbSNP:rs35198096)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025117"
FT VARIANT 71
FT /note="E -> G (in dbSNP:rs34642881)"
FT /evidence="ECO:0000269|PubMed:12734318, ECO:0000269|Ref.3"
FT /id="VAR_025118"
FT VARIANT 92
FT /note="S -> P (in dbSNP:rs2721190)"
FT /evidence="ECO:0000269|PubMed:10552928,
FT ECO:0000269|PubMed:9878247, ECO:0000269|Ref.3"
FT /id="VAR_025119"
FT VARIANT 103
FT /note="P -> L (in dbSNP:rs199543866)"
FT /evidence="ECO:0000269|PubMed:12734318"
FT /id="VAR_083742"
FT VARIANT 189
FT /note="G -> S (in dbSNP:rs34371341)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025120"
FT VARIANT 267
FT /note="E -> D (in dbSNP:rs4244612)"
FT /evidence="ECO:0000269|PubMed:12601557, ECO:0000269|Ref.3"
FT /id="VAR_023295"
FT VARIANT 273
FT /note="A -> T (in dbSNP:rs34103564)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025121"
FT VARIANT 301
FT /note="E -> K (in dbSNP:rs34633809)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025122"
FT VARIANT 355
FT /note="R -> Q (in dbSNP:rs374743591)"
FT /evidence="ECO:0000269|PubMed:15221963"
FT /id="VAR_023296"
FT VARIANT 441
FT /note="P -> S (in dbSNP:rs557142414)"
FT /evidence="ECO:0000269|PubMed:15221963"
FT /id="VAR_023297"
FT VARIANT 522
FT /note="R -> C (in dbSNP:rs35407712)"
FT /evidence="ECO:0000269|PubMed:12734318, ECO:0000269|Ref.3"
FT /id="VAR_025123"
FT VARIANT 522
FT /note="R -> H (in dbSNP:rs35842750)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025124"
FT VARIANT 523
FT /note="S -> T (in dbSNP:rs754735053)"
FT /evidence="ECO:0000269|PubMed:15964893"
FT /id="VAR_026590"
FT VARIANT 591
FT /note="P -> L (in dbSNP:rs2721191)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025125"
FT VARIANT 640..642
FT /note="LTA -> P (in RTS2; dbSNP:rs786200890)"
FT /evidence="ECO:0000269|PubMed:20503338"
FT /id="VAR_083743"
FT VARIANT 757..1208
FT /note="Missing (in RTS2; dbSNP:rs137853229)"
FT /evidence="ECO:0000269|PubMed:10319867,
FT ECO:0000269|PubMed:12734318"
FT /id="VAR_083744"
FT VARIANT 793
FT /note="P -> L (in dbSNP:rs1034558903)"
FT /id="VAR_057125"
FT VARIANT 793
FT /note="P -> S (in dbSNP:rs35098923)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025126"
FT VARIANT 799
FT /note="V -> M (in dbSNP:rs34293591)"
FT /evidence="ECO:0000269|PubMed:12734318, ECO:0000269|Ref.3"
FT /id="VAR_025127"
FT VARIANT 857..858
FT /note="Missing"
FT /id="VAR_023298"
FT VARIANT 964
FT /note="P -> T (in dbSNP:rs33972310)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025128"
FT VARIANT 976
FT /note="E -> K (in dbSNP:rs35070885)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025129"
FT VARIANT 1004
FT /note="R -> W (in dbSNP:rs36023964)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025130"
FT VARIANT 1005
FT /note="R -> Q (in dbSNP:rs4251691)"
FT /evidence="ECO:0000269|PubMed:12601557, ECO:0000269|Ref.3"
FT /id="VAR_023299"
FT VARIANT 1021
FT /note="R -> Q (in dbSNP:rs34666647)"
FT /evidence="ECO:0000269|PubMed:12734318, ECO:0000269|Ref.3"
FT /id="VAR_025131"
FT VARIANT 1021
FT /note="R -> W (in BGS; dbSNP:rs137853232)"
FT /evidence="ECO:0000269|PubMed:15964893"
FT /id="VAR_026591"
FT VARIANT 1043
FT /note="L -> P (in dbSNP:rs4925828)"
FT /id="VAR_057126"
FT VARIANT 1045
FT /note="A -> T (in dbSNP:rs35348691)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025132"
FT VARIANT 1105
FT /note="G -> D (in dbSNP:rs36078464)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025133"
FT VARIANT 1105
FT /note="G -> S (in dbSNP:rs34915097)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025134"
FT VARIANT 1106
FT /note="R -> H (in dbSNP:rs34236392)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025135"
FT VARIANT 1113
FT /note="G -> R (in dbSNP:rs35101495)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025136"
FT VARIANT 1148
FT /note="S -> F (in dbSNP:rs35346077)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025137"
FT VARIANT 1170
FT /note="P -> L (in dbSNP:rs772265082)"
FT /evidence="ECO:0000269|PubMed:12734318"
FT /id="VAR_083745"
FT HELIX 1..21
FT /evidence="ECO:0007829|PDB:2KMU"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2KMU"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:2KMU"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 485..492
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 510..522
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 559..570
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 620..630
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 684..693
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 695..699
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 710..723
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 739..744
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 750..761
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 765..771
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 772..774
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 795..802
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 807..810
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 812..817
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 823..835
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 839..849
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 900..905
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 906..913
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 917..929
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 931..933
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 936..948
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 952..957
FT /evidence="ECO:0007829|PDB:5LST"
FT TURN 958..962
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 964..972
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 985..988
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 989..996
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 1000..1008
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 1009..1011
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 1016..1018
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 1027..1039
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 1045..1078
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 1082..1085
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:5LST"
FT STRAND 1089..1091
FT /evidence="ECO:0007829|PDB:5LST"
FT HELIX 1094..1108
FT /evidence="ECO:0007829|PDB:5LST"
SQ SEQUENCE 1208 AA; 133067 MW; 7634BC134AD7FB4D CRC64;
MERLRDVRER LQAWERAFRR QRGRRPSQDD VEAAPEETRA LYREYRTLKR TTGQAGGGLR
SSESLPAAAE EAPEPRCWGP HLNRAATKSP QSTPGRSRQG SVPDYGQRLK ANLKGTLQAG
PALGRRPWPL GRASSKASTP KPPGTGPVPS FAEKVSDEPP QLPEPQPRPG RLQHLQASLS
QRLGSLDPGW LQRCHSEVPD FLGAPKACRP DLGSEESQLL IPGESAVLGP GAGSQGPEAS
AFQEVSIRVG SPQPSSSGGE KRRWNEEPWE SPAQVQQESS QAGPPSEGAG AVAVEEDPPG
EPVQAQPPQP CSSPSNPRYH GLSPSSQARA GKAEGTAPLH IFPRLARHDR GNYVRLNMKQ
KHYVRGRALR SRLLRKQAWK QKWRKKGECF GGGGATVTTK ESCFLNEQFD HWAAQCPRPA
SEEDTDAVGP EPLVPSPQPV PEVPSLDPTV LPLYSLGPSG QLAETPAEVF QALEQLGHQA
FRPGQERAVM RILSGISTLL VLPTGAGKSL CYQLPALLYS RRSPCLTLVV SPLLSLMDDQ
VSGLPPCLKA ACIHSGMTRK QRESVLQKIR AAQVHVLMLT PEALVGAGGL PPAAQLPPVA
FACIDEAHCL SQWSHNFRPC YLRVCKVLRE RMGVHCFLGL TATATRRTAS DVAQHLAVAE
EPDLHGPAPV PTNLHLSVSM DRDTDQALLT LLQGKRFQNL DSIIIYCNRR EDTERIAALL
RTCLHAAWVP GSGGRAPKTT AEAYHAGMCS RERRRVQRAF MQGQLRVVVA TVAFGMGLDR
PDVRAVLHLG LPPSFESYVQ AVGRAGRDGQ PAHCHLFLQP QGEDLRELRR HVHADSTDFL
AVKRLVQRVF PACTCTCTRP PSEQEGAVGG ERPVPKYPPQ EAEQLSHQAA PGPRRVCMGH
ERALPIQLTV QALDMPEEAI ETLLCYLELH PHHWLELLAT TYTHCRLNCP GGPAQLQALA
HRCPPLAVCL AQQLPEDPGQ GSSSVEFDMV KLVDSMGWEL ASVRRALCQL QWDHEPRTGV
RRGTGVLVEF SELAFHLRSP GDLTAEEKDQ ICDFLYGRVQ ARERQALARL RRTFQAFHSV
AFPSCGPCLE QQDEERSTRL KDLLGRYFEE EEGQEPGGME DAQGPEPGQA RLQDWEDQVR
CDIRQFLSLR PEEKFSSRAV ARIFHGIGSP CYPAQVYGQD RRFWRKYLHL SFHALVGLAT
EELLQVAR
