IBTK_HUMAN
ID IBTK_HUMAN Reviewed; 1353 AA.
AC Q9P2D0; Q2QKU2; Q2QKU3; Q2QKU4; Q5TFD7; Q5TFD9; Q8IUQ9; Q8IUY7; Q8TAI4;
AC Q9HBI8; Q9Y3T8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inhibitor of Bruton tyrosine kinase;
DE Short=IBtk;
GN Name=IBTK; Synonyms=BTKI, KIAA1417;
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; 2 AND 3), ALTERNATIVE SPLICING,
RP INTERACTION WITH BTK, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18596081; DOI=10.1093/nar/gkn413;
RA Spatuzza C., Schiavone M., Di Salle E., Janda E., Sardiello M., Fiume G.,
RA Fierro O., Simonetta M., Argiriou N., Faraonio R., Capparelli R.,
RA Quinto I., Scala G.;
RT "Physical and functional characterization of the genetic locus of IBtk, an
RT inhibitor of Bruton's tyrosine kinase: evidence for three protein isoforms
RT of IBtk.";
RL Nucleic Acids Res. 36:4402-4416(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-1185.
RC TISSUE=Brain, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 971-1353 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1159-1353 (ISOFORMS 1/3), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BTK, AND VARIANT
RP VAL-1185.
RC TISSUE=B-cell;
RX PubMed=11577348; DOI=10.1038/ni1001-939;
RA Liu W., Quinto I., Chen X., Palmieri C., Rabin R.L., Schwartz O.M.,
RA Nelson D.L., Scala G.;
RT "Direct inhibition of Bruton's tyrosine kinase by IBtk, a Btk-binding
RT protein.";
RL Nat. Immunol. 2:939-946(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990; SER-1004; SER-1045 AND
RP SER-1054, AND 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045; SER-1113 AND SER-1116,
RP AND IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045 AND SER-1083, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030; SER-1033; SER-1039 AND
RP SER-1045, AND 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: Acts as an inhibitor of BTK tyrosine kinase activity, thereby
CC playing a role in B-cell development. Down-regulates BTK kinase
CC activity, leading to interference with BTK-mediated calcium
CC mobilization and NF-kappa-B-driven transcription.
CC {ECO:0000269|PubMed:11577348}.
CC -!- SUBUNIT: Interacts with the PH domain of BTK. Isoform 2 does not
CC interact with BTK. {ECO:0000269|PubMed:11577348,
CC ECO:0000269|PubMed:18596081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Note=Translocates to the plasma membrane upon IgM stimulation.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=IBtk-alpha;
CC IsoId=Q9P2D0-1; Sequence=Displayed;
CC Name=2; Synonyms=IBtk-beta;
CC IsoId=Q9P2D0-2; Sequence=VSP_023602, VSP_023604;
CC Name=3; Synonyms=IBtk-gamma;
CC IsoId=Q9P2D0-3; Sequence=VSP_023600, VSP_023601;
CC -!- TISSUE SPECIFICITY: Expressed in DeFew, HEK293T, HeLa and in Jurkat,
CC MC3 and NB4 lymphoid cells (at protein level). Isoform 1 is the
CC predominant isoform expressed in all examined tissues and cell lines.
CC Highly expressed in hemopoietic tissues (fetal liver, spleen, lymph
CC node, thymus, peripheral blood leukocytes and bone marrow). Weakly or
CC not expressed in other tissues. {ECO:0000269|PubMed:11577348,
CC ECO:0000269|PubMed:18596081}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG27170.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAA92655.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ005633; AAY55906.1; -; mRNA.
DR EMBL; DQ005634; AAY55907.1; -; mRNA.
DR EMBL; DQ005635; AAY55908.1; -; mRNA.
DR EMBL; AB037838; BAA92655.2; ALT_INIT; mRNA.
DR EMBL; AL050333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027490; AAH27490.1; -; mRNA.
DR EMBL; BC038244; AAH38244.2; -; mRNA.
DR EMBL; BC042171; AAH42171.2; -; mRNA.
DR EMBL; BC113696; AAI13697.1; -; mRNA.
DR EMBL; BC113698; AAI13699.1; -; mRNA.
DR EMBL; AL050018; CAB43239.1; -; mRNA.
DR EMBL; AF235049; AAG27170.1; ALT_SEQ; mRNA.
DR CCDS; CCDS34490.1; -. [Q9P2D0-1]
DR PIR; T08705; T08705.
DR RefSeq; NP_001287835.1; NM_001300906.1.
DR RefSeq; NP_056340.2; NM_015525.3. [Q9P2D0-1]
DR AlphaFoldDB; Q9P2D0; -.
DR SMR; Q9P2D0; -.
DR BioGRID; 117474; 123.
DR IntAct; Q9P2D0; 48.
DR STRING; 9606.ENSP00000305721; -.
DR GlyGen; Q9P2D0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2D0; -.
DR PhosphoSitePlus; Q9P2D0; -.
DR BioMuta; IBTK; -.
DR DMDM; 134034141; -.
DR EPD; Q9P2D0; -.
DR jPOST; Q9P2D0; -.
DR MassIVE; Q9P2D0; -.
DR MaxQB; Q9P2D0; -.
DR PaxDb; Q9P2D0; -.
DR PeptideAtlas; Q9P2D0; -.
DR PRIDE; Q9P2D0; -.
DR ProteomicsDB; 83770; -. [Q9P2D0-1]
DR ProteomicsDB; 83771; -. [Q9P2D0-2]
DR ProteomicsDB; 83772; -. [Q9P2D0-3]
DR Antibodypedia; 18465; 133 antibodies from 24 providers.
DR DNASU; 25998; -.
DR Ensembl; ENST00000306270.12; ENSP00000305721.7; ENSG00000005700.15. [Q9P2D0-1]
DR Ensembl; ENST00000635454.2; ENSP00000489389.1; ENSG00000283068.2. [Q9P2D0-1]
DR GeneID; 25998; -.
DR KEGG; hsa:25998; -.
DR MANE-Select; ENST00000306270.12; ENSP00000305721.7; NM_015525.4; NP_056340.2.
DR UCSC; uc003pjl.2; human. [Q9P2D0-1]
DR CTD; 25998; -.
DR DisGeNET; 25998; -.
DR GeneCards; IBTK; -.
DR HGNC; HGNC:17853; IBTK.
DR HPA; ENSG00000005700; Low tissue specificity.
DR MIM; 606457; gene.
DR neXtProt; NX_Q9P2D0; -.
DR OpenTargets; ENSG00000005700; -.
DR PharmGKB; PA134898277; -.
DR VEuPathDB; HostDB:ENSG00000005700; -.
DR eggNOG; KOG0783; Eukaryota.
DR GeneTree; ENSGT00940000156277; -.
DR InParanoid; Q9P2D0; -.
DR OMA; FACGINT; -.
DR OrthoDB; 94875at2759; -.
DR PhylomeDB; Q9P2D0; -.
DR TreeFam; TF323747; -.
DR PathwayCommons; Q9P2D0; -.
DR SignaLink; Q9P2D0; -.
DR SIGNOR; Q9P2D0; -.
DR BioGRID-ORCS; 25998; 10 hits in 1123 CRISPR screens.
DR ChiTaRS; IBTK; human.
DR GenomeRNAi; 25998; -.
DR Pharos; Q9P2D0; Tbio.
DR PRO; PR:Q9P2D0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P2D0; protein.
DR Bgee; ENSG00000005700; Expressed in adrenal tissue and 103 other tissues.
DR ExpressionAtlas; Q9P2D0; baseline and differential.
DR Genevisible; Q9P2D0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; IDA:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.130.10.30; -; 1.
DR Gene3D; 3.30.710.10; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00651; BTB; 2.
DR Pfam; PF00415; RCC1; 3.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50097; BTB; 2.
DR PROSITE; PS50012; RCC1_3; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1353
FT /note="Inhibitor of Bruton tyrosine kinase"
FT /id="PRO_0000280276"
FT REPEAT 51..80
FT /note="ANK 1"
FT REPEAT 85..114
FT /note="ANK 2"
FT REPEAT 141..194
FT /note="RCC1 1"
FT REPEAT 195..246
FT /note="RCC1 2"
FT REPEAT 248..301
FT /note="RCC1 3"
FT DOMAIN 564..644
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 768..836
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 806..835
FT /note="ANK 3"
FT REGION 970..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPR6"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..1113
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18596081"
FT /id="VSP_023600"
FT VAR_SEQ 1114..1144
FT /note="PVSPPVVDLRTIMEIEESRQKCGATPKSHLG -> MLIDIISSKMISHGIKL
FT CQKKPLKLIGLISS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18596081"
FT /id="VSP_023601"
FT VAR_SEQ 1145..1196
FT /note="KTVSHGVKLSQKQRKMIALTTKENNSGMNSMETVLFTPSKAPKPVNAWASSL
FT -> WVENITKDHFMLYFCPKNWTDLLHLSYYFSAFDVIVNYTSFSGQFSLHNIIS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:18596081"
FT /id="VSP_023602"
FT VAR_SEQ 1197..1353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18596081"
FT /id="VSP_023604"
FT VARIANT 1065
FT /note="V -> I (in dbSNP:rs12662902)"
FT /id="VAR_031106"
FT VARIANT 1185
FT /note="A -> V (in dbSNP:rs9449444)"
FT /evidence="ECO:0000269|PubMed:11577348,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031107"
FT CONFLICT 971
FT /note="S -> G (in Ref. 6; CAB43239)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="H -> R (in Ref. 6; CAB43239)"
FT /evidence="ECO:0000305"
FT CONFLICT 1218
FT /note="H -> L (in Ref. 6; CAB43239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1353 AA; 150528 MW; 67B2D11E276A6AF1 CRC64;
MSSPMPDCTS KCRSLKHALD VLSVVTKGSE NQIKAFLSSH CYNAATIKDV FGRNALHLVS
SCGKKGVLDW LIQKGVDLLV KDKESGWTAL HRSIFYGHID CVWSLLKHGV SLYIQDKEGL
SALDLVMKDR PTHVVFKNTD PTDVYTWGDN TNFTLGHGSQ NSKHHPELVD LFSRSGIYIK
QVVLCKFHSV FLSQKGQVYT CGHGPGGRLG HGDEQTCLVP RLVEGLNGHN CSQVAAAKDH
TVVLTEDGCV YTFGLNIFHQ LGIIPPPSSC NVPRQIQAKY LKGRTIIGVA AGRFHTVLWT
REAVYTMGLN GGQLGCLLDP NGEKCVTAPR QVSALHHKDI ALSLVAASDG ATVCVTTRGD
IYLLADYQCK KMASKQLNLK KVLVSGGHME YKVDPEHLKE NGGQKICILA MDGAGRVFCW
RSVNSSLKQC RWAYPRQVFI SDIALNRNEI LFVTQDGEGF RGRWFEEKRK SSEKKEILSN
LHNSSSDVSY VSDINSVYER IRLEKLTFAH RAVSVSTDPS GCNFAILQSD PKTSLYEIPA
VSSSSFFEEF GKLLREADEM DSIHDVTFQV GNRLFPAHKY ILAVHSDFFQ KLFLSDGNTS
EFTDIYQKDE DSAGCHLFVV EKVHPDMFEY LLQFIYTDTC DFLTHGFKPR IHLNKNPEEY
QGTLNSHLNK VNFHEDDNQK SAFEVYKSNQ AQTVSERQKS KPKSCKKGKN IREDDPVRML
QTVAKKFDFS NLSSRLDGVR FENEKINVIA KNTGNKLKLS QKKCSFLCDV TMKSVDGKEF
PCHKCVLCAR LEYFHSMLSS SWIEASSCAA LEMPIHSDIL KVILDYLYTD EAVVIKESQN
VDFICSVLVV ADQLLITRLK EICEVALTEK LTLKNAAMLL EFAAMYSAKQ LKLSCLQFIG
LNMAALLEAR SLDVLSDGVL KDLSEFYRKM IPAMDRRVIT PYQDGPDISY LEVEDGDIFL
KEEINMEQNH SETMFKKAKT KAKKKPRKRS DSSGGYNLSD IIQSPSSTGL LKSGKTNSVE
SLPELLTSDS EGSYAGVGSP RDLQSPDFTT GFHSDKIEAK VKPYVNGTSP VYSREDLKPW
EKSPILKISA PQPIPSNRID TTSSASWVAG SFSPVSPPVV DLRTIMEIEE SRQKCGATPK
SHLGKTVSHG VKLSQKQRKM IALTTKENNS GMNSMETVLF TPSKAPKPVN AWASSLHSVS
SKSFRDFLLE EKKSVTSHSS GDHVKKVSFK GIENSQAPKI VRCSTHGTPG PEGNHISDLP
LLDSPNPWLS SSVTAPSMVA PVTFASIVEE ELQQEAALIR SREKPLALIQ IEEHAIQDLL
VFYEAFGNPE EFVIVERTPQ GPLAVPMWNK HGC
