IWS1_MOUSE
ID IWS1_MOUSE Reviewed; 766 AA.
AC Q8C1D8; Q3TQ25; Q3UWB0; Q6NVD1; Q8BY73; Q9D9H4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein IWS1 homolog;
DE AltName: Full=IWS1-like protein;
GN Name=Iws1; Synonyms=Iws1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, Head, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17184735; DOI=10.1016/j.bbrc.2006.11.133;
RA Liu Z., Zhou Z., Chen G., Bao S.;
RT "A putative transcriptional elongation factor hIws1 is essential for
RT mammalian cell proliferation.";
RL Biochem. Biophys. Res. Commun. 353:47-53(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-235; SER-343;
RP SER-345; SER-366; SER-368 AND SER-372, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-384 AND SER-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-209; SER-211;
RP SER-222; SER-235; SER-237; SER-261; SER-263; SER-306; SER-307; SER-309;
RP SER-321; SER-343; SER-345; SER-366; SER-368; SER-372; SER-384 AND SER-386,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor which plays a key role in defining the
CC composition of the RNA polymerase II (RNAPII) elongation complex and in
CC modulating the production of mature mRNA transcripts. Acts as an
CC assembly factor to recruit various factors to the RNAPII elongation
CC complex and is recruited to the complex via binding to the
CC transcription elongation factor SUPT6H bound to the C-terminal domain
CC (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex
CC recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone
CC modifying enzymes (such as SETD2) to ensure proper mRNA splicing,
CC efficient mRNA export and elongation-coupled H3K36 methylation, a
CC signature chromatin mark of active transcription (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SUPT6H; binds preferentially to the POLR2A-
CC bound SUPT6H. Interacts with ALYREF/THOC4, SETD2 and PRMT5 (By
CC similarity). Interacts with HDGFRP2 (By similarity). Interacts (via IBM
CC motif) with PSIP1 (via IBD domain); phosphorylation increases its
CC affinity for PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q96ST2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C1D8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C1D8-2; Sequence=VSP_016994, VSP_016995;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at highest level in kidney,
CC then testicle, large intestine, small intestine, spleen and prostate,
CC whereas the lowest level is detected in heart.
CC {ECO:0000269|PubMed:17184735}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q96ST2}.
CC -!- SIMILARITY: Belongs to the IWS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24793.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE23006.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK006925; BAB24793.1; ALT_INIT; mRNA.
DR EMBL; AK028247; BAC25838.1; -; mRNA.
DR EMBL; AK041691; BAC31034.1; -; mRNA.
DR EMBL; AK136492; BAE23006.1; ALT_INIT; mRNA.
DR EMBL; AK163972; BAE37560.1; -; mRNA.
DR EMBL; BC068184; AAH68184.1; -; mRNA.
DR CCDS; CCDS29115.1; -. [Q8C1D8-1]
DR RefSeq; NP_775617.1; NM_173441.3. [Q8C1D8-1]
DR AlphaFoldDB; Q8C1D8; -.
DR SMR; Q8C1D8; -.
DR BioGRID; 216045; 3.
DR IntAct; Q8C1D8; 3.
DR MINT; Q8C1D8; -.
DR STRING; 10090.ENSMUSP00000025243; -.
DR iPTMnet; Q8C1D8; -.
DR PhosphoSitePlus; Q8C1D8; -.
DR EPD; Q8C1D8; -.
DR jPOST; Q8C1D8; -.
DR MaxQB; Q8C1D8; -.
DR PaxDb; Q8C1D8; -.
DR PeptideAtlas; Q8C1D8; -.
DR PRIDE; Q8C1D8; -.
DR ProteomicsDB; 269021; -. [Q8C1D8-1]
DR ProteomicsDB; 269022; -. [Q8C1D8-2]
DR Antibodypedia; 47563; 116 antibodies from 22 providers.
DR DNASU; 73473; -.
DR Ensembl; ENSMUST00000025243; ENSMUSP00000025243; ENSMUSG00000024384. [Q8C1D8-1]
DR GeneID; 73473; -.
DR KEGG; mmu:73473; -.
DR UCSC; uc008eiy.2; mouse. [Q8C1D8-1]
DR CTD; 55677; -.
DR MGI; MGI:1920723; Iws1.
DR VEuPathDB; HostDB:ENSMUSG00000024384; -.
DR eggNOG; KOG1793; Eukaryota.
DR GeneTree; ENSGT00720000108834; -.
DR HOGENOM; CLU_018182_0_0_1; -.
DR InParanoid; Q8C1D8; -.
DR OMA; HTHKDET; -.
DR OrthoDB; 380765at2759; -.
DR PhylomeDB; Q8C1D8; -.
DR TreeFam; TF315504; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 73473; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Iws1; mouse.
DR PRO; PR:Q8C1D8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8C1D8; protein.
DR Bgee; ENSMUSG00000024384; Expressed in embryonic post-anal tail and 226 other tissues.
DR ExpressionAtlas; Q8C1D8; baseline and differential.
DR Genevisible; Q8C1D8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:2001253; P:regulation of histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:0090239; P:regulation of histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR Pfam; PF08711; Med26; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..766
FT /note="Protein IWS1 homolog"
FT /id="PRO_0000083347"
FT DOMAIN 561..639
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 1..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..766
FT /note="Interaction with SUPT6H and ALYREF"
FT /evidence="ECO:0000250"
FT REGION 643..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 416..442
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT COMPBIAS 16..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3SWT4"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3SWT4"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3SWT4"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT MOD_RES 672
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST2"
FT VAR_SEQ 520..543
FT /note="EDRQLNNQKKPALKKLTLLPTVVM -> VSSSRLPFSPPALNQIDGVANLSL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016994"
FT VAR_SEQ 544..766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016995"
FT CONFLICT 260..261
FT /note="AS -> VI (in Ref. 1; BAC31034)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="S -> F (in Ref. 1; BAC31034)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="L -> T (in Ref. 1; BAB24793)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="L -> M (in Ref. 1; BAB24793)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="R -> S (in Ref. 1; BAE23006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 85248 MW; 5787745679C3A3A7 CRC64;
MDSEYYSGDQ SDDGGATPVQ DERDSGSDGE DGVTEQHSGS DTGSVDHHSE NETSDREDGL
AKIHNGTDSE NDEPSNANAS DSESEELHRP KDSDSDSEEH AESPASDSEN EPVNQHGSDS
ENEELLNGHA SDSEKEEVSK HAASDSEAED TLQPQVSESD SEDPPRPQAS DSENEEPPKP
RISDSESEEL PKPRVSDSES EDPPRPQASD SESEELPKPR VSDSESEDPP RPQASDSESE
ELPKPRVSDS ESEDPQKGPA SDSEAEDASR HKEKPDSDDS DGENKREDSE VQNESDGHTD
RKGLHSSDSE EEEPKRQKID SDDDEEKEGD EEKVAKRKAA VLSDSEDDAG NASAKKSRVV
CDADDSDSDV VSDKSGKRET TVASDSEEEA GKEESSVKKK EDKDLFGSDS ESGNEEENLI
ADIFGESGDE EEEEFTGFNQ EDLEEEKNET QLKEAEDSDS DDNIKRGKHM DFLSDFEMML
QRKKSMCGKR RRNRDGGTFI SDADDVVSAM IVKMNEAAEE DRQLNNQKKP ALKKLTLLPT
VVMHLKKQDL KETFIDSGVM SAIKEWLSPL PDRSLPALKI REELLKILQE LPSVSQETLK
HSGIGRAVMY LYKHPKESRS NKDMAGKLIN EWSRPIFGLT SNYKGMTREE REQRDLEQMP
QRRRLSSTGG QTPRRDLEKV LTGEEKALRP GDPGFCARAR VPMPSNKDYV VRPKWNVEME
SSRFQASSKK GISRLDKQMR KFTDIRKKSR SAHAVKISIE GNKMPL
