TAF1B_HUMAN
ID TAF1B_HUMAN Reviewed; 588 AA.
AC Q53T94; B4DI42; F8WD72; Q15574; Q8WVC3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE AltName: Full=RNA polymerase I-specific TBP-associated factor 63 kDa;
DE Short=TAFI63;
DE AltName: Full=TATA box-binding protein-associated factor 1B;
DE Short=TBP-associated factor 1B;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit B;
GN Name=TAF1B;
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], PROTEIN SEQUENCE OF 11-20; 42-56; 93-110;
RP 123-135; 264-276; 281-289; 311-321; 331-340; 396-407; 429-444; 448-466 AND
RP 471-480, FUNCTION, INTERACTION WITH TBP; TAF1A AND TAF1C, AND VARIANTS
RP SER-6; ILE-282; ALA-351 AND ASP-462.
RX PubMed=7801123; DOI=10.1126/science.7801123;
RA Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.;
RT "Reconstitution of transcription factor SL1: exclusive binding of TBP by
RT SL1 or TFIID subunits.";
RL Science 266:1966-1972(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ILE-282;
RP ALA-351 AND ASP-462.
RC TISSUE=Corpus callosum;
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], AND VARIANTS SER-6; ILE-282;
RP ALA-351 AND ASP-462.
RC TISSUE=Colon;
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 FUNCTION.
RX PubMed=7801130; DOI=10.1126/science.7801130;
RA Zomerdijk J.C., Beckmann H., Comai L., Tjian R.;
RT "Assembly of transcriptionally active RNA polymerase I initiation factor
RT SL1 from recombinant subunits.";
RL Science 266:2015-2018(1994).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=7491500; DOI=10.1126/science.270.5241.1506;
RA Beckmann H., Chen J.L., O'Brien T., Tjian R.;
RT "Coactivator and promoter-selective properties of RNA polymerase I TAFs.";
RL Science 270:1506-1509(1995).
RN [7]
RP IDENTIFICATION.
RX PubMed=10894955; DOI=10.1159/000015592;
RA Di Pietro C., Rapisarda A., Amico V., Bonaiuto C., Viola A., Scalia M.,
RA Motta S., Amato A., Engel H., Messina A., Sichel G., Grzeschik K.,
RA Purrello M.;
RT "Genomic localization of the human genes TAF1A, TAF1B and TAF1C, encoding
RT TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I general transcription
RT initiation factor SL1.";
RL Cytogenet. Cell Genet. 89:133-136(2000).
RN [8]
RP INTERACTION WITH RRN3.
RX PubMed=11250903; DOI=10.1093/emboj/20.6.1373;
RA Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I.,
RA Zomerdijk J.C.B.M.;
RT "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to
RT rRNA gene promoters.";
RL EMBO J. 20:1373-1382(2001).
RN [9]
RP FUNCTION OF THE SL1/TIF-IB COMPLEX.
RX PubMed=15970593; DOI=10.1074/jbc.m501595200;
RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.;
RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex
RT formation and stabilizes upstream binding factor at the rDNA promoter.";
RL J. Biol. Chem. 280:29551-29558(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, 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 [11]
RP FUNCTION.
RX PubMed=21921198; DOI=10.1126/science.1207699;
RA Knutson B.A., Hahn S.;
RT "Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general
RT transcription factors.";
RL Science 333:1637-1640(2011).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF CYS-13; CYS-31 AND CYS-34.
RX PubMed=21921199; DOI=10.1126/science.1207656;
RA Naidu S., Friedrich J.K., Russell J., Zomerdijk J.C.;
RT "TAF1B is a TFIIB-like component of the basal transcription machinery for
RT RNA polymerase I.";
RL Science 333:1640-1642(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of RNA polymerase I core factor complex that acts
CC as a GTF2B/TFIIB-like factor and plays a key role in multiple steps
CC during transcription initiation such as pre-initiation complex (PIC)
CC assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC transcription. Binds rDNA promoters and plays a role in Pol I
CC recruitment as a component of the SL1/TIF-IB complex and, possibly,
CC directly through its interaction with RRN3.
CC {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:21921198,
CC ECO:0000269|PubMed:21921199, ECO:0000269|PubMed:7491500,
CC ECO:0000269|PubMed:7801123, ECO:0000269|PubMed:7801130}.
CC -!- SUBUNIT: Interacts with FLNA (via N-terminus) (By similarity).
CC Component of the transcription factor SL1/TIF-IB complex, composed of
CC TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex
CC interacts directly with TBP, TAF1A and TAF1C. Interaction of the
CC SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3.
CC {ECO:0000250, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:7801123}.
CC -!- INTERACTION:
CC Q53T94; P49748: ACADVL; NbExp=3; IntAct=EBI-1560239, EBI-727618;
CC Q53T94; P27797: CALR; NbExp=3; IntAct=EBI-1560239, EBI-1049597;
CC Q53T94; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1560239, EBI-16439278;
CC Q53T94; Q01105: SET; NbExp=3; IntAct=EBI-1560239, EBI-1053182;
CC Q53T94; P20226: TBP; NbExp=4; IntAct=EBI-1560239, EBI-355371;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q53T94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53T94-2; Sequence=VSP_021677;
CC Name=3;
CC IsoId=Q53T94-3; Sequence=VSP_042954;
CC -!- DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB,
CC displays a similar subdomain organization as GTF2B/TFIIB, with a N-
CC terminal zinc finger, a connecting region (composed of B-reader and B-
CC linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger
CC plays an essential postrecruitment role in Pol I transcription at a
CC step preceding synthesis of the first 40 nucleotides (PubMed:21921198
CC and PubMed:21921199).
CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62863.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L39061; AAA62863.1; ALT_INIT; mRNA.
DR EMBL; AK295402; BAG58354.1; -; mRNA.
DR EMBL; AC010969; AAX93272.1; -; Genomic_DNA.
DR EMBL; BC018137; AAH18137.1; -; mRNA.
DR CCDS; CCDS33143.1; -. [Q53T94-1]
DR PIR; I61581; I61581.
DR RefSeq; NP_001305905.1; NM_001318976.1.
DR RefSeq; NP_005671.2; NM_005680.2. [Q53T94-1]
DR AlphaFoldDB; Q53T94; -.
DR BioGRID; 114483; 89.
DR CORUM; Q53T94; -.
DR IntAct; Q53T94; 23.
DR MINT; Q53T94; -.
DR STRING; 9606.ENSP00000263663; -.
DR iPTMnet; Q53T94; -.
DR PhosphoSitePlus; Q53T94; -.
DR BioMuta; TAF1B; -.
DR DMDM; 74726856; -.
DR EPD; Q53T94; -.
DR jPOST; Q53T94; -.
DR MassIVE; Q53T94; -.
DR MaxQB; Q53T94; -.
DR PaxDb; Q53T94; -.
DR PeptideAtlas; Q53T94; -.
DR PRIDE; Q53T94; -.
DR ProteomicsDB; 62543; -. [Q53T94-1]
DR ProteomicsDB; 62544; -. [Q53T94-2]
DR ProteomicsDB; 62545; -. [Q53T94-3]
DR Antibodypedia; 26617; 152 antibodies from 22 providers.
DR DNASU; 9014; -.
DR Ensembl; ENST00000263663.10; ENSP00000263663.4; ENSG00000115750.17. [Q53T94-1]
DR GeneID; 9014; -.
DR KEGG; hsa:9014; -.
DR MANE-Select; ENST00000263663.10; ENSP00000263663.4; NM_005680.3; NP_005671.3.
DR UCSC; uc002qzz.4; human. [Q53T94-1]
DR CTD; 9014; -.
DR DisGeNET; 9014; -.
DR GeneCards; TAF1B; -.
DR HGNC; HGNC:11533; TAF1B.
DR HPA; ENSG00000115750; Low tissue specificity.
DR MIM; 604904; gene.
DR neXtProt; NX_Q53T94; -.
DR OpenTargets; ENSG00000115750; -.
DR PharmGKB; PA36308; -.
DR VEuPathDB; HostDB:ENSG00000115750; -.
DR eggNOG; ENOG502QVGU; Eukaryota.
DR GeneTree; ENSGT00440000033827; -.
DR HOGENOM; CLU_032815_0_0_1; -.
DR InParanoid; Q53T94; -.
DR OMA; PRSFVWL; -.
DR OrthoDB; 329399at2759; -.
DR PhylomeDB; Q53T94; -.
DR TreeFam; TF324353; -.
DR PathwayCommons; Q53T94; -.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; Q53T94; -.
DR BioGRID-ORCS; 9014; 649 hits in 1079 CRISPR screens.
DR ChiTaRS; TAF1B; human.
DR GeneWiki; TAF1B; -.
DR GenomeRNAi; 9014; -.
DR Pharos; Q53T94; Tbio.
DR PRO; PR:Q53T94; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53T94; protein.
DR Bgee; ENSG00000115750; Expressed in adrenal tissue and 175 other tissues.
DR ExpressionAtlas; Q53T94; baseline and differential.
DR Genevisible; Q53T94; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; IDA:UniProtKB.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; TAS:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
DR InterPro; IPR033599; TAF1B/Rrn7.
DR InterPro; IPR021752; TF_Rrn7_Zf.
DR PANTHER; PTHR31576; PTHR31576; 1.
DR Pfam; PF11781; zf-RRN7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..588
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit B"
FT /id="PRO_0000261392"
FT ZN_FING 4..39
FT /note="RRN7-type"
FT REGION 40..68
FT /note="B-reader"
FT REGION 69..73
FT /note="B-linker"
FT REGION 74..261
FT /note="N-terminal cyclin fold"
FT REGION 262..372
FT /note="C-terminal cyclin fold"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 440
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..255
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042954"
FT VAR_SEQ 523..588
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021677"
FT VARIANT 6
FT /note="A -> S (in dbSNP:rs2303914)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7801123"
FT /id="VAR_029378"
FT VARIANT 282
FT /note="V -> I (in dbSNP:rs396190)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123"
FT /id="VAR_029379"
FT VARIANT 292
FT /note="R -> H (in dbSNP:rs16867223)"
FT /id="VAR_057260"
FT VARIANT 351
FT /note="T -> A (in dbSNP:rs1054565)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123"
FT /id="VAR_029380"
FT VARIANT 462
FT /note="E -> D (in dbSNP:rs1820965)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123"
FT /id="VAR_029381"
FT VARIANT 487
FT /note="T -> M (in dbSNP:rs16867245)"
FT /id="VAR_029382"
FT MUTAGEN 13
FT /note="C->A: Abolishes Pol I transcription but not
FT recruitment of SL1/TIF-IB complex to rDNA promoters."
FT /evidence="ECO:0000269|PubMed:21921199"
FT MUTAGEN 31
FT /note="C->A: Abolishes Pol I transcription but not
FT recruitment of SL1/TIF-IB complex to rDNA promoters."
FT /evidence="ECO:0000269|PubMed:21921199"
FT MUTAGEN 34
FT /note="C->A: Abolishes Pol I transcription but not
FT recruitment of SL1/TIF-IB complex to rDNA promoters."
FT /evidence="ECO:0000269|PubMed:21921199"
FT CONFLICT 1
FT /note="M -> L (in Ref. 1; AAA62863)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="L -> M (in Ref. 1; AAA62863)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="C -> W (in Ref. 1; AAA62863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 68832 MW; CE45DE622E28FD6E CRC64;
MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI PNTQIKALNR
GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL KNDVLHNFWK RYLQKSKQAY
CKNPVYTTGR KPTVLEDNLS HSDWASEPEL LSDVSCPPFL ESGAESQSDI HTRKPFPVSK
ASQSETSVCS GSLDGVEYSQ RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE
DHIPYINAFQ HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC
YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK TVKYDVQAVA
IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF RKWYQIMKKA FDEKKQKWEE
ARAKYLWKSE KPLYYSFVDK PVAYKKREMV VNLQKQFSTL VESTATAGKK SPSSFQFNWT
EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ
FILNLFSFLL RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH
