KLF8_HUMAN
ID KLF8_HUMAN Reviewed; 359 AA.
AC O95600; B4DJN3; E7EQQ8; L0R3U8; L0R4U2; Q2M246; Q59GV5; Q5HYQ5; Q5JXP7;
AC Q6MZJ7; Q9UGC4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Krueppel-like factor 8;
DE AltName: Full=Basic krueppel-like factor 3;
DE AltName: Full=Zinc finger protein 741;
GN Name=KLF8; Synonyms=BKLF3, ZNF741;
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] (ISOFORM 1).
RA Gorski J.L., MacDonald M., Vananthwerp M., Burright E.N., Bialecki M.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND ALTERNATIVE SPLICING.
RX PubMed=23134681; DOI=10.1096/fj.12-220319;
RA Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B., Camacho S.C.,
RA Martignetti J.A.;
RT "Shaking the family tree: Identification of novel and biologically active
RT alternatively spliced isoforms across the KLF family of transcription
RT factors.";
RL FASEB J. 27:432-436(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=10756197; DOI=10.1093/nar/28.9.1955;
RA van Vliet J., Turner J., Crossley M.;
RT "Human Kruppel-like factor 8: a CACCC-box binding protein that associates
RT with CtBP and represses transcription.";
RL Nucleic Acids Res. 28:1955-1962(2000).
RN [9]
RP FUNCTION.
RX PubMed=12820964; DOI=10.1016/s1097-2765(03)00179-5;
RA Zhao J., Bian Z.C., Yee K., Chen B.P., Chien S., Guan J.L.;
RT "Identification of transcription factor KLF8 as a downstream target of
RT focal adhesion kinase in its regulation of cyclin D1 and cell cycle
RT progression.";
RL Mol. Cell 11:1503-1515(2003).
RN [10]
RP SUMOYLATION AT LYS-67, INTERACTION WITH PIAS1; PIAS2 AND PIAS4, FUNCTION,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-67 AND LYS-217.
RX PubMed=16617055; DOI=10.1074/jbc.m513135200;
RA Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L.,
RA Zhao J.;
RT "Sumoylation delimits KLF8 transcriptional activity associated with the
RT cell cycle regulation.";
RL J. Biol. Chem. 281:16664-16671(2006).
RN [11]
RP INACTIVATION OF 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
CC -!- FUNCTION: Transcriptional repressor and activator. Binds to CACCC-boxes
CC promoter elements. Also binds the GT-box of cyclin D1 promoter and
CC mediates cell cycle progression at G(1) phase as a downstream target of
CC focal adhesion kinase (FAK). {ECO:0000269|PubMed:10756197,
CC ECO:0000269|PubMed:12820964, ECO:0000269|PubMed:16617055}.
CC -!- SUBUNIT: Interacts with corepressor CtBP2. Interacts with PIAS1, PIAS2,
CC AND PIAS4; the interaction with each ligase sumoylates KLF8.
CC {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:16617055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95600-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95600-3; Sequence=VSP_045460;
CC Name=3;
CC IsoId=O95600-4; Sequence=VSP_047480, VSP_045460;
CC Name=4;
CC IsoId=O95600-5; Sequence=VSP_047481;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10756197}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In KLF8, the motif is
CC inactive. {ECO:0000269|PubMed:31375868}.
CC -!- PTM: Sumoylation at Lys-67 represses transcriptional activity and
CC reduces cell cycle progression into the G(1) phase. Has no effect on
CC subcellular location. {ECO:0000269|PubMed:16617055}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U28282; AAC99849.1; -; mRNA.
DR EMBL; HF546207; CCO02793.1; -; mRNA.
DR EMBL; HF546208; CCO02794.1; -; mRNA.
DR EMBL; HF546209; CCO02795.1; -; mRNA.
DR EMBL; AK296156; BAG58895.1; -; mRNA.
DR EMBL; AB209004; BAD92241.1; ALT_SEQ; mRNA.
DR EMBL; BX641066; CAE46033.1; ALT_SEQ; mRNA.
DR EMBL; AL050309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX322609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105130; AAI05131.1; -; mRNA.
DR EMBL; BC112109; AAI12110.1; -; mRNA.
DR CCDS; CCDS14373.1; -. [O95600-1]
DR CCDS; CCDS55428.1; -. [O95600-3]
DR CCDS; CCDS87749.1; -. [O95600-4]
DR RefSeq; NP_001152768.1; NM_001159296.2. [O95600-3]
DR RefSeq; NP_001311028.1; NM_001324099.1. [O95600-4]
DR RefSeq; NP_001311029.1; NM_001324100.1. [O95600-5]
DR RefSeq; NP_001311031.1; NM_001324102.1. [O95600-1]
DR RefSeq; NP_009181.2; NM_007250.5. [O95600-1]
DR RefSeq; XP_005262034.1; XM_005261977.2. [O95600-1]
DR RefSeq; XP_005262036.1; XM_005261979.3.
DR RefSeq; XP_006724638.1; XM_006724575.2. [O95600-3]
DR AlphaFoldDB; O95600; -.
DR SMR; O95600; -.
DR BioGRID; 116435; 326.
DR ELM; O95600; -.
DR IntAct; O95600; 317.
DR MINT; O95600; -.
DR STRING; 9606.ENSP00000417303; -.
DR GlyGen; O95600; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95600; -.
DR PhosphoSitePlus; O95600; -.
DR BioMuta; KLF8; -.
DR jPOST; O95600; -.
DR MassIVE; O95600; -.
DR PaxDb; O95600; -.
DR PeptideAtlas; O95600; -.
DR PRIDE; O95600; -.
DR ProteomicsDB; 50947; -. [O95600-1]
DR Antibodypedia; 13002; 225 antibodies from 32 providers.
DR DNASU; 11279; -.
DR Ensembl; ENST00000374928.7; ENSP00000364063.3; ENSG00000102349.18. [O95600-3]
DR Ensembl; ENST00000468660.6; ENSP00000417303.1; ENSG00000102349.18. [O95600-1]
DR Ensembl; ENST00000640927.1; ENSP00000492126.1; ENSG00000102349.18. [O95600-4]
DR GeneID; 11279; -.
DR KEGG; hsa:11279; -.
DR MANE-Select; ENST00000468660.6; ENSP00000417303.1; NM_007250.5; NP_009181.2.
DR UCSC; uc004dur.4; human. [O95600-1]
DR CTD; 11279; -.
DR DisGeNET; 11279; -.
DR GeneCards; KLF8; -.
DR HGNC; HGNC:6351; KLF8.
DR HPA; ENSG00000102349; Tissue enhanced (skin).
DR MIM; 300286; gene.
DR neXtProt; NX_O95600; -.
DR OpenTargets; ENSG00000102349; -.
DR PharmGKB; PA30141; -.
DR VEuPathDB; HostDB:ENSG00000102349; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161062; -.
DR HOGENOM; CLU_002678_33_0_1; -.
DR InParanoid; O95600; -.
DR OMA; KMTSPPF; -.
DR PhylomeDB; O95600; -.
DR TreeFam; TF350556; -.
DR PathwayCommons; O95600; -.
DR SignaLink; O95600; -.
DR SIGNOR; O95600; -.
DR BioGRID-ORCS; 11279; 7 hits in 721 CRISPR screens.
DR ChiTaRS; KLF8; human.
DR GeneWiki; KLF8; -.
DR GenomeRNAi; 11279; -.
DR Pharos; O95600; Tbio.
DR PRO; PR:O95600; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O95600; protein.
DR Bgee; ENSG00000102349; Expressed in esophagus squamous epithelium and 161 other tissues.
DR ExpressionAtlas; O95600; baseline and differential.
DR Genevisible; O95600; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="Krueppel-like factor 8"
FT /id="PRO_0000047176"
FT ZN_FING 274..298
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..328
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..93
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000269|PubMed:31375868"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 1..27
FT /note="MVDMDKLINNLEVQLNSEGGSMQVFKQ -> MSLPEDGMSSGHFRSPQLVTW
FT S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047480"
FT VAR_SEQ 216..299
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047481"
FT VAR_SEQ 254..359
FT /note="PAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYK
FT CTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM -> R
FT EAL (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:23134681"
FT /id="VSP_045460"
FT MUTAGEN 67
FT /note="K->R: Abolishes sumoylation. No change in nuclear
FT location. Increases transcriptional activity and cell cycle
FT progression. Abolishes sumoylation; when associated with R-
FT 217."
FT /evidence="ECO:0000269|PubMed:16617055"
FT MUTAGEN 217
FT /note="K->R: No change in sumoylation. Abolishes
FT sumoylation; when associated with R-67."
FT /evidence="ECO:0000269|PubMed:16617055"
FT CONFLICT 167
FT /note="S -> I (in Ref. 3; BAG58895)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> G (in Ref. 1; AAC99849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39314 MW; F8FDCC1FD477C04F CRC64;
MVDMDKLINN LEVQLNSEGG SMQVFKQVTA SVRNRDPPEI EYRSNMTSPT LLDANPMENP
ALFNDIKIEP PEELLASDFS LPQVEPVDLS FHKPKAPLQP ASMLQAPIRP PKPQSSPQTL
VVSTSTSDMS TSANIPTVLT PGSVLTSSQS TGSQQILHVI HTIPSVSLPN KMGGLKTIPV
VVQSLPMVYT TLPADGGPAA ITVPLIGGDG KNAGSVKVDP TSMSPLEIPS DSEESTIESG
SSALQSLQGL QQEPAAMAQM QGEESLDLKR RRIHQCDFAG CSKVYTKSSH LKAHRRIHTG
EKPYKCTWDG CSWKFARSDE LTRHFRKHTG IKPFRCTDCN RSFSRSDHLS LHRRRHDTM
