NS1BP_MOUSE
ID NS1BP_MOUSE Reviewed; 642 AA.
AC Q920Q8; Q06BK6; Q3TXI1; Q3UJE3; Q3UJS1; Q3UKH9; Q3UMK9; Q6ZQ34; Q99KN0;
AC Q9D978;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Influenza virus NS1A-binding protein homolog;
DE Short=NS1-BP;
DE Short=NS1-binding protein homolog;
DE AltName: Full=Kelch family protein Nd1-L;
DE AltName: Full=ND1-L2;
DE AltName: Full=Nd1-S;
GN Name=Ivns1abp; Synonyms=Kiaa0850, Nd1, Nd1L, Nd1S, Ns1, Ns1bp;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12213805; DOI=10.1074/jbc.m202596200;
RA Sasagawa K., Matsudo Y., Kang M., Fujimura L., Iitsuka Y., Okada S.,
RA Ochiai T., Tokuhisa T., Hatano M.;
RT "Identification of Nd1, a novel murine kelch family protein, involved in
RT stabilization of actin filaments.";
RL J. Biol. Chem. 277:44140-44146(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=KM;
RA Wang J., Xiao X.;
RT "Identification of novel variants of gene Nd1 in mouse.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=BALB/cJ, and C57BL/6J;
RC TISSUE=Amnion, Kidney, Lung, Mammary gland, Placenta, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 GENOMIC ORGANIZATION.
RX PubMed=11418182; DOI=10.1016/s0167-4781(01)00231-7;
RA Kang M., Matsudo Y., Sasagawa K., Tokuhisa T., Hatano M.;
RT "Nd1, a novel murine Kelch family protein, may play the role of a
RT housekeeping gene.";
RL Biochim. Biophys. Acta 1519:167-174(2001).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=15485691; DOI=10.1016/j.cardiores.2004.07.009;
RA Fujimura L., Matsudo Y., Kang M., Takamori Y., Tokuhisa T., Hatano M.;
RT "Protective role of Nd1 in doxorubicin-induced cardiotoxicity.";
RL Cardiovasc. Res. 64:315-321(2004).
RN [8]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION (ISOFORM
RP 2).
RX PubMed=15684717; DOI=10.1089/dna.2005.24.30;
RA Inoue A., Kang M., Fujimura L., Takamori Y., Sasagawa K., Itoh H.,
RA Tokuhisa T., Hatano M.;
RT "Overexpression of Nd1-s, a variant form of new kelch family protein,
RT perturbs the cell cycle progression of fibroblasts.";
RL DNA Cell Biol. 24:30-34(2005).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16317045; DOI=10.1242/jcs.02692;
RA Fujii R., Takumi T.;
RT "TLS facilitates transport of mRNA encoding an actin-stabilizing protein to
RT dendritic spines.";
RL J. Cell Sci. 118:5755-5765(2005).
RN [10]
RP INDUCTION.
RX PubMed=17016628;
RA Takamori Y., Matsudo Y., Fujimura L., Kang M., Harada Y., Moriya H.,
RA Tokuhisa T., Hatano M.;
RT "Expression of the Nd1 gene is down-regulated by doxorubicin at post-
RT transcriptional level.";
RL Int. J. Mol. Med. 18:963-967(2006).
RN [11]
RP TRANSGENIC MICE, FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16952015; DOI=10.1007/s11248-006-9010-x;
RA Matsudo Y., Takamori Y., Fujimura L., Nishio S., Sasagawa K., Komuro I.,
RA Tokuhisa T., Hatano M.;
RT "Overexpression of Nd1, a novel Kelch family protein, in the heart of
RT transgenic mice protects against doxorubicin-induced cardiomyopathy.";
RL Transgenic Res. 15:573-581(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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: Involved in many cell functions, including pre-mRNA splicing,
CC the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and
CC protein ubiquitination. Plays a role in the dynamic organization of the
CC actin skeleton as a stabilizer of actin filaments by association with
CC F-actin through Kelch repeats (PubMed:12213805, PubMed:16317045).
CC Protects cells from cell death induced by actin destabilization
CC (PubMed:16952015). Functions as modifier of the AHR/Aryl hydrocarbon
CC receptor pathway increasing the concentration of AHR available to
CC activate transcription (By similarity). In addition, functions as a
CC negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to
CC prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor
CC suppressors (By similarity). Inhibits pre-mRNA splicing (in vitro) (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y6Y0,
CC ECO:0000269|PubMed:12213805, ECO:0000269|PubMed:16317045,
CC ECO:0000269|PubMed:16952015}.
CC -!- FUNCTION: [Isoform 2]: May play a role in cell cycle progression in the
CC nucleus. {ECO:0000269|PubMed:15684717}.
CC -!- SUBUNIT: Homodimer; through the BTB domain. Interacts with AHR/Aryl
CC hydrocarbon receptor (By similarity). {ECO:0000250|UniProtKB:Q9Y6Y0}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12213805}. Note=Associated with actin filaments.
CC {ECO:0000269|PubMed:12213805}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:15684717}. Note=Not associated with actin filaments
CC (PubMed:15684717). {ECO:0000269|PubMed:15684717}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Nd1-L;
CC IsoId=Q920Q8-1; Sequence=Displayed;
CC Name=2; Synonyms=Nd1-S;
CC IsoId=Q920Q8-2; Sequence=VSP_024812, VSP_024813;
CC Name=3; Synonyms=Nd1-L2;
CC IsoId=Q920Q8-3; Sequence=VSP_024811;
CC Name=4;
CC IsoId=Q920Q8-4; Sequence=VSP_024810;
CC -!- TISSUE SPECIFICITY: Ubiquitous expression. In the heart, the highest
CC expression is detected in the ventricles and the lowest in the atria.
CC Expressed in dendrites and spines in neurons.
CC {ECO:0000269|PubMed:12213805, ECO:0000269|PubMed:15684717,
CC ECO:0000269|PubMed:16317045}.
CC -!- DEVELOPMENTAL STAGE: Barely detected in the heart at 15.5 dpc, but
CC clearly expressed in newborn heart with increased amount up to 8 weeks
CC of age. {ECO:0000269|PubMed:16952015}.
CC -!- INDUCTION: Decreased expression in various organs and cultured cell
CC lines by doxorubicin treatment which may reduce mRNA stability.
CC {ECO:0000269|PubMed:16952015, ECO:0000269|PubMed:17016628}.
CC -!- DOMAIN: When the BTB domain is lacking, AHR signaling induction
CC promoted by IVNS1ABP is massively increased; Thus, the BTB domain
CC inhibits AHR signaling induced by IVNS1ABP.
CC {ECO:0000250|UniProtKB:Q9Y6Y0}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally with no gross
CC abnormalities. However, they display marked sensitivity to doxorubicin
CC cardiotoxicity with increased number of cardiomyocytes apoptosis.
CC Analysis of hearts from knockout mice reveal vacuolization and edema of
CC cardiomaycytes. {ECO:0000269|PubMed:15485691}.
CC -!- MISCELLANEOUS: Transgenic mice overexpressing Ivns1abp develop normally
CC with no gross abnormalities up to 7-month old. However, they display a
CC marked resistance to the cardiotoxic effect of doxorubicin which is an
CC anti-neoplastic agent known to affect actin skeleton and an effective
CC drug for cancer therapy with cardiotoxicity as side effect.
CC Overexpression of Ivns1abp in the heart protect cardiomyocytes from
CC apoptosis and improved survival rate after doxorubicin injection.
CC {ECO:0000269|PubMed:15485691}.
CC -!- MISCELLANEOUS: Disorganized actin skeleton is observed in cells
CC transfected with isoform 2 (Nd1-S), which lacks the six kelch repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AB055737; BAB69058.1; -; mRNA.
DR EMBL; AB055738; BAB69059.1; -; mRNA.
DR EMBL; DQ914522; ABI84241.1; -; mRNA.
DR EMBL; AK129229; BAC98039.1; ALT_INIT; mRNA.
DR EMBL; AK007291; BAB24936.1; -; mRNA.
DR EMBL; AK144835; BAE26089.1; -; mRNA.
DR EMBL; AK145071; BAE26221.1; -; mRNA.
DR EMBL; AK146001; BAE26822.1; -; mRNA.
DR EMBL; AK146329; BAE27084.1; -; mRNA.
DR EMBL; AK146494; BAE27212.1; -; mRNA.
DR EMBL; AK146645; BAE27326.1; -; mRNA.
DR EMBL; AK159254; BAE34935.1; -; mRNA.
DR EMBL; BC004092; AAH04092.1; -; mRNA.
DR EMBL; BC040250; AAH40250.1; -; mRNA.
DR CCDS; CCDS15358.1; -. [Q920Q8-4]
DR CCDS; CCDS15359.1; -. [Q920Q8-1]
DR CCDS; CCDS35735.1; -. [Q920Q8-2]
DR RefSeq; NP_001034600.1; NM_001039511.1. [Q920Q8-2]
DR RefSeq; NP_001034601.1; NM_001039512.1. [Q920Q8-4]
DR RefSeq; NP_473443.2; NM_054102.2. [Q920Q8-1]
DR AlphaFoldDB; Q920Q8; -.
DR SMR; Q920Q8; -.
DR BioGRID; 228184; 28.
DR IntAct; Q920Q8; 8.
DR MINT; Q920Q8; -.
DR STRING; 10090.ENSMUSP00000023918; -.
DR iPTMnet; Q920Q8; -.
DR PhosphoSitePlus; Q920Q8; -.
DR EPD; Q920Q8; -.
DR jPOST; Q920Q8; -.
DR MaxQB; Q920Q8; -.
DR PaxDb; Q920Q8; -.
DR PeptideAtlas; Q920Q8; -.
DR PRIDE; Q920Q8; -.
DR ProteomicsDB; 294052; -. [Q920Q8-1]
DR ProteomicsDB; 294053; -. [Q920Q8-2]
DR ProteomicsDB; 294054; -. [Q920Q8-3]
DR ProteomicsDB; 294055; -. [Q920Q8-4]
DR Antibodypedia; 1274; 121 antibodies from 26 providers.
DR DNASU; 117198; -.
DR Ensembl; ENSMUST00000023918; ENSMUSP00000023918; ENSMUSG00000023150. [Q920Q8-1]
DR Ensembl; ENSMUST00000097543; ENSMUSP00000095150; ENSMUSG00000023150. [Q920Q8-4]
DR Ensembl; ENSMUST00000111887; ENSMUSP00000107518; ENSMUSG00000023150. [Q920Q8-2]
DR Ensembl; ENSMUST00000186745; ENSMUSP00000140708; ENSMUSG00000023150. [Q920Q8-2]
DR GeneID; 117198; -.
DR KEGG; mmu:117198; -.
DR UCSC; uc007cym.1; mouse. [Q920Q8-2]
DR UCSC; uc007cyn.1; mouse. [Q920Q8-1]
DR UCSC; uc007cyo.1; mouse. [Q920Q8-4]
DR CTD; 10625; -.
DR MGI; MGI:2152389; Ivns1abp.
DR VEuPathDB; HostDB:ENSMUSG00000023150; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155635; -.
DR HOGENOM; CLU_004253_11_0_1; -.
DR InParanoid; Q920Q8; -.
DR OMA; TWTFIAP; -.
DR OrthoDB; 251780at2759; -.
DR PhylomeDB; Q920Q8; -.
DR TreeFam; TF329218; -.
DR BioGRID-ORCS; 117198; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ivns1abp; mouse.
DR PRO; PR:Q920Q8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q920Q8; protein.
DR Bgee; ENSMUSG00000023150; Expressed in metanephric cortical collecting duct and 302 other tissues.
DR ExpressionAtlas; Q920Q8; baseline and differential.
DR Genevisible; Q920Q8; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; ISO:MGI.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Kelch repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..642
FT /note="Influenza virus NS1A-binding protein homolog"
FT /id="PRO_0000285078"
FT DOMAIN 32..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 134..233
FT /note="BACK"
FT REPEAT 369..415
FT /note="Kelch 1"
FT REPEAT 416..463
FT /note="Kelch 2"
FT REPEAT 465..512
FT /note="Kelch 3"
FT REPEAT 513..559
FT /note="Kelch 4"
FT REPEAT 561..606
FT /note="Kelch 5"
FT REPEAT 608..642
FT /note="Kelch 6"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Y0"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Y0"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Y0"
FT VAR_SEQ 178..219
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024810"
FT VAR_SEQ 179..218
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024811"
FT VAR_SEQ 221
FT /note="Q -> Y (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12213805,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_024812"
FT VAR_SEQ 222..642
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12213805,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_024813"
FT CONFLICT 106
FT /note="Y -> H (in Ref. 4; BAE26822)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="W -> R (in Ref. 4; BAE34935)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="P -> T (in Ref. 4; BAE27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="E -> K (in Ref. 4; BAE27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="P -> S (in Ref. 5; AAH04092)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="A -> S (in Ref. 4; BAE27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="R -> K (in Ref. 1; BAB69058)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="M -> I (in Ref. 4; BAE27084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 71581 MW; 7240360079C16B50 CRC64;
MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL ACCSPYLFEI
FNSDSDPHGV SHVKLDDLNP EAVEVLLNYA YTAQLKADKE LVKDVYSAAK KLKMDRVKQV
CGDYLLSRMD VTSCISYRNF ASCMGDSRLL NKVDAYIQEH LLQISEEEEF LKLPRLKLEV
MLEDNVCLPS NGKLYTKVIN WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNPLDGQ
AEVFGSDDDH IQFVQKKPPR ENGHKQISGS STGCLSSPNA SMQSPKHEWK IVASEKTSNN
TYLCLAVLDS TFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQPDELLEKP MSPMQYARSG
LGTAEMNGKL IAAGGYNREE CLRTVECYDP HTDHWSFLAP MRTPRARFQM AVLMGQLYVV
GGSNGHSDDL SCGEMYDPNI DDWTPVPELR TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK
NCDVFDPVTK SWTSCAPLNI RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT
LIAPMNVARR GAGVAVLDGK LFVGGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG
ITTVGNTIYA VGGFDGNEFL NTVEVYNPQS NEWSPYTKIF QF
