HBB1_MOUSE
ID HBB1_MOUSE Reviewed; 147 AA.
AC P02088; Q54AI0; Q91V86; Q9CRZ2; Q9CXH5; Q9CY12; Q9CY54; Q9R0S6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Hemoglobin beta-1 chain;
DE AltName: Full=Hemoglobin beta-major chain;
GN Name=Hbb-b1;
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 [GENOMIC DNA].
RX PubMed=2926808; DOI=10.1016/0022-2836(89)90363-x;
RA Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P.,
RA Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F.,
RA Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III;
RT "Nucleotide sequence of the BALB/c mouse beta-globin complex.";
RL J. Mol. Biol. 205:41-62(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=519759; DOI=10.1016/0092-8674(79)90138-7;
RA Konkel D.A., Maizel J.V. Jr., Leder P.;
RT "The evolution and sequence comparison of two recently diverged mouse
RT chromosomal beta-globin genes.";
RL Cell 18:865-873(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=482942; DOI=10.1126/science.482942;
RA van Ooyen A., van den Berg J., Mantei N., Weissmann C.;
RT "Comparison of total sequence of a cloned rabbit beta-globin gene and its
RT flanking regions with a homologous mouse sequence.";
RL Science 206:337-344(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S).
RC STRAIN=C57BL/10;
RX PubMed=3870864; DOI=10.1093/oxfordjournals.molbev.a040353;
RA Erhart M.A., Simons K.S., Weaver S.;
RT "Evolution of the mouse beta-globin genes: a recent gene conversion in the
RT Hbbs haplotype.";
RL Mol. Biol. Evol. 2:304-320(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES P AND W1).
RX PubMed=10441738; DOI=10.1007/s003359901107;
RA Ueda Y., Miyashita N., Imai K., Yamaguchi Y., Takamura K., Notohara M.,
RA Shiroishi T., Kawashima T., Ning L., Wang C., Wu X., Moriwaki K.;
RT "Nucleotide sequences of the mouse globin beta gene cDNAs in a wild derived
RT new haplotype Hbb(w1).";
RL Mamm. Genome 10:879-882(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Head, Heart, Kidney, Liver, Placenta, Spleen, Stomach, 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 [7]
RP PROTEIN SEQUENCE OF 19-41; 32-60 AND 67-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-109.
RX PubMed=277329; DOI=10.1101/sqb.1978.042.01.098;
RA Curtis P.J., Mantei N., Weissmann C.;
RT "Characterization and kinetics of synthesis of 15S beta-globin RNA, a
RT putative precursor of beta-globin mRNA.";
RL Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-44 AND 100-115.
RX PubMed=264241; DOI=10.1038/276037a0;
RA van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G.,
RA Flavell R.A., Weissmann C.;
RT "Comparison of cloned rabbit and mouse beta-globin genes showing strong
RT evolutionary divergence of two homologous pairs of introns.";
RL Nature 276:37-44(1978).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-105.
RX PubMed=273235; DOI=10.1073/pnas.75.2.725;
RA Tilghman S.M., Tiemeier D.C., Seidman J.G., Peterlin B.M., Sullivan M.,
RA Maizel J.V. Jr., Leder P.;
RT "Intervening sequence of DNA identified in the structural portion of a
RT mouse beta-globin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:725-729(1978).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [13]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME.
RX PubMed=11747442; DOI=10.1021/bi011329f;
RA Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.;
RT "The role of beta chains in the control of the hemoglobin oxygen binding
RT function: chimeric human/mouse proteins, structure, and function.";
RL Biochemistry 40:15669-15675(2001).
RN [15]
RP VARIANTS ALLELIC.
RX PubMed=999642; DOI=10.1042/bj1590043;
RA Gilman J.G.;
RT "Mouse haemoglobin beta chains. Comparative sequence data on adult major
RT and minor beta chains from two species, Mus musculus and Mus cervicolor.";
RL Biochem. J. 159:43-53(1976).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: Inbred mouse strains possess 1 of 4 alleles at the HBB
CC locus: D (diffuse), S (single), P and W1. The D and P alleles are
CC actually closely linked doublets that coordinately express a major and
CC a minor chain, the minor chain being slightly different in the two
CC alleles. The S allele produces only 1 chain, it is characteristic of
CC North American wild mice. The W1 allele is observed mainly in
CC Northwestern China. {ECO:0000269|PubMed:10441738,
CC ECO:0000269|PubMed:3870864, ECO:0000269|PubMed:999642}.
CC -!- MISCELLANEOUS: The D-major sequence is shown. See also the entry for
CC the beta D and P-minor chain.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X14061; CAA32224.1; -; Genomic_DNA.
DR EMBL; J00413; AAA37791.1; -; Genomic_DNA.
DR EMBL; AB020013; BAA77353.1; -; mRNA.
DR EMBL; AB020015; BAA77355.1; -; mRNA.
DR EMBL; AK002258; BAB21971.1; -; mRNA.
DR EMBL; AK002394; BAB22067.1; -; mRNA.
DR EMBL; AK003096; BAB22562.1; -; mRNA.
DR EMBL; AK003472; BAB22806.1; -; mRNA.
DR EMBL; AK005442; BAB24036.1; -; mRNA.
DR EMBL; AK005490; BAB24075.1; -; mRNA.
DR EMBL; AK005496; BAB24080.1; -; mRNA.
DR EMBL; AK010873; BAB27237.1; -; mRNA.
DR EMBL; AK010902; BAB27255.1; -; mRNA.
DR EMBL; AK010980; BAB27302.1; -; mRNA.
DR EMBL; AK010981; BAB27303.1; -; mRNA.
DR EMBL; AK010991; BAB27310.1; -; mRNA.
DR EMBL; AK010993; BAB27312.1; -; mRNA.
DR EMBL; AK011006; BAB27325.1; -; mRNA.
DR EMBL; AK011013; BAB27331.1; -; mRNA.
DR EMBL; AK011016; BAB27334.1; -; mRNA.
DR EMBL; AK011027; BAB27343.1; -; mRNA.
DR EMBL; AK011033; BAB27347.1; -; mRNA.
DR EMBL; AK011050; BAB27360.1; -; mRNA.
DR EMBL; AK011052; BAB27361.1; -; mRNA.
DR EMBL; AK011053; BAB27362.1; -; mRNA.
DR EMBL; AK011057; BAB27365.1; -; mRNA.
DR EMBL; AK011067; BAB27374.1; -; mRNA.
DR EMBL; AK011069; BAB27376.1; -; mRNA.
DR EMBL; AK011075; BAB27380.1; -; mRNA.
DR EMBL; AK011077; BAB27382.1; -; mRNA.
DR EMBL; AK011083; BAB27387.1; -; mRNA.
DR EMBL; AK011102; BAB27399.1; -; mRNA.
DR EMBL; AK012551; BAB28311.1; -; mRNA.
DR EMBL; AK014364; BAB29299.1; -; mRNA.
DR EMBL; AK027903; BAC25655.1; -; mRNA.
DR EMBL; AK027904; BAC25656.1; -; mRNA.
DR EMBL; AK028067; BAC25734.1; -; mRNA.
DR EMBL; AK088149; BAC40173.1; -; mRNA.
DR EMBL; AK133714; BAE21794.1; -; mRNA.
DR EMBL; AK147001; BAE27598.1; -; mRNA.
DR EMBL; AK160629; BAE35926.1; -; mRNA.
DR EMBL; AK161021; BAE36152.1; -; mRNA.
DR EMBL; AK165490; BAE38217.1; -; mRNA.
DR EMBL; AK167615; BAE39668.1; -; mRNA.
DR EMBL; AK168412; BAE40327.1; -; mRNA.
DR EMBL; AK168477; BAE40366.1; -; mRNA.
DR EMBL; AK168562; BAE40435.1; -; mRNA.
DR EMBL; AK168584; BAE40453.1; -; mRNA.
DR EMBL; AK168819; BAE40646.1; -; mRNA.
DR EMBL; AK168826; BAE40653.1; -; mRNA.
DR EMBL; AK168846; BAE40669.1; -; mRNA.
DR EMBL; M19236; AAA37788.1; -; mRNA.
DR EMBL; M10828; AAA37786.1; -; Genomic_DNA.
DR EMBL; M10830; AAA37787.1; -; Genomic_DNA.
DR EMBL; M10829; AAA37787.1; JOINED; Genomic_DNA.
DR EMBL; M10688; AAA37790.1; -; Genomic_DNA.
DR PIR; A90790; HBMS.
DR RefSeq; NP_001188320.1; NM_001201391.1.
DR RefSeq; NP_001265090.1; NM_001278161.1.
DR RefSeq; NP_032246.2; NM_008220.5.
DR PDB; 1JEB; X-ray; 2.10 A; B/D=2-147.
DR PDB; 3HRW; X-ray; 2.80 A; B/D=2-147.
DR PDBsum; 1JEB; -.
DR PDBsum; 3HRW; -.
DR AlphaFoldDB; P02088; -.
DR SMR; P02088; -.
DR BioGRID; 1639840; 3.
DR BioGRID; 200219; 8.
DR BioGRID; 3405151; 3.
DR ComplexPortal; CPX-2922; Hemoglobin HbA complex, variant HBB1.
DR IntAct; P02088; 7.
DR MINT; P02088; -.
DR STRING; 10090.ENSMUSP00000023934; -.
DR CarbonylDB; P02088; -.
DR iPTMnet; P02088; -.
DR PhosphoSitePlus; P02088; -.
DR SwissPalm; P02088; -.
DR REPRODUCTION-2DPAGE; IPI00553333; -.
DR REPRODUCTION-2DPAGE; P02088; -.
DR SWISS-2DPAGE; P02088; -.
DR jPOST; P02088; -.
DR MaxQB; P02088; -.
DR PaxDb; P02088; -.
DR PeptideAtlas; P02088; -.
DR PRIDE; P02088; -.
DR ProteomicsDB; 269721; -.
DR DNASU; 15129; -.
DR GeneID; 100503605; -.
DR GeneID; 101488143; -.
DR GeneID; 15129; -.
DR KEGG; mmu:100503605; -.
DR KEGG; mmu:101488143; -.
DR KEGG; mmu:15129; -.
DR UCSC; uc009iuq.3; mouse.
DR CTD; 100503605; -.
DR CTD; 101488143; -.
DR CTD; 15129; -.
DR MGI; MGI:96021; Hbb-b1.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P02088; -.
DR OrthoDB; 1370439at2759; -.
DR PhylomeDB; P02088; -.
DR BioGRID-ORCS; 100503605; 0 hits in 20 CRISPR screens.
DR BioGRID-ORCS; 101488143; 0 hits in 20 CRISPR screens.
DR BioGRID-ORCS; 15129; 3 hits in 18 CRISPR screens.
DR EvolutionaryTrace; P02088; -.
DR PRO; PR:P02088; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P02088; protein.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:MGI.
DR GO; GO:0005833; C:hemoglobin complex; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0031720; F:haptoglobin binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; ISO:MGI.
DR GO; GO:0031722; F:hemoglobin beta binding; ISO:MGI.
DR GO; GO:0030492; F:hemoglobin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; ISO:MGI.
DR GO; GO:0005344; F:oxygen carrier activity; IMP:MGI.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0015671; P:oxygen transport; IMP:MGI.
DR GO; GO:0010999; P:regulation of eIF2 alpha phosphorylation by heme; IMP:MGI.
DR CDD; cd08925; Hb-beta-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Methylation; Oxygen transport; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000053024"
FT BINDING 64
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000250|UniProtKB:P80044"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:11747442,
FT ECO:0007744|PDB:1JEB, ECO:0007744|PDB:3HRW"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11517"
FT VARIANT 14
FT /note="C -> G (in allele S and allele W1)"
FT /evidence="ECO:0000269|PubMed:10441738,
FT ECO:0000269|PubMed:3870864, ECO:0000269|PubMed:999642"
FT VARIANT 21
FT /note="S -> A (in allele S)"
FT /evidence="ECO:0000269|PubMed:3870864,
FT ECO:0000269|PubMed:999642"
FT VARIANT 74
FT /note="D -> E (in allele W1)"
FT /evidence="ECO:0000269|PubMed:10441738,
FT ECO:0000269|PubMed:999642"
FT VARIANT 135
FT /note="V -> M (in allele W1)"
FT /evidence="ECO:0000269|PubMed:10441738,
FT ECO:0000269|PubMed:999642"
FT VARIANT 140
FT /note="T -> A (in allele S)"
FT /evidence="ECO:0000269|PubMed:3870864,
FT ECO:0000269|PubMed:999642"
FT CONFLICT 15
FT /note="L -> Q (in Ref. 6; BAB27362)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="T -> A (in Ref. 6; BAB29299)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="A -> T (in Ref. 6; BAB27237)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="E -> Q (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> S (in Ref. 6; BAB29299)"
FT /evidence="ECO:0000305"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:1JEB"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1JEB"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:1JEB"
SQ SEQUENCE 147 AA; 15840 MW; 8190EAEEFD9036A3 CRC64;
MVHLTDAEKA AVSCLWGKVN SDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK
VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
KDFTPAAQAA FQKVVAGVAT ALAHKYH
