CASB_BOVIN
ID CASB_BOVIN Reviewed; 224 AA.
AC P02666; A1YQZ8; A6N8V0; Q2TA13; Q5EEQ6; Q5EEQ7; Q6UN63; Q9BDG5; Q9TSD5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Beta-casein;
DE Contains:
DE RecName: Full=Casoparan;
DE Contains:
DE RecName: Full=Antioxidant peptide;
DE Contains:
DE RecName: Full=Casohypotensin;
DE Flags: Precursor;
GN Name=CSN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-108; PRO-152 AND LEU-153.
RX PubMed=3814153; DOI=10.1016/0006-291x(87)90318-4;
RA Jimenez-Flores R., Kang Y.C., Richardson T.;
RT "Cloning and sequence analysis of bovine beta-casein cDNA.";
RL Biochem. Biophys. Res. Commun. 142:617-621(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-82.
RA Baev A.A., Smirnov I.K., Gorodetsky S.I.;
RT "Primary structure of bovine beta-casein cDNA.";
RL Mol. Biol. (Mosk.) 21:214-222(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2833669; DOI=10.1093/oxfordjournals.molbev.a040437;
RA Stewart A.F., Bonsing J., Beattie C.W., Shah F., Willis I.M.,
RA Mackinlay A.G.;
RT "Complete nucleotide sequences of bovine alpha S2- and beta-casein cDNAs:
RT comparisons with related sequences in other species.";
RL Mol. Biol. Evol. 4:231-241(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-82.
RX PubMed=3271384; DOI=10.1071/bi9880527;
RA Bonsing J., Ring J.M., Stewart A.F., Mackinlay A.G.;
RT "Complete nucleotide sequence of the bovine beta-casein gene.";
RL Aust. J. Biol. Sci. 41:527-537(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT A3 GLN-121.
RC TISSUE=Mammary gland;
RX PubMed=8248100; DOI=10.1093/protein/6.7.763;
RA Simons G., van den Heuvel W., Reynen T., Frijters A., Rutten G.,
RA Slangen C.J., Groenen M., de Vos W.M., Siezen R.J.;
RT "Overproduction of bovine beta-casein in Escherichia coli and engineering
RT of its main chymosin cleavage site.";
RL Protein Eng. 6:763-770(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-82 AND ARG-137.
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-101.
RC TISSUE=Mammary epithelium;
RX PubMed=16624358; DOI=10.1016/j.rvsc.2006.02.002;
RA Anaya-Lopez J.L., Contreras-Guzman O.E., Carabez-Trejo A.,
RA Baizabal-Aguirre V.M., Lopez-Meza J.E., Valdez-Alarcon J.J.,
RA Ochoa-Zarzosa A.;
RT "Invasive potential of bacterial isolates associated with subclinical
RT bovine mastitis.";
RL Res. Vet. Sci. 81:358-361(2006).
RN [8]
RP PROTEIN SEQUENCE OF 16-224 (VARIANT A2), AND VARIANT LEU-108.
RX PubMed=4557764; DOI=10.1111/j.1432-1033.1972.tb01722.x;
RA Ribadeau-Dumas B., Brignon G., Grosclaude F., Mercier J.-C.;
RT "Primary structure of bovine beta casein. Complete sequence.";
RL Eur. J. Biochem. 25:505-514(1972).
RN [9]
RP PROTEIN SEQUENCE OF 16-224 (VARIANT A2).
RX PubMed=3278933; DOI=10.1016/0014-5793(88)81138-4;
RA Carles C., Huet J.-C., Ribadeau-Dumas B.;
RT "A new strategy for primary structure determination of proteins:
RT application to bovine beta-casein.";
RL FEBS Lett. 229:265-272(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-57, PROTEIN SEQUENCE OF 16-224
RP (VARIANT H), AND VARIANT D LYS-33.
RC STRAIN=Korean; TISSUE=Milk;
RX PubMed=10690361; DOI=10.1046/j.1365-2052.2000.00582.x;
RA Han S.K., Shin Y.C., Byun H.D.;
RT "Biochemical, molecular and physiological characterization of a new beta-
RT casein variant detected in Korean cattle.";
RL Anim. Genet. 31:49-51(2000).
RN [11]
RP PROTEIN SEQUENCE OF 41-71; 113-157 AND 180-224, AND VARIANT GLN-132.
RX PubMed=1804413; DOI=10.1002/rcm.1290050410;
RA Jones D.S., Heerma W., van Wassenaar P.D., Haverkamp J.;
RT "Analysis of bovine beta-casein tryptic digest by continuous-flow fast-atom
RT bombardment mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 5:192-195(1991).
RN [12]
RP PROTEIN SEQUENCE OF 41-45, AND FUNCTION.
RX PubMed=15545057; DOI=10.1080/09629350400003068;
RA Lebrun I., Cavallaro V., Juliano L., Juliano M.A., de Sousa e Silva M.C.C.;
RT "Effects of 'casoparan', a peptide isolated from casein hydrolysates with
RT mastoparan-like properties.";
RL Mediators Inflamm. 13:263-268(2004).
RN [13]
RP PROTEIN SEQUENCE OF 48-63, AND VARIANT E LYS-51.
RX PubMed=4411121; DOI=10.1016/0014-5793(74)80796-9;
RA Grosclaude F., Mahe M.-F., Voglino G.-F.;
RT "The beta E variant and the phosphorylation code of bovine caseins.";
RL FEBS Lett. 45:3-5(1974).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-223.
RA Otaviano A.R., Lima A.L.F., Laureano M.M.M., Albuquerque L.G., Tonhati H.,
RA Sena J.A.D.;
RT "Polymorphisms in beta and kappa casein genes in bubaline and bovine.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-223.
RA Shahla M.N., Cheema F.R., Naeem M.K., Riazuddin S.;
RT "Polymorphism in the cattle beta casein gene.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-208.
RC TISSUE=Mammary gland;
RA Klotz A., Buchberger J., Krause I., Einspanier R.;
RT "Characterization of milk proteins.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-105.
RX PubMed=6397405; DOI=10.1016/0378-1119(84)90013-1;
RA Ivanov V.N., Kershulite D.R., Bayev A.A., Akhundova A.A., Sulimova G.E.,
RA Judinkova E.S., Gorodetsky S.I.;
RT "Identification of bacterial clones encoding bovine caseins by direct
RT immunological screening of the cDNA library.";
RL Gene 32:381-388(1984).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-95.
RX PubMed=3900695;
RA Ivanov V.N., Kershulite D.R., Bayev A.A., Akhundova A.A., Silimova G.E.;
RT "Identification of bacterial clones that encode cow's caseins by direct
RT immunological screening of the cDNA library.";
RL Mol. Biol. (Mosk.) 19:955-963(1985).
RN [19]
RP PROTEIN SEQUENCE OF 74-108, VARIANT LEU-108, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17720176; DOI=10.1016/j.chroma.2007.08.015;
RA Schmelzer C.E.H., Schoeps R., Reynell L., Ulbrich-Hofmann R.,
RA Neubert R.H.H., Raith K.;
RT "Peptic digestion of beta-casein: Time course and fate of possible
RT bioactive peptides.";
RL J. Chromatogr. A 1166:108-115(2007).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-143, AND VARIANT LEU-108.
RA Jann O., Ceriotti G., Caroli A., Erhardt G.;
RT "A new variant in exon VII of bovine beta-casein gene (CSN2) and its
RT contribution among European cattle breeds.";
RL J. Anim. Breed. Genet. 119:65-68(2002).
RN [21]
RP PROTEIN SEQUENCE OF 113-120, FUNCTION, AND MASS SPECTROMETRY.
RA Gupta A., Mann B., Kumar Bajaj R., Sangwan R.B.;
RT "Studies on antioxidative peptides generated in cheddar cheese.";
RL Submitted (JAN-2008) to UniProtKB.
RN [22]
RP PROTEIN SEQUENCE OF 118-124, AND VARIANT A3 GLN-121.
RX PubMed=4997616;
RA Ribadeau-Dumas B., Grosclaude F., Mercier J.-C.;
RT "Localization in the peptide chain of bovine beta casein of the His-Gln
RT substitution differentiating the A2 and A3 genetic variants.";
RL C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 270:2369-2372(1970).
RN [23]
RP PROTEIN SEQUENCE OF 125-195 (VARIANTS A1 AND G).
RX AGRICOLA=IND22004684; DOI=10.1016/S0958-6946(99)00019-9;
RA Dong C., Ng-Kwai-Hang K.F.;
RT "Characterization of a non-electrophoretic genetic variant of beta-casein
RT by peptide mapping and mass spectrometric analysis.";
RL Int. Dairy J. 8:967-972(1998).
RN [24]
RP PROTEIN SEQUENCE OF 129-136, FUNCTION, AND VARIANT GLN-132.
RX PubMed=7600458; DOI=10.1139/y95-012;
RA Lebrun I., Lebrun F.L.A.S., Henriques O.B., Carmona A.K., Juliano L.,
RA Camargo A.C.M.;
RT "Isolation and characterization of a new bradykinin potentiating
RT octapeptide from gamma-casein.";
RL Can. J. Physiol. Pharmacol. 73:85-91(1995).
RN [25]
RP PROTEIN SEQUENCE OF 129-136, AND FUNCTION.
RX PubMed=14714726; DOI=10.1023/b:jopc.0000008724.98339.ff;
RA Perpetuo E.A., Juliano L., Lebrun I.;
RT "Biochemical and pharmacological aspects of two bradykinin-potentiating
RT peptides obtained from tryptic hydrolysis of casein.";
RL J. Protein Chem. 22:601-606(2003).
RN [26]
RP PROTEIN SEQUENCE OF 160-171 (VARIANT F).
RX PubMed=7496485; DOI=10.1016/0021-9673(95)00058-u;
RA Visser S., Slangen C.J., Lagerwerf F.M., Van Dongen W.D., Haverkamp J.;
RT "Identification of a new genetic variant of bovine beta-casein using
RT reversed-phase high-performance liquid chromatography and mass
RT spectrometric analysis.";
RL J. Chromatogr. A 711:141-150(1995).
RN [27]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-184.
RX PubMed=6897774; DOI=10.1089/dna.1982.1.375;
RA Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.;
RT "Construction and identification by partial nucleotide sequence analysis of
RT bovine casein and beta-lactoglobulin cDNA clones.";
RL DNA 1:375-386(1982).
RN [28]
RP PHOSPHORYLATION AT SER-30; SER-32; SER-33; SER-34 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16083266; DOI=10.1021/pr050113n;
RA Wu S.L., Kim J., Hancock W.S., Karger B.;
RT "Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS
RT platform for high sequence coverage of complex proteins with extensive
RT post-translational modifications-comprehensive analysis of beta-casein and
RT epidermal growth factor receptor (EGFR).";
RL J. Proteome Res. 4:1155-1170(2005).
RN [29]
RP PHOSPHORYLATION AT SER-30; SER-32; SER-33; SER-34 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17510049; DOI=10.1074/mcp.m600480-mcp200;
RA Imanishi S.Y., Kochin V., Ferraris S.E., de Thonel A., Pallari H.M.,
RA Corthals G.L., Eriksson J.E.;
RT "Reference-facilitated phosphoproteomics: fast and reliable phosphopeptide
RT validation by micro LC-ESI-Q-TOF MS/MS.";
RL Mol. Cell. Proteomics 6:1380-1391(2007).
RN [30]
RP VARIANTS A1; B AND C.
RX PubMed=5064450; DOI=10.1111/j.1432-1033.1972.tb01771.x;
RA Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.;
RT "Characterization of genetic variants of alpha-S1 and beta bovine
RT caseins.";
RL Eur. J. Biochem. 26:328-337(1972).
CC -!- FUNCTION: Important role in determination of the surface properties of
CC the casein micelles.
CC -!- FUNCTION: Casoparan acts as a macrophage activator, increasing the
CC phagocytic activity of macrophages and peroxide release from
CC macrophages. It also acts as a bradykinin-potentiating peptide.
CC -!- FUNCTION: Casohypotensin acts as a bradykinin-potentiating peptide.
CC Induces hypotension in rats. Acts as a strong competitive inhibitor of
CC endo-oligopeptidase A.
CC -!- FUNCTION: Antioxidant peptide has antioxidant activity.
CC -!- INTERACTION:
CC P02666; P0C0V0: degP; Xeno; NbExp=9; IntAct=EBI-5260183, EBI-547165;
CC P02666; Q8IXL6: FAM20C; Xeno; NbExp=3; IntAct=EBI-5260183, EBI-7147442;
CC P02666; O43464: HTRA2; Xeno; NbExp=7; IntAct=EBI-5260183, EBI-517086;
CC P02666; PRO_0000026946 [O43464]: HTRA2; Xeno; NbExp=2; IntAct=EBI-5260183, EBI-5271862;
CC P02666; P83110: HTRA3; Xeno; NbExp=8; IntAct=EBI-5260183, EBI-2867394;
CC P02666; P83105: HTRA4; Xeno; NbExp=5; IntAct=EBI-5260183, EBI-21776319;
CC P02666; P36776: LONP1; Xeno; NbExp=6; IntAct=EBI-5260183, EBI-357448;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- MASS SPECTROMETRY: [Antioxidant peptide]: Mass=872.51;
CC Method=Electrospray; Evidence={ECO:0000269|Ref.21};
CC -!- POLYMORPHISM: Leu-152 is present in the variants F and G; Gln-190 and
CC Glu-210 are present in the variant H. The sequence shown is the A2
CC variant.
CC -!- SIMILARITY: Belongs to the beta-casein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW84270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAW84271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABL74247.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion and
CC glue - Issue 16 of November 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/016";
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DR EMBL; M15132; AAA30430.1; -; mRNA.
DR EMBL; X06359; CAA29658.1; -; mRNA.
DR EMBL; M16645; AAA30480.1; -; mRNA.
DR EMBL; M55158; AAA30431.1; -; Genomic_DNA.
DR EMBL; S67277; AAB29137.1; -; mRNA.
DR EMBL; BC111172; AAI11173.1; -; mRNA.
DR EMBL; AY899917; AAW84270.1; ALT_INIT; mRNA.
DR EMBL; AY899918; AAW84271.1; ALT_INIT; mRNA.
DR EMBL; AH007287; AAD09813.1; -; Genomic_DNA.
DR EMBL; EF123100; ABL74247.1; ALT_FRAME; Genomic_DNA.
DR EMBL; EF628290; ABR10906.1; -; Genomic_DNA.
DR EMBL; AJ296330; CAC37028.1; -; Genomic_DNA.
DR EMBL; M64756; AAB59254.1; -; mRNA.
DR EMBL; AY366419; AAR14677.1; -; Genomic_DNA.
DR EMBL; K01087; AAA30481.1; -; mRNA.
DR PIR; A59068; A59068.
DR PIR; I45873; KBBOA2.
DR AlphaFoldDB; P02666; -.
DR DIP; DIP-46257N; -.
DR IntAct; P02666; 7.
DR MINT; P02666; -.
DR STRING; 9913.ENSBTAP00000003409; -.
DR BindingDB; P02666; -.
DR ChEMBL; CHEMBL3313833; -.
DR Allergome; 10199; Bos d 11.0101.
DR Allergome; 167; Bos d 8.
DR Allergome; 2736; Bos d 11.
DR iPTMnet; P02666; -.
DR PaxDb; P02666; -.
DR PeptideAtlas; P02666; -.
DR PRIDE; P02666; -.
DR eggNOG; ENOG502RU0R; Eukaryota.
DR HOGENOM; CLU_106775_0_0_1; -.
DR InParanoid; P02666; -.
DR OrthoDB; 1336883at2759; -.
DR TreeFam; TF336929; -.
DR PRO; PR:P02666; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
DR GO; GO:0005796; C:Golgi lumen; IDA:AgBase.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
DR GO; GO:1903720; P:negative regulation of I-kappaB phosphorylation; IDA:CAFA.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:CAFA.
DR GO; GO:1903488; P:negative regulation of lactation; IDA:AgBase.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:CAFA.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
DR GO; GO:1903494; P:response to dehydroepiandrosterone; IDA:AgBase.
DR GO; GO:0032355; P:response to estradiol; IDA:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR DisProt; DP00329; -.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR016345; Casein_beta.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR11500; PTHR11500; 1.
DR Pfam; PF00363; Casein; 1.
DR PIRSF; PIRSF002372; Beta-casein; 1.
DR PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Direct protein sequencing; Hypotensive agent;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Milk protein;
KW Phosphoprotein; Protease inhibitor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:10690361,
FT ECO:0000269|PubMed:3278933, ECO:0000269|PubMed:4557764"
FT CHAIN 16..224
FT /note="Beta-casein"
FT /id="PRO_0000004470"
FT PEPTIDE 41..45
FT /note="Casoparan"
FT /id="PRO_0000292031"
FT PEPTIDE 113..120
FT /note="Antioxidant peptide"
FT /id="PRO_0000320153"
FT PEPTIDE 129..136
FT /note="Casohypotensin"
FT /id="PRO_0000308464"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:17510049, ECO:0000269|PubMed:4557764"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:17510049, ECO:0000269|PubMed:4557764"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:17510049, ECO:0000269|PubMed:4557764"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:17510049, ECO:0000269|PubMed:4557764"
FT MOD_RES 50
FT /note="Phosphoserine; in variant A1, variant A2, variant
FT A3, variant B, variant E, variant F, variant G and variant
FT H"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:17510049"
FT VARIANT 33
FT /note="S -> K (in variant D)"
FT /evidence="ECO:0000269|PubMed:10690361"
FT VARIANT 40
FT /note="R -> C (in variant H)"
FT VARIANT 51
FT /note="E -> K (in variant E)"
FT /evidence="ECO:0000269|PubMed:4411121"
FT VARIANT 52
FT /note="E -> K (in variant C)"
FT VARIANT 82
FT /note="P -> H (in variants A1, B, C, F and G)"
FT /evidence="ECO:0000269|PubMed:3271384, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.6"
FT VARIANT 103
FT /note="L -> I (in variant H)"
FT VARIANT 108
FT /note="M -> L"
FT /evidence="ECO:0000269|PubMed:17720176,
FT ECO:0000269|PubMed:3814153, ECO:0000269|PubMed:4557764,
FT ECO:0000269|Ref.20"
FT VARIANT 121
FT /note="H -> Q (in variant A3)"
FT /evidence="ECO:0000269|PubMed:4997616,
FT ECO:0000269|PubMed:8248100"
FT VARIANT 132
FT /note="E -> Q (in variants A1 and G)"
FT /evidence="ECO:0000269|PubMed:1804413,
FT ECO:0000269|PubMed:7600458"
FT VARIANT 137
FT /note="S -> R (in variant B)"
FT /evidence="ECO:0000269|Ref.6"
FT VARIANT 152
FT /note="L -> P (in variants A1 and H)"
FT /evidence="ECO:0000269|PubMed:3814153"
FT VARIANT 153
FT /note="P -> L (in variants A1, G and H)"
FT /evidence="ECO:0000269|PubMed:3814153"
FT VARIANT 167
FT /note="P -> L (in variant F)"
FT VARIANT 190
FT /note="Q -> E (in variants A1 and G)"
FT CONFLICT 50
FT /note="S -> Z (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Q -> R (in Ref. 14; ABL74247)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> R (in Ref. 14; ABL74247)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Y -> V (in Ref. 16; CAC37028)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="QE -> EQ (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="E -> Q (in Ref. 1; AAA30430 and 8; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="V -> A (in Ref. 15; ABR10906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25107 MW; F0BBDD8148A238AE CRC64;
MKVLILACLV ALALARELEE LNVPGEIVES LSSSEESITR INKKIEKFQS EEQQQTEDEL
QDKIHPFAQT QSLVYPFPGP IPNSLPQNIP PLTQTPVVVP PFLQPEVMGV SKVKEAMAPK
HKEMPFPKYP VEPFTESQSL TLTDVENLHL PLPLLQSWMH QPHQPLPPTV MFPPQSVLSL
SQSKVLPVPQ KAVPYPQRDM PIQAFLLYQE PVLGPVRGPF PIIV
