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 27-MAR-2024, entry version 188. 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"; 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; 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 RefSeq; XP_010804480.1; XM_010806178.1. DR PDB; 7TTR; EM; 2.96 A; P=1-224. DR PDB; 7TTS; EM; 2.90 A; P=1-224. DR PDBsum; 7TTR; -. DR PDBsum; 7TTS; -. DR AlphaFoldDB; P02666; -. DR PCDDB; P02666; -. DR SMR; 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; 9913-ENSBTAP00000003409; -. DR PeptideAtlas; P02666; -. DR GeneID; 281099; -. DR eggNOG; ENOG502RU0R; Eukaryota. DR HOGENOM; CLU_106775_0_0_1; -. DR InParanoid; P02666; -. DR TreeFam; TF336929; -. DR PRO; PR:P02666; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005615; C:extracellular space; IDA:CAFA. 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:0043167; F:ion binding; EXP:DisProt. DR GO; GO:0046872; F:metal ion binding; EXP:DisProt. 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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IDA:CAFA. DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; 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; BETA CASEIN; 1. DR PANTHER; PTHR11500:SF0; BETA-CASEIN; 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 3D-structure; 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 //