CASA1_BOVIN
ID CASA1_BOVIN Reviewed; 214 AA.
AC P02662; A5YK80; A8WCP1; A8WCP2; A8WCP3; A8WCP4; A8WCP5; A8WCP6; A8WCP7;
AC A8WCP8; A8WCP9; A8WCQ0; A8WCQ1; A8WCQ2; A8WCQ3; A8WCQ4; A8WCQ5; A8WCQ6;
AC A8WCQ7; A8WCQ8; A8WCQ9; A8WCR0; A8WCR1; A8WCR2; A8WCR3; A8WCR4; A8WCR5;
AC A8WCR6; A8WCR7; A8WCR8; A8WCR9; A8WCS0; A8WCS1; Q28048; Q28069; Q32LE8;
AC Q7M2U6; Q9TRH5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Alpha-S1-casein;
DE AltName: Allergen=Bos d 8;
DE Contains:
DE RecName: Full=Antioxidant peptide;
DE Flags: Precursor;
GN Name=CSN1S1;
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].
RX PubMed=6328443; DOI=10.1093/nar/12.9.3895;
RA Stewart A.F., Willis I.M., Mackinlay A.G.;
RT "Nucleotide sequences of bovine alpha S1- and kappa-casein cDNAs.";
RL Nucleic Acids Res. 12:3895-3907(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagao M., Maki M., Sasaki R., Chiba R.;
RT "Isolation and sequence analysis of bovine alpha-S1-casein cDNA clone.";
RL Agric. Biol. Chem. 48:1663-1667(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=3022833;
RA Gorodetskii S.I., Zakhar'ev V.M., Kyarshulite D.R., Kapelinskaya T.V.,
RA Skryabin K.G.;
RT "cDNA of cattle alpha S1-casein: cloning and nucleotide sequence.";
RL Biokhimiia 51:1641-1648(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1658736; DOI=10.1093/nar/19.20.5591;
RA Koczan D., Hobom G., Seyfert H.-M.;
RT "Genomic organization of the bovine alpha-S1 casein gene.";
RL Nucleic Acids Res. 19:5591-5596(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALLERGEN.
RX PubMed=19454699; DOI=10.4049/jimmunol.0712366;
RA Schulmeister U., Hochwallner H., Swoboda I., Focke-Tejkl M., Geller B.,
RA Nystrand M., Harlin A., Thalhamer J., Scheiblhofer S., Keller W.,
RA Niggemann B., Quirce S., Ebner C., Mari A., Pauli G., Herz U., Valenta R.,
RA Spitzauer S.;
RT "Cloning, expression, and mapping of allergenic determinants of alphaS1-
RT casein, a major cow's milk allergen.";
RL J. Immunol. 182:7019-7029(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 16-214 (VARIANT B).
RX PubMed=4331376; DOI=10.1111/j.1432-1033.1971.tb01590.x;
RA Mercier J.-C., Grosclaude F., Ribadeau-Dumas B.;
RT "Primary structure of bovine alpha-s1 casein. Complete sequence.";
RL Eur. J. Biochem. 23:41-51(1971).
RN [8]
RP SEQUENCE REVISION TO 74 AND 92-93 (VARIANTS A; B; C AND D).
RX PubMed=4797901; DOI=10.1111/j.1432-1033.1973.tb03199.x;
RA Mercier J.-C., Grosclaude F., Ribadeau-Dumas B.;
RT "Primary structure of alpha casein and of bovine beta casein. Correction.";
RL Eur. J. Biochem. 40:323-323(1973).
RN [9]
RP PROTEIN SEQUENCE OF 16-214 (VARIANT D).
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).
RN [10]
RP PROTEIN SEQUENCE OF 23-49 (VARIANT A).
RX PubMed=11945462; DOI=10.1016/0014-5793(70)80504-x;
RA Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.;
RT "Localization in the N-terminal part of bovine casein alpha-s1 of a 13
RT amino-acid deletion that differentiates variant A from variants B and C.";
RL FEBS Lett. 11:109-112(1970).
RN [11]
RP PROTEIN SEQUENCE OF 39-55.
RC TISSUE=Mammary gland;
RX PubMed=1299613; DOI=10.1016/0014-5793(92)80664-3;
RA Neuteboom B., Giuffrida M.G., Conti A.;
RT "Isolation of a new ligand-carrying casein fragment from bovine mammary
RT gland microsomes.";
RL FEBS Lett. 305:189-191(1992).
RN [12]
RP PROTEIN SEQUENCE OF 39-47 AND 166-188.
RX PubMed=8841384; DOI=10.1016/0167-4838(96)00103-3;
RA Ramalho-Santos M., Verissimo P., Faro C., Pires E.;
RT "Action on bovine alpha s1-casein of cardosins A and B, aspartic
RT proteinases from the flowers of the cardoon Cynara cardunculus L.";
RL Biochim. Biophys. Acta 1297:83-89(1996).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-130.
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 [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-110.
RA Shahla M.N., Farooq M.S., Naeem M.K., Riazuddin S.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP PROTEIN SEQUENCE OF 95-105, AND FUNCTION.
RA Gupta A., Mann B., Kumar R., Sangwan R.B.;
RT "Antioxidant peptides isolated from cheddar cheese made with adjunct
RT culture L.casei ssp. casei 300.";
RL Submitted (MAR-2008) to UniProtKB.
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-214.
RX PubMed=3838718;
RA Kiarshulite D.R., Zakhar'ev V.M., Gorodetskii S.I.;
RT "Nucleotide sequence of the 3'-nontranslated region of the mRNA of alpha
RT S1-casein in cows.";
RL Dokl. Akad. Nauk SSSR 280:1433-1437(1985).
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-214.
RX PubMed=1343827;
RA Chen R., Wang B., Zhang Y., Liu W., Zhang J., Lao W.;
RT "Cloning, mapping, and sequencing of 3' and its flanking region of bovine
RT alpha-s1 casein gene.";
RL Chin. J. Biotechnol. 8:235-245(1992).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 185-202.
RC TISSUE=Mammary gland;
RA Maki M., Nagao M., Hirose M., Chiba H.;
RT "Cloning of cDNA sequence coding for bovine alpha-s1-casein.";
RL Agric. Biol. Chem. 47:441-444(1983).
RN [19]
RP PROTEIN SEQUENCE OF 205-214 (VARIANT C).
RA Grosclaude F., Mercier J.-C., Ribadeau-Dumas B.;
RT "On the localization in the C-terminal sequence of bovine casein alpha-s1
RT of a Glu/Gly substitution that differentiates the genetic variants B and
RT C.";
RL C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 268:3133-3136(1970).
RN [20]
RP ALLERGEN.
RX PubMed=11174208; DOI=10.1067/mai.2001.112372;
RA Chatchatee P., Jaervinen K.M., Bardina L., Beyer K., Sampson H.A.;
RT "Identification of IgE- and IgG-binding epitopes on alpha(s1)-casein:
RT differences in patients with persistent and transient cow's milk allergy.";
RL J. Allergy Clin. Immunol. 107:379-383(2001).
RN [21]
RP PHOSPHORYLATION AT SER-56; SER-61; SER-63; SER-79; SER-81; SER-82; SER-83;
RP SER-90 AND SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15858219; DOI=10.1074/mcp.t500007-mcp200;
RA Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., Jorgensen T.J.;
RT "Highly selective enrichment of phosphorylated peptides from peptide
RT mixtures using titanium dioxide microcolumns.";
RL Mol. Cell. Proteomics 4:873-886(2005).
RN [22]
RP PHOSPHORYLATION AT SER-56.
RA Bai F., Liu S., Witzmann F.A.;
RL Submitted (SEP-2005) to UniProtKB.
CC -!- FUNCTION: Important role in the capacity of milk to transport calcium
CC phosphate. {ECO:0000269|Ref.15}.
CC -!- FUNCTION: Antioxidant peptide has 2,2-diphenyl-1-picrylhydrazyl (DPPH)
CC radical scavenging activity. {ECO:0000269|Ref.15}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- ALLERGEN: Causes an allergic reaction in human. Has six major and 3
CC minor IgE-binding regions and 5 major and 1 minor IgG-binding regions.
CC Is a cause of cow's milk allergy (CMA). {ECO:0000269|PubMed:11174208,
CC ECO:0000269|PubMed:19454699}.
CC -!- MISCELLANEOUS: The B variant sequence is shown.
CC -!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/CASA/";
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; X00564; CAB57792.1; -; mRNA.
DR EMBL; M33123; AAA30428.1; -; mRNA.
DR EMBL; M38641; AAA30429.1; -; mRNA.
DR EMBL; X59856; CAA42516.1; -; Genomic_DNA.
DR EMBL; EU221551; ABW98936.1; -; Genomic_DNA.
DR EMBL; EU221552; ABW98937.1; -; Genomic_DNA.
DR EMBL; EU221553; ABW98938.1; -; Genomic_DNA.
DR EMBL; EU221554; ABW98939.1; -; Genomic_DNA.
DR EMBL; EU221555; ABW98940.1; -; Genomic_DNA.
DR EMBL; EU221556; ABW98941.1; -; Genomic_DNA.
DR EMBL; EU221557; ABW98942.1; -; Genomic_DNA.
DR EMBL; EU221558; ABW98943.1; -; Genomic_DNA.
DR EMBL; EU221559; ABW98944.1; -; Genomic_DNA.
DR EMBL; EU221560; ABW98945.1; -; Genomic_DNA.
DR EMBL; EU221561; ABW98946.1; -; Genomic_DNA.
DR EMBL; EU221562; ABW98947.1; -; Genomic_DNA.
DR EMBL; EU221563; ABW98948.1; -; Genomic_DNA.
DR EMBL; EU221564; ABW98949.1; -; Genomic_DNA.
DR EMBL; EU221565; ABW98950.1; -; Genomic_DNA.
DR EMBL; EU221566; ABW98951.1; -; Genomic_DNA.
DR EMBL; EU221567; ABW98952.1; -; Genomic_DNA.
DR EMBL; EU221568; ABW98953.1; -; Genomic_DNA.
DR EMBL; EU221569; ABW98954.1; -; Genomic_DNA.
DR EMBL; EU221570; ABW98955.1; -; Genomic_DNA.
DR EMBL; EU221571; ABW98956.1; -; Genomic_DNA.
DR EMBL; EU221572; ABW98957.1; -; Genomic_DNA.
DR EMBL; EU221573; ABW98958.1; -; Genomic_DNA.
DR EMBL; EU221574; ABW98959.1; -; Genomic_DNA.
DR EMBL; EU221575; ABW98960.1; -; Genomic_DNA.
DR EMBL; EU221576; ABW98961.1; -; Genomic_DNA.
DR EMBL; EU221577; ABW98962.1; -; Genomic_DNA.
DR EMBL; EU221578; ABW98963.1; -; Genomic_DNA.
DR EMBL; EU221579; ABW98964.1; -; Genomic_DNA.
DR EMBL; EU221580; ABW98965.1; -; Genomic_DNA.
DR EMBL; EU221581; ABW98966.1; -; Genomic_DNA.
DR EMBL; BC109618; AAI09619.1; -; mRNA.
DR EMBL; K01084; AAA30478.1; -; mRNA.
DR EMBL; EF538766; ABQ88318.1; -; Genomic_DNA.
DR EMBL; M38658; AAA62707.1; -; mRNA.
DR EMBL; AH007360; AAD14099.1; -; Genomic_DNA.
DR EMBL; D00412; BAA00313.1; -; mRNA.
DR PIR; S22575; KABOSB.
DR PIR; S72220; S72220.
DR RefSeq; NP_851372.1; NM_181029.2.
DR AlphaFoldDB; P02662; -.
DR BioGRID; 159482; 3.
DR DIP; DIP-29917N; -.
DR IntAct; P02662; 3.
DR MINT; P02662; -.
DR STRING; 9913.ENSBTAP00000010119; -.
DR Allergome; 10197; Bos d 9.0101.
DR Allergome; 167; Bos d 8.
DR Allergome; 2734; Bos d 9.
DR CarbonylDB; P02662; -.
DR iPTMnet; P02662; -.
DR PaxDb; P02662; -.
DR PeptideAtlas; P02662; -.
DR PRIDE; P02662; -.
DR Ensembl; ENSBTAT00000010119; ENSBTAP00000010119; ENSBTAG00000007695.
DR Ensembl; ENSBTAT00000084279; ENSBTAP00000071217; ENSBTAG00000007695.
DR GeneID; 282208; -.
DR KEGG; bta:282208; -.
DR CTD; 1446; -.
DR VEuPathDB; HostDB:ENSBTAG00000007695; -.
DR VGNC; VGNC:27763; CSN1S1.
DR eggNOG; ENOG502TEWT; Eukaryota.
DR GeneTree; ENSGT00390000017378; -.
DR HOGENOM; CLU_126070_0_0_1; -.
DR InParanoid; P02662; -.
DR OMA; WYYPPQV; -.
DR OrthoDB; 1478191at2759; -.
DR TreeFam; TF340763; -.
DR PRO; PR:P02662; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000007695; Expressed in milk and 36 other tissues.
DR ExpressionAtlas; P02662; baseline.
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:0001540; F:amyloid-beta binding; IDA:CAFA.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:WormBase.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IDA:CAFA.
DR GO; GO:1903456; P:positive regulation of androst-4-ene-3,17-dione biosynthetic process; IMP:AgBase.
DR GO; GO:2000839; P:positive regulation of androstenedione secretion; IMP:AgBase.
DR GO; GO:2000184; P:positive regulation of progesterone biosynthetic process; IMP:AgBase.
DR GO; GO:2000872; P:positive regulation of progesterone secretion; IMP:AgBase.
DR GO; GO:0050821; P:protein stabilization; IDA:CAFA.
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:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR InterPro; IPR026999; Alpha-s1_casein.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR10240; PTHR10240; 1.
DR Pfam; PF00363; Casein; 1.
DR PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Allergen; Antioxidant; Direct protein sequencing; Milk protein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:4331376,
FT ECO:0000269|PubMed:5064450"
FT CHAIN 16..214
FT /note="Alpha-S1-casein"
FT /id="PRO_0000004446"
FT PEPTIDE 95..105
FT /note="Antioxidant peptide"
FT /id="PRO_0000331578"
FT REPEAT 85..99
FT REPEAT 125..140
FT REGION 195..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219, ECO:0000269|Ref.22"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15858219"
FT VARIANT 29..41
FT /note="Missing (in variant A)"
FT VARIANT 68
FT /note="A -> T (in variant D)"
FT VARIANT 207
FT /note="E -> G (in variant C)"
FT CONFLICT 11..12
FT /note="AV -> SA (in Ref. 5; ABW98943)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="P -> L (in Ref. 3; AAA30429)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="P -> S (in Ref. 5; ABW98945)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="H -> Q (in Ref. 13; AAA30478)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> D (in Ref. 14; ABQ88318)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="H -> D (in Ref. 3; AAA30429)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="L -> P (in Ref. 5; ABW98953)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="S -> L (in Ref. 16; AAA62707)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..212
FT /note="MP -> IS (in Ref. 3; AAA30429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24529 MW; F066B5C8AE55828B CRC64;
MKLLILTCLV AVALARPKHP IKHQGLPQEV LNENLLRFFV APFPEVFGKE KVNELSKDIG
SESTEDQAME DIKQMEAESI SSSEEIVPNS VEQKHIQKED VPSERYLGYL EQLLRLKKYK
VPQLEIVPNS AEERLHSMKE GIHAQQKEPM IGVNQELAYF YPELFRQFYQ LDAYPSGAWY
YVPLGTQYTD APSFSDIPNP IGSENSEKTT MPLW
