CASA2_BOVIN
ID CASA2_BOVIN Reviewed; 222 AA.
AC P02663; Q1RMQ6; Q9TR51;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alpha-S2-casein;
DE Contains:
DE RecName: Full=Casocidin-1;
DE AltName: Full=Casocidin-I;
DE Flags: Precursor;
GN Name=CSN1S2;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 16-222 (A ALLELE).
RC TISSUE=Milk;
RX PubMed=862906; DOI=10.1016/0014-5793(77)80167-1;
RA Brignon G., Ribadeau-Dumas B., Mercier J.-C., Pelissier J.-P., Das B.C.;
RT "Complete amino acid sequence of bovine alphaS2-casein.";
RL FEBS Lett. 76:274-279(1977).
RN [4]
RP PARTIAL PROTEIN SEQUENCE (D ALLELE).
RC TISSUE=Milk;
RX PubMed=469044; DOI=10.1017/s0022029900017052;
RA Grosclaude F., Joudrier P., Mahe M.-F.;
RT "A genetic and biochemical analysis of a polymorphism of bovine alpha S2-
RT casein.";
RL J. Dairy Res. 46:211-213(1979).
RN [5]
RP PROTEIN SEQUENCE OF 165-203, CHARACTERIZATION OF CASOCIDIN, AND MASS
RP SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=7556666; DOI=10.1016/0014-5793(95)00974-e;
RA Zucht H.-D., Raida M., Adermann K., Meagert H.-J., Forssmann W.-G.;
RT "Casocidin-I: a casein-alpha s2 derived peptide exhibits antibacterial
RT activity.";
RL FEBS Lett. 372:185-188(1995).
RN [6]
RP PHOSPHORYLATION AT SER-46 AND SER-158.
RA Bai F., Liu S., Witzmann F.A.;
RL Submitted (SEP-2005) to UniProtKB.
RN [7]
RP PHOSPHORYLATION AT SER-23; SER-24; SER-25; SER-28; SER-71; SER-72; SER-73;
RP SER-76 AND SER-158, AND 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).
CC -!- FUNCTION: Important role in the capacity of milk to transport calcium
CC phosphate.
CC -!- FUNCTION: Casocidin-I inhibits the growth of E.coli and S.carnosus.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- MASS SPECTROMETRY: [Casocidin-1]: Mass=4870; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7556666};
CC -!- POLYMORPHISM: At least two alleles exist. The sequence of the A allele
CC is shown here. The D allele sequence differs from that shown in having
CC a deletion of nine residues, which may be 49-58, 50-59, or 51-60.
CC -!- SIMILARITY: Belongs to the alpha-casein family. {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; M16644; AAA30479.1; -; mRNA.
DR EMBL; BC114773; AAI14774.1; -; mRNA.
DR PIR; JQ2008; KABOS2.
DR RefSeq; NP_776953.1; NM_174528.2.
DR PDB; 6FS4; NMR; -; A=166-196.
DR PDB; 6FS5; NMR; -; A=165-203.
DR PDBsum; 6FS4; -.
DR PDBsum; 6FS5; -.
DR AlphaFoldDB; P02663; -.
DR SMR; P02663; -.
DR STRING; 9913.ENSBTAP00000006590; -.
DR Allergome; 10198; Bos d 10.0101.
DR Allergome; 167; Bos d 8.
DR Allergome; 2735; Bos d 10.
DR CarbonylDB; P02663; -.
DR iPTMnet; P02663; -.
DR PaxDb; P02663; -.
DR PeptideAtlas; P02663; -.
DR PRIDE; P02663; -.
DR Ensembl; ENSBTAT00000006590; ENSBTAP00000006590; ENSBTAG00000005005.
DR GeneID; 282209; -.
DR KEGG; bta:282209; -.
DR CTD; 100327035; -.
DR VEuPathDB; HostDB:ENSBTAG00000005005; -.
DR eggNOG; ENOG502TDWX; Eukaryota.
DR GeneTree; ENSGT00940000164399; -.
DR HOGENOM; CLU_121717_0_0_1; -.
DR InParanoid; P02663; -.
DR OMA; VMNPWDQ; -.
DR OrthoDB; 1489083at2759; -.
DR TreeFam; TF339561; -.
DR PRO; PR:P02663; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000005005; Expressed in milk and 29 other tissues.
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:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0035375; F:zymogen binding; IPI:AgBase.
DR GO; GO:0042742; P:defense response to bacterium; 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:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR InterPro; IPR011175; Alpha-s2_casein.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR16656; PTHR16656; 1.
DR Pfam; PF00363; Casein; 1.
DR PIRSF; PIRSF002371; Alpha-s2-casein; 1.
DR PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Milk protein; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:862906"
FT CHAIN 16..222
FT /note="Alpha-S2-casein"
FT /id="PRO_0000004460"
FT PEPTIDE 165..203
FT /note="Casocidin-1"
FT /id="PRO_0000004461"
FT REPEAT 76..140
FT REPEAT 158..222
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O97944"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O97944"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O97944"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17510049, ECO:0000269|Ref.6"
FT CONFLICT 42
FT /note="A -> D (in Ref. 2; AAI14774)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="Q -> R (in Ref. 2; AAI14774)"
FT /evidence="ECO:0000305"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:6FS4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6FS4"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:6FS5"
SQ SEQUENCE 222 AA; 26019 MW; 81E7408AF1C12F7C CRC64;
MKFFIFTCLL AVALAKNTME HVSSSEESII SQETYKQEKN MAINPSKENL CSTFCKEVVR
NANEEEYSIG SSSEESAEVA TEEVKITVDD KHYQKALNEI NQFYQKFPQY LQYLYQGPIV
LNPWDQVKRN AVPITPTLNR EQLSTSEENS KKTVDMESTE VFTKKTKLTE EEKNRLNFLK
KISQRYQKFA LPQYLKTVYQ HQKAMKPWIQ PKTKVIPYVR YL
