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Alpha-S2-casein [Cleaved into: Casocidin-1 (Casocidin-I)]

 CASA2_BOVIN             Reviewed;         222 AA.
P02663; Q1RMQ6; Q9TR51;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
28-FEB-2018, entry version 135.
RecName: Full=Alpha-S2-casein;
Contains:
RecName: Full=Casocidin-1;
AltName: Full=Casocidin-I;
Flags: Precursor;
Name=CSN1S2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2833669;
Stewart A.F., Bonsing J., Beattie C.W., Shah F., Willis I.M.,
Mackinlay A.G.;
"Complete nucleotide sequences of bovine alpha S2- and beta-casein
cDNAs: comparisons with related sequences in other species.";
Mol. Biol. Evol. 4:231-241(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 16-222 (A ALLELE).
TISSUE=Milk;
PubMed=862906; DOI=10.1016/0014-5793(77)80167-1;
Brignon G., Ribadeau-Dumas B., Mercier J.-C., Pelissier J.-P.,
Das B.C.;
"Complete amino acid sequence of bovine alphaS2-casein.";
FEBS Lett. 76:274-279(1977).
[4]
PARTIAL PROTEIN SEQUENCE (D ALLELE).
TISSUE=Milk;
PubMed=469044;
Grosclaude F., Joudrier P., Mahe M.-F.;
"A genetic and biochemical analysis of a polymorphism of bovine alpha
S2-casein.";
J. Dairy Res. 46:211-213(1979).
[5]
PROTEIN SEQUENCE OF 165-203, CHARACTERIZATION OF CASOCIDIN, AND MASS
SPECTROMETRY.
TISSUE=Milk;
PubMed=7556666; DOI=10.1016/0014-5793(95)00974-E;
Zucht H.-D., Raida M., Adermann K., Meagert H.-J., Forssmann W.-G.;
"Casocidin-I: a casein-alpha s2 derived peptide exhibits antibacterial
activity.";
FEBS Lett. 372:185-188(1995).
[6]
PHOSPHORYLATION AT SER-46 AND SER-158.
Bai F., Liu S., Witzmann F.A.;
Submitted (SEP-2005) to UniProtKB.
[7]
PHOSPHORYLATION AT SER-23; SER-24; SER-25; SER-28; SER-71; SER-72;
SER-73; SER-76 AND SER-158, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17510049; DOI=10.1074/mcp.M600480-MCP200;
Imanishi S.Y., Kochin V., Ferraris S.E., de Thonel A., Pallari H.M.,
Corthals G.L., Eriksson J.E.;
"Reference-facilitated phosphoproteomics: fast and reliable
phosphopeptide validation by micro LC-ESI-Q-TOF MS/MS.";
Mol. Cell. Proteomics 6:1380-1391(2007).
-!- FUNCTION: Important role in the capacity of milk to transport
calcium phosphate.
-!- FUNCTION: Casocidin-I inhibits the growth of E.coli and
S.carnosus.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
-!- MASS SPECTROMETRY: Mass=4870; Method=Electrospray; Range=165-203;
Evidence={ECO:0000269|PubMed:7556666};
-!- POLYMORPHISM: At least two alleles exist. The sequence of the A
allele is shown here. The D allele sequence differs from that
shown in having a deletion of nine residues, which may be 49-58,
50-59, or 51-60.
-!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion
and glue - Issue 16 of November 2001;
URL="https://web.expasy.org/spotlight/back_issues/016";
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EMBL; M16644; AAA30479.1; -; mRNA.
EMBL; BC114773; AAI14774.1; -; mRNA.
PIR; JQ2008; KABOS2.
RefSeq; NP_776953.1; NM_174528.2.
UniGene; Bt.57616; -.
ProteinModelPortal; P02663; -.
STRING; 9913.ENSBTAP00000006590; -.
Allergome; 10198; Bos d 10.0101.
Allergome; 167; Bos d 8.
Allergome; 2735; Bos d 10.
CarbonylDB; P02663; -.
iPTMnet; P02663; -.
PaxDb; P02663; -.
PeptideAtlas; P02663; -.
PRIDE; P02663; -.
Ensembl; ENSBTAT00000006590; ENSBTAP00000006590; ENSBTAG00000005005.
GeneID; 282209; -.
KEGG; bta:282209; -.
CTD; 100327035; -.
eggNOG; ENOG410JE87; Eukaryota.
eggNOG; ENOG4111369; LUCA.
GeneTree; ENSGT00530000065240; -.
HOGENOM; HOG000111307; -.
HOVERGEN; HBG005244; -.
InParanoid; P02663; -.
OMA; VMNPWDQ; -.
OrthoDB; EOG091G0QMQ; -.
TreeFam; TF339561; -.
PMAP-CutDB; P02663; -.
PRO; PR:P02663; -.
Proteomes; UP000009136; Chromosome 6.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
GO; GO:0005796; C:Golgi lumen; IDA:AgBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
GO; GO:0035375; F:zymogen binding; IPI:AgBase.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
GO; GO:1903494; P:response to dehydroepiandrosterone; IDA:AgBase.
GO; GO:0032355; P:response to estradiol; IDA:AgBase.
GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
GO; GO:0032570; P:response to progesterone; IDA:AgBase.
InterPro; IPR011175; Alpha-s2_casein.
InterPro; IPR001588; Casein.
InterPro; IPR031305; Casein_CS.
PANTHER; PTHR16656; PTHR16656; 1.
Pfam; PF00363; Casein; 2.
PIRSF; PIRSF002371; Alpha-s2-casein; 1.
PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Milk protein; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 15 {ECO:0000269|PubMed:862906}.
CHAIN 16 222 Alpha-S2-casein.
/FTId=PRO_0000004460.
PEPTIDE 165 203 Casocidin-1.
/FTId=PRO_0000004461.
REPEAT 76 140
REPEAT 158 222
MOD_RES 23 23 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 46 46 Phosphoserine. {ECO:0000269|Ref.6}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000269|PubMed:17510049}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000250|UniProtKB:O97944}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:O97944}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:O97944}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000269|PubMed:17510049,
ECO:0000269|Ref.6}.
CONFLICT 42 42 A -> D (in Ref. 2; AAI14774).
{ECO:0000305}.
CONFLICT 102 102 Q -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 Q -> R (in Ref. 2; AAI14774).
{ECO:0000305}.
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


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