CASA2_EQUAS
ID CASA2_EQUAS Reviewed; 236 AA.
AC B7VGF9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Alpha-S2-casein {ECO:0000312|EMBL:CAV00691.1};
DE Flags: Precursor;
GN Name=CSN1S2 {ECO:0000312|EMBL:CAV00691.1};
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAV00691.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland {ECO:0000312|EMBL:CAV00691.1};
RA Ramunno L.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 16-236, MASS SPECTROMETRY, VARIANT A1 191-ASN--GLN-195
RP DEL, VARIANTS A1D 27-ASP--GLU-57 DEL AND 191-ASN--GLN-195 DEL, VARIANT A2
RP 227-TYR--LEU-233 DEL, AND VARIANTS A2D 27-ASP--GLU-57 DEL AND
RP 227-TYR--LEU-233 DEL.
RC STRAIN=Ragusana; TISSUE=Milk;
RX PubMed=22972783; DOI=10.1002/jms.3031;
RA Saletti R., Muccilli V., Cunsolo V., Fontanini D., Capocchi A., Foti S.;
RT "MS-based characterization of alpha(s2)-casein isoforms in donkey's milk.";
RL J. Mass Spectrom. 47:1150-1159(2012).
RN [3] {ECO:0000305}
RP PHOSPHORYLATION, AND MASS SPECTROMETRY.
RX PubMed=20541767; DOI=10.1016/j.chroma.2010.05.017;
RA Chianese L., Calabrese M.G., Ferranti P., Mauriello R., Garro G.,
RA De Simone C., Quarto M., Addeo F., Cosenza G., Ramunno L.;
RT "Proteomic characterization of donkey milk 'caseome'.";
RL J. Chromatogr. A 1217:4834-4840(2010).
CC -!- FUNCTION: Important role in the capacity of milk to transport calcium
CC phosphate. {ECO:0000250|UniProtKB:P02663}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- PTM: There are at least three different forms found in milk, with
CC varying degrees of phosphorylation. These include form 10-P which is
CC phosphorylated at ten sites that have not been determined, form 11-P
CC which is phosphorylated at eleven sites and form 12-P which is
CC phosphorylated at twelve sites. {ECO:0000269|PubMed:20541767}.
CC -!- MASS SPECTROMETRY: Mass=26029; Method=MALDI; Note=Variant A and
CC dephosphorylated.; Evidence={ECO:0000269|PubMed:20541767};
CC -!- MASS SPECTROMETRY: Mass=26829; Method=MALDI; Note=Form 10-P.;
CC Evidence={ECO:0000269|PubMed:20541767};
CC -!- MASS SPECTROMETRY: Mass=26909; Method=MALDI; Note=Form 11-P.;
CC Evidence={ECO:0000269|PubMed:20541767};
CC -!- MASS SPECTROMETRY: Mass=26989; Method=MALDI; Note=Form 12-P.;
CC Evidence={ECO:0000269|PubMed:20541767};
CC -!- MASS SPECTROMETRY: Mass=25429; Method=MALDI; Note=Variant A1.;
CC Evidence={ECO:0000269|PubMed:22972783};
CC -!- MASS SPECTROMETRY: Mass=21939; Method=MALDI; Note=Variant A1d.;
CC Evidence={ECO:0000269|PubMed:22972783};
CC -!- MASS SPECTROMETRY: Mass=25203; Method=MALDI; Note=Variant A2.;
CC Evidence={ECO:0000269|PubMed:22972783};
CC -!- MASS SPECTROMETRY: Mass=21713; Method=MALDI; Note=Variant A2d.;
CC Evidence={ECO:0000269|PubMed:22972783};
CC -!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000255}.
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DR EMBL; FM946022; CAV00691.1; -; mRNA.
DR RefSeq; XP_014702742.1; XM_014847256.1.
DR AlphaFoldDB; B7VGF9; -.
DR SMR; B7VGF9; -.
DR GeneID; 106835119; -.
DR OrthoDB; 1489083at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Direct protein sequencing; Milk protein; Phosphoprotein; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255, ECO:0000312|EMBL:CAV00691.1"
FT CHAIN 16..236
FT /note="Alpha-S2-casein"
FT /id="PRO_5000419614"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O97944"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02663"
FT VARIANT 27..57
FT /note="Missing (in A1d and A2d)"
FT /evidence="ECO:0000269|PubMed:22972783"
FT VARIANT 191..195
FT /note="Missing (in A1 and A1d)"
FT /evidence="ECO:0000269|PubMed:22972783"
FT VARIANT 227..233
FT /note="Missing (in A2 and A2d)"
FT /evidence="ECO:0000269|PubMed:22972783"
SQ SEQUENCE 236 AA; 27700 MW; 62BF95638612E22D CRC64;
MKFFIFTCLL AVALAKHNME HRSSSEDSVN ISQEKFKQEK YVVIPTSKES ICSTSCEEAT
RNINEMESAK FPTEVYSSSS SSEESAKFPT EREEKEVEEK HHLKQLNKIN QFYEKLNFLQ
YLQALRQPRI VLTPWDQTKT GASPFIPIVN TEQLFTSEEI PKKTVDMEST EVVTEKTELT
EEEKNYLKLL NKINQYYEKF TLPQYFKIVH QHQTTMDPQS HSKTNSYQII PVLRYF
