CASB_HORSE
ID CASB_HORSE Reviewed; 241 AA.
AC Q9GKK3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Beta-casein;
DE Flags: Precursor;
GN Name=CSN2 {ECO:0000250|UniProtKB:P39037};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG43954.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Warmblood {ECO:0000269|PubMed:12617390};
RC TISSUE=Lactating mammary gland {ECO:0000312|EMBL:AAG43954.1};
RX PubMed=12617390; DOI=10.1017/s002202990200599x;
RA Lenasi T., Rogelj I., Dovc P.;
RT "Characterization of equine cDNA sequences for alphaS1-, beta- and kappa-
RT casein.";
RL J. Dairy Res. 70:29-36(2003).
RN [2]
RP PROTEIN SEQUENCE OF 16-241 (ISOFORM 1), DEAMIDATION AT ASN-150, AND MASS
RP SPECTROMETRY.
RC STRAIN=Haflinger {ECO:0000269|PubMed:16691551};
RC TISSUE=Milk {ECO:0000269|PubMed:16691551};
RX PubMed=16691551; DOI=10.1002/pmic.200500728;
RA Girardet J.-M., Miclo L., Florent S., Molle D., Gaillard J.-L.;
RT "Determination of the phosphorylation level and deamidation susceptibility
RT of equine beta-casein.";
RL Proteomics 6:3707-3717(2006).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 16-241 (ISOFORM 3), AND MASS SPECTROMETRY.
RC STRAIN=Haflinger {ECO:0000269|PubMed:17366489};
RC TISSUE=Milk {ECO:0000269|PubMed:17366489};
RX PubMed=17366489; DOI=10.1002/pmic.200600683;
RA Miclo L., Girardet J.-M., Egito A.S., Molle D., Martin P., Gaillard J.-L.;
RT "The primary structure of a low-M(r) multiphosphorylated variant of beta-
RT casein in equine milk.";
RL Proteomics 7:1327-1335(2007).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 16-50 (ISOFORM 1), AND PROTEIN SEQUENCE OF 16-58
RP (ISOFORM 2).
RC STRAIN=Welsh pony {ECO:0000269|PubMed:15274143};
RC TISSUE=Milk {ECO:0000269|PubMed:15274143};
RX PubMed=15274143; DOI=10.1002/pmic.200300765;
RA Miranda G., Mahe M.-F., Leroux C., Martin P.;
RT "Proteomic tools to characterize the protein fraction of Equidae milk.";
RL Proteomics 4:2496-2509(2004).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 16-30, AND SUBCELLULAR LOCATION.
RC STRAIN=Haflinger {ECO:0000269|PubMed:12018413};
RC TISSUE=Milk {ECO:0000269|PubMed:12018413};
RX PubMed=12018413; DOI=10.3168/jds.s0022-0302(02)74126-x;
RA Egito A.S., Miclo L., Lopez C., Adam A., Girardet J.-M., Gaillard J.-L.;
RT "Separation and characterization of mares' milk alpha(s1)-, beta-, kappa-
RT caseins, gamma-casein-like, and proteose peptone component 5-like
RT peptides.";
RL J. Dairy Sci. 85:697-706(2002).
RN [6]
RP PHOSPHORYLATION AT SER-24; SER-25; THR-27; SER-33; SER-38; SER-39 AND
RP SER-40.
RX PubMed=20486249; DOI=10.1002/rcm.4552;
RA Mateos A., Girardet J.M., Molle D., Corbier C., Gaillard J.L., Miclo L.;
RT "Identification of phosphorylation sites of equine beta-casein isoforms.";
RL Rapid Commun. Mass Spectrom. 24:1533-1542(2010).
CC -!- FUNCTION: Important role in determination of the surface properties of
CC the casein micelles. {ECO:0000250|UniProtKB:P39037}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12018413}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16691551}; Synonyms=B
CC {ECO:0000269|PubMed:16691551};
CC IsoId=Q9GKK3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12617390};
CC IsoId=Q9GKK3-2; Sequence=VSP_051779;
CC Name=3 {ECO:0000269|PubMed:17366489}; Synonyms=low molecular weight
CC beta-casein {ECO:0000269|PubMed:17366489};
CC IsoId=Q9GKK3-3; Sequence=VSP_051780;
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC {ECO:0000305}.
CC -!- PTM: There are at least five different forms found in milk, with
CC varying degrees of phosphorylation. These include form 3-P which is
CC phosphorylated at three sites that have not been determined, this form
CC is present in very low amounts, form 4-P which is phosphorylated at
CC four sites, form 5-P which is phosphorylated at five sites, form 6-P
CC which is phosphorylated at six sites, and form 7-P which is
CC phosphorylated at seven sites. {ECO:0000269|PubMed:16691551,
CC ECO:0000269|PubMed:20486249}.
CC -!- PTM: Spontaneous deamidation of Asn-150 produces aspartate or
CC isoaspartate. {ECO:0000269|PubMed:16691551}.
CC -!- MASS SPECTROMETRY: [Isoform 1]: Mass=25514; Mass_error=3;
CC Method=Electrospray; Note=Dephosphorylated. The measured range is 16-
CC 241.; Evidence={ECO:0000269|PubMed:16691551};
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10591; Mass_error=2;
CC Method=Electrospray; Note=Dephosphorylated. The measured range is 16-
CC 109.; Evidence={ECO:0000269|PubMed:17366489};
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10911; Method=Electrospray;
CC Note=Form 4-P. The measured range is 16-109.;
CC Evidence={ECO:0000269|PubMed:17366489};
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10991; Method=Electrospray;
CC Note=Form 5-P. The measured range is 16-109.;
CC Evidence={ECO:0000269|PubMed:17366489};
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=11071; Method=Electrospray;
CC Note=Form 6-P. The measured range is 16-109.;
CC Evidence={ECO:0000269|PubMed:17366489};
CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=11150; Method=Electrospray;
CC Note=Form 7-P. The measured range is 16-109.;
CC Evidence={ECO:0000269|PubMed:17366489};
CC -!- MISCELLANEOUS: [Isoform 3]: Accounts for 4% of total casein.
CC {ECO:0000269|PubMed:17366489}.
CC -!- SIMILARITY: Belongs to the beta-casein family. {ECO:0000255}.
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; AF214526; AAG43954.1; -; mRNA.
DR RefSeq; NP_001075321.1; NM_001081852.1. [Q9GKK3-2]
DR AlphaFoldDB; Q9GKK3; -.
DR STRING; 9796.ENSECAP00000042870; -.
DR iPTMnet; Q9GKK3; -.
DR PaxDb; Q9GKK3; -.
DR PeptideAtlas; Q9GKK3; -.
DR Ensembl; ENSECAT00000010264; ENSECAP00000007906; ENSECAG00000009837. [Q9GKK3-2]
DR Ensembl; ENSECAT00000064283; ENSECAP00000042870; ENSECAG00000009837. [Q9GKK3-1]
DR GeneID; 100033903; -.
DR KEGG; ecb:100033903; -.
DR CTD; 1447; -.
DR GeneTree; ENSGT00390000001890; -.
DR HOGENOM; CLU_106775_0_0_1; -.
DR InParanoid; Q9GKK3; -.
DR OMA; LMHQIPQ; -.
DR OrthoDB; 1336883at2759; -.
DR TreeFam; TF336929; -.
DR Proteomes; UP000002281; Chromosome 3.
DR Bgee; ENSECAG00000009837; Expressed in prefrontal cortex.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IEA:Ensembl.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR016345; Casein_beta.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR11500; PTHR11500; 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 Alternative splicing; Direct protein sequencing; Milk protein;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12018413"
FT CHAIN 16..241
FT /note="Beta-casein"
FT /id="PRO_0000004474"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 30
FT /note="Not phosphorylated"
FT SITE 32
FT /note="Not phosphorylated"
FT MOD_RES 24
FT /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 25
FT /note="Phosphoserine; in form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 27
FT /note="Phosphothreonine; in form 6-P and form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05814"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05814"
FT MOD_RES 33
FT /note="Phosphoserine; in form 5-P, form 6-P and form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 38
FT /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 39
FT /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 40
FT /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT form 7-P"
FT /evidence="ECO:0000269|PubMed:20486249"
FT MOD_RES 150
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:16691551"
FT VAR_SEQ 42..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12617390"
FT /id="VSP_051779"
FT VAR_SEQ 65..196
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17366489"
FT /id="VSP_051780"
SQ SEQUENCE 241 AA; 27049 MW; 140B6EBF3D2323C0 CRC64;
MKILILACLV ALALAREKEE LNVSSETVES LSSNEPDSSS EESITHINKE KLQKFKHEGQ
QQREVERQDK ISRFVQPQPV VYPYAEPVPY AVVPQSILPL AQPPILPFLQ PEIMEVSQAK
ETILPKRKVM PFLKSPIVPF SERQILNPTN GENLRLPVHL IQPFMHQVPQ SLLQTLMLPS
QPVLSPPQSK VAPFPQPVVP YPQRDTPVQA FLLYQDPRLG PTGELDPATQ PIVAVHNPVI
V