CASK_BUBBU
ID CASK_BUBBU Reviewed; 190 AA.
AC P11840;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Kappa-casein;
DE Flags: Precursor;
GN Name=CSN3; Synonyms=CSN10, CSNK;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8587130; DOI=10.1007/bf00173165;
RA Chikuni K., Mori Y., Tabata T., Saito M., Monma M., Kosugiyama M.;
RT "Molecular phylogeny based on the kappa-casein and cytochrome b sequences
RT in the mammalian suborder ruminantia.";
RL J. Mol. Evol. 41:859-866(1995).
RN [2]
RP PROTEIN SEQUENCE OF 116-190.
RX PubMed=328059; DOI=10.1016/s0300-9084(77)80313-1;
RA Addeo F., Mercier J.-C.;
RT "Primary structure of the casein macropeptide of kappa casein of buffalo.";
RL Biochimie 59:375-379(1977).
CC -!- FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein
CC precipitation in milk.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- SIMILARITY: Belongs to the kappa-casein family. {ECO:0000305}.
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DR EMBL; D14370; BAA03285.1; -; Genomic_DNA.
DR RefSeq; NP_001277901.1; NM_001290972.1.
DR AlphaFoldDB; P11840; -.
DR Allergome; 1259; Bub b 8.
DR GeneID; 102395364; -.
DR KEGG; bbub:102395364; -.
DR CTD; 1448; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR000117; Casein_kappa.
DR PANTHER; PTHR11470; PTHR11470; 1.
DR Pfam; PF00997; Casein_kappa; 1.
DR PIRSF; PIRSF002374; Casein_kappa; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Milk protein; Phosphoprotein;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..190
FT /note="Kappa-casein"
FT /id="PRO_0000004489"
FT SITE 126..127
FT /note="Cleavage; by chymosin/rennin"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 170
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02670"
FT CARBOHYD 142
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 153
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 154
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 157
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 163
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 170
FT /note="O-linked (GalNAc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 186
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT VARIANT 156
FT /note="T -> I"
FT VARIANT 172
FT /note="E -> D"
SQ SEQUENCE 190 AA; 21398 MW; EE858824628A98AD CRC64;
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI RCEKEERFFN DKIAKYIPIQ YVLSRYPSYG
LNYYQQKPVA LINNQFLPYP YYAKPAAVRS PAQILQWQVL PNTVPAKSCQ AQPTTMTRHP
HPHLSFMAIP PKKNQDKTEI PTINTIVSVE PTSTPTTEAI ENTVATLEAS SEVIESVPET
NTAQVTSTVV
