CASK_RUSUN
ID CASK_RUSUN Reviewed; 122 AA.
AC Q95177;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Kappa-casein;
DE Flags: Fragment;
GN Name=CSN3; Synonyms=CSN10, CSNK;
OS Rusa unicolor (Sambar) (Cervus unicolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Rusa.
OX NCBI_TaxID=662561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8899730; DOI=10.1006/mpev.1996.0078;
RA Cronin M.A., Stuart R., Pierson B.J., Patton J.C.;
RT "K-casein gene phylogeny of higher ruminants (Pecora, Artiodactyla).";
RL Mol. Phylogenet. Evol. 6:295-311(1996).
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}.
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; U37508; AAC48654.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95177; -.
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.
PE 2: Evidence at transcript level;
KW Glycoprotein; Milk protein; Phosphoprotein; Secreted.
FT CHAIN <1..122
FT /note="Kappa-casein"
FT /id="PRO_0000144107"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58..59
FT /note="Cleavage; by chymosin/rennin"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 102
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02670"
FT CARBOHYD 84
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 86
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 89
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 95
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 102
FT /note="O-linked (GalNAc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 118
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT NON_TER 1
SQ SEQUENCE 122 AA; 13188 MW; 5FFC35706AF862AA CRC64;
VALINNQFLP YPYYAKPGAV RSPAQILQWQ VLPNTVPARS CQPQPTTMAR HPHPHLSFMA
IPPKKNQDKT DIPSINTIAT AESTITPTTE AIVDTVATQE ASSEVIESAP EAKADQVTST
VV