ID   CASK_CAMDR              Reviewed;         182 AA.
AC   P79139;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Kappa-casein;
DE   Flags: Precursor;
GN   Name=CSN3; Synonyms=CSN10, CSNK;
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Somali; TISSUE=Udder;
RX   PubMed=9627840; DOI=10.1017/s0022029997002847;
RA   Kappeler S., Farah Z., Puhan Z.;
RT   "Sequence analysis of Camelus dromedarius milk caseins.";
RL   J. Dairy Res. 65:209-222(1998).
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; Y10082; CAA71171.1; -; mRNA.
DR   RefSeq; NP_001290489.1; NM_001303560.1.
DR   AlphaFoldDB; P79139; -.
DR   STRING; 9838.ENSCDRP00005027658; -.
DR   GeneID; 105090949; -.
DR   KEGG; cdk:105090949; -.
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..20
FT   CHAIN           21..182
FT                   /note="Kappa-casein"
FT                   /id="PRO_0000004490"
FT   SITE            117..118
FT                   /note="Cleavage; by chymosin/rennin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         161
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02670"
FT   CARBOHYD        154
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
FT   CARBOHYD        178
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02668"
SQ   SEQUENCE   182 AA;  20418 MW;  418D19E061DA7338 CRC64;
     MKSFFLVVTI LALTLPFLGA EVQNQEQPTC FEKVERLLNE KTVKYFPIQF VQSRYPSYGI
     NYYQHRLAVP INNQFIPYPN YAKPVAIRLH AQIPQCQALP NIDPPTVERR PRPRPSFIAI
     PPKKTQDKTV NPAINTVATV EPPVIPTAEP AVNTVVIAEA SSEFITTSTP ETTTVQITST
     EI