CASK_CAPHI
ID CASK_CAPHI Reviewed; 192 AA.
AC P02670; Q8SPM9; Q8SPN0; Q8SPV1; Q8SPW6; Q8SPW7; Q8SPW8; Q8WMV5; Q8WN74;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Kappa-casein;
DE Short=Kappa-CN;
DE Flags: Precursor;
GN Name=CSN3; Synonyms=CSN10, CSNK;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ssp. aegagrus; TISSUE=Mammary gland;
RX PubMed=8226388; DOI=10.2527/1993.71102833x;
RA Coll A., Folch J.M., Sanchez A.;
RT "Nucleotide sequence of the goat kappa-casein cDNA.";
RL J. Anim. Sci. 71:2833-2833(1993).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 22-192, AND PYROGLUTAMATE FORMATION AT GLN-22.
RX PubMed=16386026; DOI=10.1016/0014-5793(76)80972-6;
RA Mercier J.-C., Chobert J.-M., Addeo F.;
RT "Comparative study of the amino acid sequences of the caseinomacropeptides
RT from seven species.";
RL FEBS Lett. 72:208-214(1976).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-192, AND VARIANTS ARG-65; ILE-86;
RP ILE-140 AND PRO-180.
RX PubMed=11531704; DOI=10.1046/j.1365-2052.2001.00765.x;
RA Caroli A., Jann O., Budelli E., Bolla P., Jaeger S., Erhardt G.;
RT "Genetic polymorphism of goat kappa-casein (CSN3) in different breeds and
RT characterization at DNA level.";
RL Anim. Genet. 32:226-230(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 31-192, AND VARIANTS ILE-86; ILE-140; VAL-177 AND
RP PRO-180.
RX PubMed=11504385; DOI=10.1017/s0022029901004733;
RA Yahyaoui M.H., Coll A., Sanchez A., Folch J.M.;
RT "Genetic polymorphism of the caprine kappa casein gene.";
RL J. Dairy Res. 68:209-216(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 31-192, AND VARIANTS GLY-111 AND ILE-140.
RA Angiolillo A., Yahyaoui M.H., Sanchez A., Pilla F., Folch J.M.;
RT "Characterization of a new genetic variant in the caprine k-casein gene.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE OF 31-192, AND VARIANTS ARG-65; ILE-86; ILE-140 AND
RP PRO-180.
RA Yahyaoui M.H., Sanchez A., Folch J.M.;
RT "Characterization of new genetic variants and genotyping of the caprine
RT kappa casein gene.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE OF 31-189, AND VARIANT ILE-140.
RA Feligini M., Cubric-Curik V., Parma P., Curik I., Greppi G., Enne G.;
RT "Polymorphism of kappa-casein in Italian goat breeds: a new ACRS-PCR
RT designed DNA test for discrimination of A and B alleles.";
RL Food Technol. Biotechnol. 40:293-298(2002).
RN [9]
RP PROTEIN SEQUENCE OF 127-192, AND PHOSPHORYLATION AT SER-172 AND SER-189.
RX PubMed=1016651;
RA Mercier J.-C., Addeo F., Pelissier J.-P.;
RT "Primary structure of the casein macropeptide of caprine kappa casein.";
RL Biochimie 58:1303-1310(1976).
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; D14373; BAA03286.1; -; Genomic_DNA.
DR EMBL; X60763; CAA43174.1; -; mRNA.
DR EMBL; AY027868; AAK17010.1; -; Genomic_DNA.
DR EMBL; AF485339; AAL90871.1; -; Genomic_DNA.
DR EMBL; AF485340; AAL90872.1; -; Genomic_DNA.
DR EMBL; AF485341; AAL90873.1; -; Genomic_DNA.
DR EMBL; AF486523; AAL93193.1; -; Genomic_DNA.
DR EMBL; AY090465; AAM12025.1; -; Genomic_DNA.
DR EMBL; AY090466; AAM12026.1; -; Genomic_DNA.
DR EMBL; AY090467; AAM12027.1; -; Genomic_DNA.
DR EMBL; AF434988; AAL31535.1; -; Genomic_DNA.
DR PIR; A94479; KKGT.
DR PIR; S15513; S15513.
DR RefSeq; NP_001272516.1; NM_001285587.1.
DR AlphaFoldDB; P02670; -.
DR STRING; 9925.ENSCHIP00000033244; -.
DR Allergome; 1242; Cap h 8.
DR Allergome; 2969; Cap h 12.
DR iPTMnet; P02670; -.
DR PRIDE; P02670; -.
DR GeneID; 100861231; -.
DR KEGG; chx:100861231; -.
DR CTD; 1448; -.
DR OrthoDB; 1540917at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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 Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:16386026"
FT CHAIN 22..192
FT /note="Kappa-casein"
FT /id="PRO_0000004492"
FT REGION 167..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 126..127
FT /note="Cleavage; by chymosin/rennin"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:16386026"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT MOD_RES 172
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000269|PubMed:1016651"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1016651"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 155
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 156
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 159
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 165
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 172
FT /note="O-linked (GalNAc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 188
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT VARIANT 65
FT /note="Q -> R (in allele CSN3-B)"
FT /evidence="ECO:0000269|PubMed:11531704, ECO:0000269|Ref.7"
FT VARIANT 86
FT /note="V -> I (in allele CSN3-B, allele C and allele G)"
FT /evidence="ECO:0000269|PubMed:11504385,
FT ECO:0000269|PubMed:11531704, ECO:0000269|Ref.7"
FT VARIANT 111
FT /note="D -> G (in allele E)"
FT /evidence="ECO:0000269|Ref.6"
FT VARIANT 140
FT /note="V -> I (in allele CSN3-B, allele B, allele C, allele
FT E, allele F and allele G)"
FT /evidence="ECO:0000269|PubMed:11504385,
FT ECO:0000269|PubMed:11531704, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT VARIANT 177
FT /note="A -> V (in allele C)"
FT /evidence="ECO:0000269|PubMed:11504385"
FT VARIANT 180
FT /note="S -> P (in allele CSN3-B, allele C, allele F and
FT allele G)"
FT /evidence="ECO:0000269|PubMed:11504385,
FT ECO:0000269|PubMed:11531704, ECO:0000269|Ref.7"
FT CONFLICT 134
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21441 MW; 009F5858F4BFB178 CRC64;
MMKSFFLVVT ILALTLPFLG AQEQNQEQPI CCEKDERFFD DKIAKYIPIQ YVLSRYPSYG
LNYYQQRPVA LINNQFLPYP YYAKPVAVRS PAQTLQWQVL PNTVPAKSCQ DQPTTLARHP
HPHLSFMAIP PKKDQDKTEV PAINTIASAE PTVHSTPTTE AIVNTVDNPE ASSESIASAS
ETNTAQVTST EV
