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 29-MAY-2024, entry version 120. 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}. 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; 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 GlyCosmos; P02670; 7 sites, No reported glycans. DR iPTMnet; P02670; -. DR GeneID; 100861231; -. DR KEGG; chx:100861231; -. DR CTD; 1448; -. DR OrthoDB; 5265313at2759; -. DR Proteomes; UP000291000; Unassembled WGS sequence. DR Proteomes; UP000694566; Unplaced. DR Proteomes; UP000694900; Chromosome 6. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0007595; P:lactation; IEA:TreeGrafter. DR GO; GO:0050821; P:protein stabilization; IEA:TreeGrafter. DR InterPro; IPR000117; Casein_kappa. DR PANTHER; PTHR11470; KAPPA CASEIN; 1. DR PANTHER; PTHR11470:SF2; KAPPA-CASEIN; 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 //