CASA1_CAPHI
ID CASA1_CAPHI Reviewed; 214 AA.
AC P18626;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Alpha-S1-casein;
DE Short=Alpha-S1-CN;
DE Flags: Precursor;
GN Name=CSN1S1;
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], AND VARIANTS ALLELE A LEU-31 AND GLN-92.
RX PubMed=1372900; DOI=10.1016/s0021-9258(18)42674-9;
RA Leroux C., Mazure N., Martin P.;
RT "Mutations away from splice site recognition sequences might cis-modulate
RT alternative splicing of goat alpha s1-casein transcripts. Structural
RT organization of the relevant gene.";
RL J. Biol. Chem. 267:6147-6157(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALLELE E 74-GLN--LEU-110 DEL;
RP LYS-115 AND ALA-210.
RC TISSUE=Mammary gland;
RX PubMed=7926797; DOI=10.1016/0378-1119(94)90063-9;
RA Perez M.J., Leroux C., Bonastre A.S., Martin P.;
RT "Occurrence of a LINE sequence in the 3' UTR of the goat alpha s1-casein E-
RT encoding allele associated with reduced protein synthesis level.";
RL Gene 147:179-187(1994).
RN [3]
RP PROTEIN SEQUENCE OF 16-214 (VARIANTS D; E AND F), AND PHOSPHORYLATION AT
RP SER-90.
RX PubMed=2226443; DOI=10.1111/j.1432-1033.1990.tb19328.x;
RA Brignon G., Mahe M.-F., Ribadeau-Dumas B., Mercier J.-C., Grosclaude F.;
RT "Two of the three genetic variants of goat alpha s1-casein which are
RT synthesized at a reduced level have an internal deletion possibly due to
RT altered RNA splicing.";
RL Eur. J. Biochem. 193:237-241(1990).
RN [4]
RP PROTEIN SEQUENCE OF 16-214 (VARIANTS A; B AND C), AND PHOSPHORYLATION AT
RP SER-61; SER-63; SER-79; SER-80; SER-81; SER-82; SER-83; SER-90 AND SER-130.
RX PubMed=2755948;
RA Brignon G., Mahe M.-F., Grosclaude F., Ribadeau-Dumas B.;
RT "Sequence of caprine alpha s1-casein and characterization of those of its
RT genetic variants which are synthesized at a high level, alpha s1-CnA, B and
RT C.";
RL Protein Seq. Data Anal. 2:181-188(1989).
CC -!- FUNCTION: Important role in the capacity of milk to transport calcium
CC phosphate.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- MISCELLANEOUS: The sequence shown is variant form B.
CC -!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000305}.
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DR EMBL; X59836; CAA42496.1; -; mRNA.
DR EMBL; X72221; CAA51022.1; -; mRNA.
DR PIR; S34262; S34262.
DR RefSeq; XP_017904616.1; XM_018049127.1.
DR AlphaFoldDB; P18626; -.
DR Allergome; 1242; Cap h 8.
DR Allergome; 2966; Cap h 9.
DR iPTMnet; P18626; -.
DR GeneID; 100750242; -.
DR CTD; 1446; -.
DR OrthoDB; 1478191at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR026999; Alpha-s1_casein.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR10240; PTHR10240; 1.
DR Pfam; PF00363; Casein; 1.
DR PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Milk protein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:2226443,
FT ECO:0000269|PubMed:2755948"
FT CHAIN 16..214
FT /note="Alpha-S1-casein"
FT /id="PRO_0000004448"
FT REGION 59..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2226443,
FT ECO:0000269|PubMed:2755948"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2755948"
FT VARIANT 23
FT /note="H -> I (in variant C)"
FT VARIANT 31
FT /note="P -> L (in variant A)"
FT /evidence="ECO:0000269|PubMed:1372900"
FT VARIANT 74..110
FT /note="Missing (in variant F)"
FT /evidence="ECO:0000269|PubMed:7926797"
FT VARIANT 74..84
FT /note="Missing (in variant D)"
FT VARIANT 92
FT /note="E -> Q (in variant A)"
FT /evidence="ECO:0000269|PubMed:1372900"
FT VARIANT 115
FT /note="R -> K (in variants E and C)"
FT /evidence="ECO:0000269|PubMed:7926797"
FT VARIANT 209
FT /note="T -> A (in variant E)"
FT VARIANT 210
FT /note="T -> A (in variants E and C)"
FT /evidence="ECO:0000269|PubMed:7926797"
FT CONFLICT 24
FT /note="R -> Q (in Ref. 1; CAA42496 and 2; CAA51022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24290 MW; 33070A587E5811D9 CRC64;
MKLLILTCLV AVALARPKHP INHRGLSPEV PNENLLRFVV APFPEVFRKE NINELSKDIG
SESTEDQAME DAKQMKAGSS SSSEEIVPNS AEQKYIQKED VPSERYLGYL EQLLRLKKYN
VPQLEIVPKS AEEQLHSMKE GNPAHQKQPM IAVNQELAYF YPQLFRQFYQ LDAYPSGAWY
YLPLGTQYTD APSFSDIPNP IGSENSGKTT MPLW
