CASA1_RAT
ID CASA1_RAT Reviewed; 284 AA.
AC P02661;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Alpha-S1-casein;
DE Short=Alpha-casein;
DE Flags: Precursor;
GN Name=Csn1s1; Synonyms=Csna;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6298707; DOI=10.1093/nar/10.24.8079;
RA Hobbs A.A., Rosen J.M.;
RT "Sequence of rat alpha- and gamma-casein mRNAs: evolutionary comparison of
RT the calcium-dependent rat casein multigene family.";
RL Nucleic Acids Res. 10:8079-8098(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX PubMed=3952000; DOI=10.1093/nar/14.4.1883;
RA Yu-Lee L.Y., Richter-Mann L., Couch C.H., Stewart A.F., Mackinlay A.G.,
RA Rosen J.M.;
RT "Evolution of the casein multigene family: conserved sequences in the 5'
RT flanking and exon regions.";
RL Nucleic Acids Res. 14:1883-1902(1986).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000305}.
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DR EMBL; J00710; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X03585; CAA27261.1; -; Genomic_DNA.
DR EMBL; X03586; CAA27262.1; -; Genomic_DNA.
DR EMBL; X03587; CAA27263.1; -; Genomic_DNA.
DR EMBL; X03588; CAA27264.1; -; Genomic_DNA.
DR PIR; A03105; KART.
DR RefSeq; NP_620229.2; NM_138874.2.
DR AlphaFoldDB; P02661; -.
DR SMR; P02661; -.
DR STRING; 10116.ENSRNOP00000056956; -.
DR Allergome; 2151; Rat n 8.
DR iPTMnet; P02661; -.
DR PhosphoSitePlus; P02661; -.
DR PaxDb; P02661; -.
DR PRIDE; P02661; -.
DR GeneID; 24284; -.
DR KEGG; rno:24284; -.
DR UCSC; RGD:2430; rat.
DR CTD; 1446; -.
DR RGD; 2430; Csn1s1.
DR eggNOG; ENOG502TEWT; Eukaryota.
DR InParanoid; P02661; -.
DR OrthoDB; 1563397at2759; -.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR PRO; PR:P02661; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1903496; P:response to 11-deoxycorticosterone; IBA:GO_Central.
DR GO; GO:1903494; P:response to dehydroepiandrosterone; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
DR GO; GO:0032570; P:response to progesterone; IBA:GO_Central.
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 Milk protein; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000250"
FT CHAIN 16..284
FT /note="Alpha-S1-casein"
FT /id="PRO_0000004458"
FT REPEAT 138..143
FT /note="1"
FT REPEAT 144..149
FT /note="2"
FT REPEAT 150..155
FT /note="3"
FT REPEAT 156..161
FT /note="4"
FT REPEAT 162..167
FT /note="5"
FT REPEAT 168..173
FT /note="6"
FT REPEAT 174..179
FT /note="7"
FT REPEAT 180..185
FT /note="8"
FT REPEAT 186..191
FT /note="9"
FT REPEAT 192..197
FT /note="10"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..197
FT /note="10 X 6 AA tandem repeats"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02662"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O97943"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47710"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04653"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18626"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04653"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02662"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04653"
SQ SEQUENCE 284 AA; 31802 MW; FB3D34DA46417CD5 CRC64;
MKLLILTCLV AAALALPRAH RRNAVSSQTQ QENSSSEEQE IVKQPKYLSL NEEFVNNLNR
QRELLTEQDN EIKITMDSSA EEQATASAQE DSSSSSSSSE ESKDAIPSAT EQKNIANKEI
LNRCTLEQLQ RQIKYSQLLQ QASLAQQASL AQQASLAQQA LLAQQPSLAQ QAALAQQASL
AQQASLAQQA SLAQKHHPRL SQVYYPNMEQ PYRMNAYSQV QMRHPMSVVD QAQFSVQSFP
QLSQYGAYPL WLYFPQDMQY LTPEAVLNTF KPIAPKDAEN TNVW