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Alpha-S1-casein [Cleaved into: Casoxin-D]

 CASA1_HUMAN             Reviewed;         185 AA.
P47710; A1A510; A1A511; E9PB60; Q4PNR5;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
15-MAR-2017, entry version 143.
RecName: Full=Alpha-S1-casein;
Contains:
RecName: Full=Casoxin-D;
Flags: Precursor;
Name=CSN1S1; Synonyms=CASA, CSN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Mammary gland;
PubMed=7619062; DOI=10.1042/bj3090237;
Johnsen L.B., Rasmussen L.K., Petersen T.E., Berglund L.;
"Characterization of three types of human alpha s1-casein mRNA
transcripts.";
Biochem. J. 309:237-242(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
Yu D.Y., Jeong S., Lee K.K., Lonnerdal B.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z.,
Liang M., Wen S., Li H., Yang S.;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-117.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-185 (ISOFORMS 1; 2 AND 3).
Martin P., Brignon G., Furet J.-P., Leroux C.;
"The gene encoding alpha s1-casein is expressed in human mammary
epithelial cells during lactation.";
Lait 76:525-537(1996).
[8]
PROTEIN SEQUENCE OF 16-29.
PubMed=8192860; DOI=10.1515/bchm3.1994.375.2.149;
Cavaletto M., Cantisani A., Giuffrida G., Napolitano L., Conti A.;
"Human alpha S1-casein like protein: purification and N-terminal
sequence determination.";
Biol. Chem. Hoppe-Seyler 375:149-151(1994).
[9]
PROTEIN SEQUENCE OF 16-29 AND 99-105, AND CHARACTERIZATION.
PubMed=7749638; DOI=10.1016/0305-0491(94)00225-J;
Rasmussen L.K., Due H.A., Petersen T.E.;
"Human alpha s1-casein: purification and characterization.";
Comp. Biochem. Physiol. 111B:75-81(1995).
[10]
PROTEIN SEQUENCE OF 27-42 AND 83-98, PHOSPHORYLATION AT SER-33;
SER-41; SER-88 AND SER-90, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17646876; DOI=10.1039/b701902e;
Kjeldsen F., Savitski M.M., Nielsen M.L., Shi L., Zubarev R.A.;
"On studying protein phosphorylation patterns using bottom-up LC-
MS/MS: the case of human alpha-casein.";
Analyst 132:768-776(2007).
[11]
PROTEIN SEQUENCE OF 28-48, PHOSPHORYLATION AT SER-31; SER-33; SER-41;
SER-86; SER-88; SER-89; SER-90 AND SER-91, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18847231; DOI=10.1021/pr800387s;
Poth A.G., Deeth H.C., Alewood P.F., Holland J.W.;
"Analysis of the human casein phosphoproteome by 2-D electrophoresis
and MALDI-TOF/TOF MS reveals new phosphoforms.";
J. Proteome Res. 7:5017-5027(2008).
[12]
PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-33 AND SER-41, LACK
OF GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12919330; DOI=10.1046/j.1432-1033.2003.03755.x;
Sorensen E.S., Moller L., Vinther M., Petersen T.E., Rasmussen L.K.;
"The phosphorylation pattern of human alphas1-casein is markedly
different from the ruminant species.";
Eur. J. Biochem. 270:3651-3655(2003).
[13]
GENOMIC ORGANIZATION, AND CHROMOSOMAL LOCATION.
PubMed=9050925; DOI=10.1007/s004390050374;
Fujiwara Y., Miwa M., Nogami M., Okumura K., Nobori T., Suzuki T.,
Ueda M.;
"Genomic organization and chromosomal localization of the human casein
gene family.";
Hum. Genet. 99:368-373(1997).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
-!- FUNCTION: Important role in the capacity of milk to transport
calcium phosphate.
-!- FUNCTION: Casoxin D acts as opioid antagonist and has vasorelaxing
activity mediated by bradykinin B1 receptors.
-!- SUBUNIT: Heteromultimers of alpha-s1 casein and kappa-casein;
disulfide-linked.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P47710-1; Sequence=Displayed;
Name=2;
IsoId=P47710-2; Sequence=VSP_000795;
Name=3;
IsoId=P47710-3; Sequence=VSP_000796;
Name=4;
IsoId=P47710-4; Sequence=VSP_000795, VSP_046130;
-!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
-!- PTM: Not glycosylated.
-!- MISCELLANEOUS: In milk, the alpha s1- and beta-caseins precipitate
in presence of calcium (so-called calcium-sensitive caseins).
Kappa-casein prevents the precipitation of the other caseins by
calcium through the formation of large stable colloidal particles
termed micelles.
-!- SIMILARITY: Belongs to the alpha-casein family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion
and glue - Issue 16 of November 2001;
URL="http://web.expasy.org/spotlight/back_issues/016";
-----------------------------------------------------------------------
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EMBL; X78416; CAA55185.1; -; mRNA.
EMBL; U23157; AAA69477.1; -; mRNA.
EMBL; DQ064604; AAY68392.1; -; mRNA.
EMBL; AC108941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX05599.1; -; Genomic_DNA.
EMBL; BC128227; AAI28228.1; -; mRNA.
EMBL; BC128228; AAI28229.1; -; mRNA.
EMBL; X98084; CAA66708.1; -; mRNA.
CCDS; CCDS47067.1; -. [P47710-1]
CCDS; CCDS54769.1; -. [P47710-4]
PIR; S56013; S56013.
RefSeq; NP_001020275.1; NM_001025104.1. [P47710-4]
RefSeq; NP_001881.1; NM_001890.1. [P47710-1]
RefSeq; XP_006714152.1; XM_006714089.2. [P47710-2]
RefSeq; XP_006714153.1; XM_006714090.2. [P47710-3]
UniGene; Hs.3155; -.
ProteinModelPortal; P47710; -.
BioGrid; 107833; 22.
IntAct; P47710; 3.
STRING; 9606.ENSP00000246891; -.
Allergome; 1064; Hom s 8.
iPTMnet; P47710; -.
PhosphoSitePlus; P47710; -.
SwissPalm; P47710; -.
BioMuta; CSN1S1; -.
PaxDb; P47710; -.
PeptideAtlas; P47710; -.
PRIDE; P47710; -.
Ensembl; ENST00000246891; ENSP00000246891; ENSG00000126545. [P47710-1]
Ensembl; ENST00000507763; ENSP00000422611; ENSG00000126545. [P47710-4]
GeneID; 1446; -.
KEGG; hsa:1446; -.
UCSC; uc003hep.2; human. [P47710-1]
CTD; 1446; -.
DisGeNET; 1446; -.
GeneCards; CSN1S1; -.
HGNC; HGNC:2445; CSN1S1.
HPA; HPA035659; -.
HPA; HPA057031; -.
MIM; 115450; gene.
neXtProt; NX_P47710; -.
OpenTargets; ENSG00000126545; -.
PharmGKB; PA26948; -.
eggNOG; ENOG410J2MD; Eukaryota.
eggNOG; ENOG41114JX; LUCA.
GeneTree; ENSGT00390000017378; -.
HOGENOM; HOG000115954; -.
HOVERGEN; HBG005242; -.
InParanoid; P47710; -.
KO; K17281; -.
OMA; SKCAEQF; -.
OrthoDB; EOG091G0XI1; -.
PhylomeDB; P47710; -.
TreeFam; TF340763; -.
Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
SIGNOR; P47710; -.
GeneWiki; CSN1S1; -.
GenomeRNAi; 1446; -.
PMAP-CutDB; P47710; -.
PRO; PR:P47710; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000126545; -.
CleanEx; HS_CSN1S1; -.
ExpressionAtlas; P47710; baseline and differential.
Genevisible; P47710; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR026999; Alpha-s1_casein.
InterPro; IPR031305; Casein_CS.
PANTHER; PTHR10240; PTHR10240; 1.
PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Milk protein; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 15 {ECO:0000269|PubMed:7749638,
ECO:0000269|PubMed:8192860}.
CHAIN 16 185 Alpha-S1-casein.
/FTId=PRO_0000004450.
PEPTIDE 158 164 Casoxin-D.
/FTId=PRO_0000004451.
MOD_RES 31 31 Phosphoserine.
{ECO:0000269|PubMed:18847231}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000269|PubMed:12919330,
ECO:0000269|PubMed:17646876,
ECO:0000269|PubMed:18847231}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:12919330,
ECO:0000269|PubMed:17646876,
ECO:0000269|PubMed:18847231}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:P02662}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000269|PubMed:18847231}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000269|PubMed:17646876,
ECO:0000269|PubMed:18847231}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000269|PubMed:18847231}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000269|PubMed:17646876,
ECO:0000269|PubMed:18847231}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000269|PubMed:18847231}.
VAR_SEQ 52 52 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:7619062,
ECO:0000303|Ref.3, ECO:0000303|Ref.7}.
/FTId=VSP_000795.
VAR_SEQ 66 73 Missing (in isoform 3).
{ECO:0000303|PubMed:7619062,
ECO:0000303|Ref.7}.
/FTId=VSP_000796.
VAR_SEQ 93 100 Missing (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_046130.
VARIANT 117 117 A -> V (in dbSNP:rs10030475).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_048614.
CONFLICT 80 80 P -> S (in Ref. 3; AAY68392).
{ECO:0000305}.
SEQUENCE 185 AA; 21671 MW; A7717899CDC7D563 CRC64;
MRLLILTCLV AVALARPKLP LRYPERLQNP SESSEPIPLE SREEYMNGMN RQRNILREKQ
TDEIKDTRNE STQNCVVAEP EKMESSISSS SEEMSLSKCA EQFCRLNEYN QLQLQAAHAQ
EQIRRMNENS HVQVPFQQLN QLAAYPYAVW YYPQIMQYVP FPPFSDISNP TAHENYEKNN
VMLQW


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