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CASB_MOUSE
ID   CASB_MOUSE              Reviewed;         231 AA.
AC   P10598; Q543D9; Q8VCT6; Q8VCU8; Q91VI5; Q922Y5; Q9D1U6; Q9D1U7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Beta-casein;
DE   Flags: Precursor;
GN   Name=Csn2; Synonyms=Csnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3774558; DOI=10.1093/nar/14.20.8224;
RA   Yoshimura M., Banerjee M.R., Oka T.;
RT   "Nucleotide sequence of a cDNA encoding mouse beta casein.";
RL   Nucleic Acids Res. 14:8224-8224(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2673924; DOI=10.1016/0378-1119(89)90229-1;
RA   Yoshimura M., Oka T.;
RT   "Isolation and structural analysis of the mouse beta-casein gene.";
RL   Gene 78:267-275(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C3H/HeN; TISSUE=Liver;
RX   PubMed=2187188; DOI=10.1073/pnas.87.10.3670;
RA   Yoshimura M., Oka T.;
RT   "Transfection of beta-casein chimeric gene and hormonal induction of its
RT   expression in primary murine mammary epithelial cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3670-3674(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Important role in determination of the surface properties of
CC       the casein micelles.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC   -!- SIMILARITY: Belongs to the beta-casein family. {ECO:0000305}.
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DR   EMBL; X04490; CAA28178.1; -; mRNA.
DR   EMBL; X13484; CAA31840.1; -; Genomic_DNA.
DR   EMBL; AK021324; BAB32374.1; -; mRNA.
DR   EMBL; AK021328; BAB32375.1; -; mRNA.
DR   EMBL; AK052803; BAC35152.1; -; mRNA.
DR   EMBL; AK052805; BAC35153.1; -; mRNA.
DR   EMBL; AK085694; BAC39508.1; -; mRNA.
DR   EMBL; AK085729; BAC39522.1; -; mRNA.
DR   EMBL; AK142616; BAE25131.1; -; mRNA.
DR   EMBL; AK142620; BAE25133.1; -; mRNA.
DR   EMBL; AK142635; BAE25141.1; -; mRNA.
DR   EMBL; AK164747; BAE37898.1; -; mRNA.
DR   EMBL; AK164791; BAE37917.1; -; mRNA.
DR   EMBL; AK164792; BAE37918.1; -; mRNA.
DR   EMBL; AK164793; BAE37919.1; -; mRNA.
DR   EMBL; AK164794; BAE37920.1; -; mRNA.
DR   EMBL; BC013332; AAH13332.1; -; mRNA.
DR   EMBL; BC019114; AAH19114.1; -; mRNA.
DR   EMBL; BC019189; AAH19189.1; -; mRNA.
DR   EMBL; BC021153; AAH21153.1; -; mRNA.
DR   CCDS; CCDS39131.1; -.
DR   PIR; JU0061; JU0061.
DR   RefSeq; NP_001272949.1; NM_001286020.1.
DR   RefSeq; NP_001272950.1; NM_001286021.1.
DR   RefSeq; NP_001272952.1; NM_001286023.1.
DR   RefSeq; NP_034102.1; NM_009972.2.
DR   AlphaFoldDB; P10598; -.
DR   BioGRID; 198938; 3.
DR   STRING; 10090.ENSMUSP00000080976; -.
DR   PhosphoSitePlus; P10598; -.
DR   PaxDb; P10598; -.
DR   PeptideAtlas; P10598; -.
DR   PRIDE; P10598; -.
DR   ProteomicsDB; 265548; -.
DR   Antibodypedia; 24273; 219 antibodies from 24 providers.
DR   DNASU; 12991; -.
DR   Ensembl; ENSMUST00000197422; ENSMUSP00000143341; ENSMUSG00000063157.
DR   Ensembl; ENSMUST00000199624; ENSMUSP00000143409; ENSMUSG00000063157.
DR   GeneID; 12991; -.
DR   KEGG; mmu:12991; -.
DR   UCSC; uc008xyu.2; mouse.
DR   CTD; 1447; -.
DR   MGI; MGI:88541; Csn2.
DR   VEuPathDB; HostDB:ENSMUSG00000063157; -.
DR   eggNOG; ENOG502RU0R; Eukaryota.
DR   GeneTree; ENSGT00390000001890; -.
DR   InParanoid; P10598; -.
DR   OMA; LMHQIPQ; -.
DR   OrthoDB; 1336883at2759; -.
DR   PhylomeDB; P10598; -.
DR   TreeFam; TF336929; -.
DR   BioGRID-ORCS; 12991; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Csn2; mouse.
DR   PRO; PR:P10598; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P10598; protein.
DR   Bgee; ENSMUSG00000063157; Expressed in thoracic mammary gland and 23 other tissues.
DR   ExpressionAtlas; P10598; differential.
DR   Genevisible; P10598; MM.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0007595; P:lactation; ISO:MGI.
DR   GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR   InterPro; IPR001588; Casein.
DR   InterPro; IPR016345; Casein_beta.
DR   InterPro; IPR031305; Casein_CS.
DR   PANTHER; PTHR11500; PTHR11500; 1.
DR   Pfam; PF00363; Casein; 1.
DR   PIRSF; PIRSF002372; Beta-casein; 1.
DR   PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Milk protein; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000250"
FT   CHAIN           16..231
FT                   /note="Beta-casein"
FT                   /id="PRO_0000004477"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GKK3"
FT   MOD_RES         26
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GKK3"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05814"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05814"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05814"
FT   CONFLICT        3
FT                   /note="V -> T (in Ref. 5; AAH19189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="Missing (in Ref. 4; BAB32374/BAB32375 and 5;
FT                   AAH19114/AAH19189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="S -> C (in Ref. 4; BAB32374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="Q -> R (in Ref. 5; AAH13332)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..166
FT                   /note="VV -> GG (in Ref. 4; BAB32375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="L -> V (in Ref. 4; BAB32374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="T -> P (in Ref. 4; BAB32374/BAB32375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   231 AA;  25337 MW;  7DD7DFF0766A9422 CRC64;
     MKVFILACLV ALALARETTF TVSSETDSIS SEESVEHINE QKLQKVNLMG QLQAEDVLQA
     KVHSSIQSQP QAFPYAQAQT ISCNPVPQNI QPIAQPPVVP SLGPVISPEL ESFLKAKATI
     LPKHKQMPLL NSETVLRLIN SQIPSLASLA NLHLPQSLVQ LLAQVVQAFP QTHLVSSQTQ
     LSLPQSKVLY FLQQVAPFLP QDMSVQDLLQ YLELLNPTVQ FPATPQHSVS V
 
 
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