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Breast carcinoma-amplified sequence 3 homolog (K20D4) (Protein rudhira)

 BCAS3_MOUSE             Reviewed;         928 AA.
Q8CCN5; Q8CC16; Q9EPX3;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 2.
18-JUL-2018, entry version 129.
RecName: Full=Breast carcinoma-amplified sequence 3 homolog {ECO:0000250|UniProtKB:Q9H6U6};
AltName: Full=K20D4 {ECO:0000303|PubMed:16099728};
AltName: Full=Protein rudhira {ECO:0000303|PubMed:16099728};
Name=Bcas3 {ECO:0000250|UniProtKB:Q9H6U6,
ECO:0000312|MGI:MGI:2385848};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Diencephalon, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 1), SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
PubMed=16099728; DOI=10.1016/j.modgep.2005.06.002;
Siva K., Inamdar M.S.;
"Rudhira is a cytoplasmic WD40 protein expressed in mouse embryonic
stem cells and during embryonic erythropoiesis.";
Gene Expr. Patterns 6:225-234(2006).
[3]
TISSUE SPECIFICITY.
PubMed=16617102; DOI=10.1073/pnas.0601989103;
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
"MTA1, a transcriptional activator of breast cancer amplified sequence
3.";
Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
[4]
ERRATUM.
Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
[5]
INDUCTION, AND CHROMATIN-BINDING.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-480; SER-488;
SER-838; SER-886 AND SER-898, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22300583; DOI=10.1016/j.yexcr.2012.01.016;
Jain M., Bhat G.P., Vijayra havan K., Inamdar M.S.;
"Rudhira/BCAS3 is a cytoskeletal protein that controls Cdc42
activation and directional cell migration during angiogenesis.";
Exp. Cell Res. 318:753-767(2012).
-!- FUNCTION: Functions synergistically with PELP1 as a
transcriptional coactivator of estrogen receptor-responsive genes.
Stimulates histone acetyltransferase activity. Binds to chromatin
(By similarity). Plays a role in angiogenesis. Participates in the
regulation of cell polarity and directional endothelial cell
migration by mediating both the activation and recruitment of
CDC42 and the reorganization of the actin cytoskeleton at the cell
leading edge. Promotes filipodia formation.
{ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}.
-!- SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the
interactions occur in a estrogen-dependent manner. Interacts with
beta-tubulin and VIM. {ECO:0000250|UniProtKB:Q9H6U6}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6U6}.
Cytoplasm {ECO:0000269|PubMed:16099728,
ECO:0000269|PubMed:22300583}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:22300583}. Note=Associates with chromatin.
Recruited to estrogen receptor-induced promoters in a PELP1-
dependent manner (By similarity). Localizes in the cytoplasm in
stationary cells. Translocates from the cytoplasm to the leading
edge in motile cells. Colocalizes with microtubules and
intermediate filaments in both stationary and motile cells.
{ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CCN5-1; Sequence=Displayed;
Name=2;
IsoId=Q8CCN5-2; Sequence=VSP_007861, VSP_007862;
Note=Due to an intron retention.;
-!- TISSUE SPECIFICITY: Expressed in blood islands and yolk sac blood
islands (at protein level). Highly expressed in mammary tumors.
Expressed in eostrogen-induced epithelial cells of mammary glands.
Expressed in brain, heart, kidney, lung, liver and spleen.
Expressed in embryonic stem cells, embryoid bodies, endothelial
cells and fibroblasts. {ECO:0000269|PubMed:16099728,
ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058}.
-!- DEVELOPMENTAL STAGE: Expressed in erythroid cells in the vessels
at 9.5 and 10.5 dpc (at protein level). Expressed in embryo at 7.5
dpc and in the yolk sac at 10.5 dpc. Expressed in the heart and
yolk sac mesoderm at 8.5 dpc. Expressed in the head mesenchyme,
somitic mesoderm, otic vesicle, vessels and few blood cells at 9.5
to 11.5 dpc. {ECO:0000269|PubMed:16099728}.
-!- INDUCTION: Up-regulated by PELP1 in response to estrogen.
{ECO:0000269|PubMed:17505058}.
-!- DOMAIN: Has been proposed to contain 7 WD repeats. This prediction
could not be reproduced. {ECO:0000305|PubMed:16099728}.
-!- MISCELLANEOUS: 'Rudhira' stands for 'blood' in Sanskrit as this
protein is strongly expressed in blood vessels.
{ECO:0000269|PubMed:16099728}.
-!- SIMILARITY: Belongs to the BCAS3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG34697.1; Type=Erroneous termination; Positions=388; Note=Translated as Ser.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF313800; AAG34697.1; ALT_SEQ; mRNA.
EMBL; AK032423; BAC27862.1; -; mRNA.
EMBL; AK034117; BAC28592.1; -; mRNA.
CCDS; CCDS25195.1; -. [Q8CCN5-1]
RefSeq; NP_001160114.1; NM_001166642.1.
RefSeq; NP_619622.3; NM_138681.4. [Q8CCN5-1]
RefSeq; XP_006532603.1; XM_006532540.2. [Q8CCN5-1]
UniGene; Mm.209989; -.
UniGene; Mm.287663; -.
ProteinModelPortal; Q8CCN5; -.
STRING; 10090.ENSMUSP00000074416; -.
iPTMnet; Q8CCN5; -.
PhosphoSitePlus; Q8CCN5; -.
SwissPalm; Q8CCN5; -.
EPD; Q8CCN5; -.
PaxDb; Q8CCN5; -.
PeptideAtlas; Q8CCN5; -.
PRIDE; Q8CCN5; -.
Ensembl; ENSMUST00000074875; ENSMUSP00000074416; ENSMUSG00000059439. [Q8CCN5-1]
Ensembl; ENSMUST00000108056; ENSMUSP00000103691; ENSMUSG00000059439. [Q8CCN5-2]
GeneID; 192197; -.
KEGG; mmu:192197; -.
UCSC; uc007krn.2; mouse. [Q8CCN5-2]
UCSC; uc007krp.2; mouse. [Q8CCN5-1]
CTD; 54828; -.
MGI; MGI:2385848; Bcas3.
eggNOG; KOG2109; Eukaryota.
eggNOG; KOG4415; Eukaryota.
eggNOG; ENOG410XSW7; LUCA.
GeneTree; ENSGT00390000006454; -.
HOGENOM; HOG000049129; -.
HOVERGEN; HBG050676; -.
InParanoid; Q8CCN5; -.
PRO; PR:Q8CCN5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000059439; -.
CleanEx; MM_BCAS3; -.
ExpressionAtlas; Q8CCN5; baseline and differential.
Genevisible; Q8CCN5; MM.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0010698; F:acetyltransferase activator activity; ISO:MGI.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
GO; GO:0042594; P:response to starvation; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035148; P:tube formation; IMP:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR022175; BCAS3.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12490; BCAS3; 1.
SUPFAM; SSF50978; SSF50978; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Angiogenesis; Complete proteome;
Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 928 Breast carcinoma-amplified sequence 3
homolog.
/FTId=PRO_0000050884.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9H6U6}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q9H6U6}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9H6U6}.
VAR_SEQ 498 527 LTSQDSYNNFTNNNPGNPRLSPLPSLMVVT -> HFPLMLL
SSRFLLYHLGSDANFYSVCAEHS (in isoform 2).
{ECO:0000269|PubMed:16141072}.
/FTId=VSP_007861.
VAR_SEQ 528 928 Missing (in isoform 2).
{ECO:0000269|PubMed:16141072}.
/FTId=VSP_007862.
CONFLICT 75 75 R -> Q (in Ref. 1; BAC27862).
{ECO:0000305}.
CONFLICT 472 472 T -> D (in Ref. 2). {ECO:0000305}.
SEQUENCE 928 AA; 101021 MW; EF8FE46CF7011A7B CRC64;
MNETMATDSP RRPSRCTGGV VVRPQAVTEQ SYMESVVTFL QDVVPQAYSG SPLTEEKEKI
VWVRFENADL NDTSRNLEFH ELHSTGNEPP LLVMIGYSDG MQVWGIPISG EAQELFSVRH
GPVRAARILP APQLGAQKCD NFAEKRPLLG VCKSIGSSGT TPPYCCVDLY SLRTGEMVKS
IQFKTPIYDL HCNKRILVVV LQEKIAAFDS CTFTKKFFVT SCYPCPGPNM NPIALGSRWL
AYAENKLIRC HQSRGGACGD NIQSYTATVL SAAKTLKSGL TMVGKVVTQL TGTLPSGVTE
DDVALHCNSR RSPLVPGIIT VIDTETVGEG QVLVSEDSDS DGIVAHFPAH EKPVCCMAFN
TSGMLLVTTD TLGHDFHVFQ ILTHPWSSSQ CAVHHLYTLH RGETEAKVQD ICFSHDCRWV
VVSTLRGTSH VFPINPYGGQ PCVRTHMSPR VVNRMSRFQK SAGLEEIEQE LTSKQGGRCS
PVPGLSSSPS GSPLHGKLTS QDSYNNFTNN NPGNPRLSPL PSLMVVTPLA QIKQPMTLGT
ITKRTGPYLF GAGCFSIKAP CKVKSPPQIS PSKSMGGEFC VAAVFGTSRS WFANNAGLKR
EKDQSKQVVV ESLYIISCYG TLVEHMIEPR PISTAPKISD DTPLEIMTSP RASWTLVRTP
QWNELQPPFN ANHPLLLAAE AVQYYQLLLA GSLPPGSPGP ITRHGSYDSL ASDHSGQEDE
EWLSQVEIVT HTGPHRRLWM GPQFHFKTIQ TSGQTTVIST SSSVLQSHGP SDTPQPLLDF
DTDDLDLNSL RIQPVRSDPV SMPGSSRAVS DRRGVSTVTD AASGTFDRSV TLLEVCGSWP
EGFGLRHMSS MEHSEEGLRE RLADAMAESP SRDVVGSGTE LQREGSIETL SNSSGSTSGS
IPRNFDGYRS PLPTNESQPL SLFPTGFP


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