BCAS1_MOUSE
ID BCAS1_MOUSE Reviewed; 633 AA.
AC Q80YN3; A2AVX2; Q9CVA1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Breast carcinoma-amplified sequence 1 homolog;
DE AltName: Full=Novel amplified in breast cancer 1 homolog;
GN Name=Bcas1; Synonyms=Nabc1;
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=14567997; DOI=10.1016/s0014-4827(03)00353-7;
RA Beardsley D.I., Kowbel D., Lataxes T.A., Mannino J.M., Xin H., Kim W.-J.,
RA Collins C., Brown K.D.;
RT "Characterization of the novel amplified in breast cancer-1 (NABC1) gene
RT product.";
RL Exp. Cell Res. 290:402-413(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-633.
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-425;
RP SER-443; THR-523; SER-525 AND SER-615, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28230289; DOI=10.1002/glia.23129;
RA Ishimoto T., Ninomiya K., Inoue R., Koike M., Uchiyama Y., Mori H.;
RT "Mice lacking BCAS1, a novel myelin-associated protein, display
RT hypomyelination, schizophrenia-like abnormal behaviors, and upregulation of
RT inflammatory genes in the brain.";
RL Glia 65:727-739(2017).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=29212715; DOI=10.1126/scitranslmed.aam7816;
RA Fard M.K., van der Meer F., Sanchez P., Cantuti-Castelvetri L., Mandad S.,
RA Jaekel S., Fornasiero E.F., Schmitt S., Ehrlich M., Starost L.,
RA Kuhlmann T., Sergiou C., Schultz V., Wrzos C., Brueck W., Urlaub H.,
RA Dimou L., Stadelmann C., Simons M.;
RT "BCAS1 expression defines a population of early myelinating
RT oligodendrocytes in multiple sclerosis lesions.";
RL Sci. Transl. Med. 9:0-0(2017).
CC -!- FUNCTION: Required for myelination. {ECO:0000269|PubMed:28230289}.
CC -!- SUBUNIT: Homodimer. Interacts with DYNLL1 and DYNLL2.
CC {ECO:0000250|UniProtKB:O75363, ECO:0000250|UniProtKB:Q3ZB98}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZB98}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and, more
CC specifically, in oligodendrocytes. Expressed in the Schwann cells (at
CC protein level). {ECO:0000269|PubMed:28230289,
CC ECO:0000269|PubMed:29212715}.
CC -!- DISRUPTION PHENOTYPE: Mice display hypomyelination, schizophrenia-like
CC behavioral abnormalities and a tendency toward reduced anxiety-like
CC behaviors and up-regulation of inflammatory genes in the brain.
CC {ECO:0000269|PubMed:28230289}.
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DR EMBL; AY219233; AAO88011.1; -; mRNA.
DR EMBL; AL928812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK008957; BAB25989.1; -; mRNA.
DR CCDS; CCDS17121.1; -.
DR RefSeq; NP_084091.2; NM_029815.2.
DR AlphaFoldDB; Q80YN3; -.
DR BioGRID; 218429; 4.
DR IntAct; Q80YN3; 3.
DR MINT; Q80YN3; -.
DR STRING; 10090.ENSMUSP00000013667; -.
DR iPTMnet; Q80YN3; -.
DR PhosphoSitePlus; Q80YN3; -.
DR MaxQB; Q80YN3; -.
DR PaxDb; Q80YN3; -.
DR PeptideAtlas; Q80YN3; -.
DR PRIDE; Q80YN3; -.
DR ProteomicsDB; 277190; -.
DR Antibodypedia; 28750; 178 antibodies from 26 providers.
DR DNASU; 76960; -.
DR Ensembl; ENSMUST00000013667; ENSMUSP00000013667; ENSMUSG00000013523.
DR GeneID; 76960; -.
DR KEGG; mmu:76960; -.
DR UCSC; uc008obx.2; mouse.
DR CTD; 8537; -.
DR MGI; MGI:1924210; Bcas1.
DR VEuPathDB; HostDB:ENSMUSG00000013523; -.
DR eggNOG; ENOG502QTR2; Eukaryota.
DR GeneTree; ENSGT00390000003167; -.
DR HOGENOM; CLU_031051_0_0_1; -.
DR InParanoid; Q80YN3; -.
DR OMA; EPAQCAE; -.
DR OrthoDB; 1009953at2759; -.
DR PhylomeDB; Q80YN3; -.
DR TreeFam; TF335555; -.
DR BioGRID-ORCS; 76960; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Slc4a11; mouse.
DR PRO; PR:Q80YN3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80YN3; protein.
DR Bgee; ENSMUSG00000013523; Expressed in cerebellar nuclear complex and 152 other tissues.
DR ExpressionAtlas; Q80YN3; baseline and differential.
DR Genevisible; Q80YN3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR InterPro; IPR026115; NABC1.
DR PANTHER; PTHR15016; PTHR15016; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..633
FT /note="Breast carcinoma-amplified sequence 1 homolog"
FT /id="PRO_0000235984"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..633
FT /note="Interacts with DYNLL1 AND DYNLL2"
FT /evidence="ECO:0000250|UniProtKB:Q3ZB98"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZB98"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZB98"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZB98"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 122
FT /note="G -> E (in Ref. 1; AAO88011)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> E (in Ref. 3; BAB25989)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="H -> R (in Ref. 1; AAO88011)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="P -> S (in Ref. 1; AAO88011)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="S -> L (in Ref. 1; AAO88011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 67378 MW; 53DBECB3581A245D CRC64;
MGNQMSVPLR PGDQEHDPGA DTCKVTSDNE CVQNGNPVVL STRVIQHYEE VDLGISSSKD
NVATSSPKTM EAQAVGDASG KNLGKEAKTK APAARSHFFL TLSRPVPGRP GDQGTDSSAA
SGRFDVSPSA APENKDPSEH GALPVAAAPG QAPDKTPGCP EAKQQTLPAT GPLAPSPPES
QAEAPAQDKD FGFLNRFFKL DKGRESAPVN SQPKEAKGSE DPEQATEAPA VPGNPHGVSA
GEDIVDSEQR GQDVDTLSYS VPGDPEVPGT TKEDPQVVDT TENSSSIMSF FKTLVSPNKT
ETKKDPEDTK ATKADSVCDG HAAGQKMSET QAKSKKKRLD SPRLGLSFRK LFRHKDTENS
PTTSANLKSD KANFTPQETR GKTKATKSCS PPPPPPEPTS EGRDSGKEKA GPTSLPLGKL
FWKKSVKEDT LSTGAEENAV CESPVETVRL EEVESSLQTV DLSEETQPEP TDVKVKEESK
PRKTPLMAFL RQMSVRSSEG IPRSEESNVK DSSCQTSNSV EKTPSPPEPE PAGTAQKNKE
TSSSKDKKSV DKKSATENSK QKNGKQEVRE PAPCVQPPTV EANAMQTGDK TPKKSEKRRQ
SLGGFLKGLG PKRMSDAQVQ TDPVSIGPVG KSK
