BCAS1_RAT
ID BCAS1_RAT Reviewed; 589 AA.
AC Q3ZB98; F1LN49; Q52KK0; Q5TLG8; Q5TLG9; Q5TLH0; Q5TLH1; Q8K4U9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Breast carcinoma-amplified sequence 1 homolog;
DE AltName: Full=Protein whose mRNA is enriched in synaptosomes 2;
DE Short=Pmes-2;
GN Name=Bcas1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-589 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-589 (ISOFORM 3).
RC TISSUE=Brain, and Prostate;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-589 (ISOFORM 6), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12427555; DOI=10.1016/s0167-4781(02)00538-9;
RA Ishimoto T., Ninomiya K., Miyaji K., Uyeda A., Kasai M., Taguchi T.;
RT "Cloning and characterization of a novel synaptosome-enriched mRNA that
RT encodes 31 kDa protein.";
RL Biochim. Biophys. Acta 1579:189-195(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-589 (ISOFORMS 2; 3; 4 AND 5), INTERACTION
RP WITH DYNLL1 AND DYNLL2, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=16133941; DOI=10.1007/s10571-005-4955-5;
RA Ninomiya K., Ishimoto T., Taguchi T.;
RT "Subcellular localization of PMES-2 proteins regulated by their two
RT cytoskeleton-associated domains.";
RL Cell. Mol. Neurobiol. 25:899-911(2005).
RN [5]
RP PROTEIN SEQUENCE OF 323-338, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-192; SER-314;
RP THR-480; SER-482 AND SER-557, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Required for myelination. {ECO:0000250|UniProtKB:Q80YN3}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with DYNLL1 and DYNLL2
CC (PubMed:16133941). {ECO:0000250|UniProtKB:O75363,
CC ECO:0000269|PubMed:16133941}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16133941}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PMES-2A;
CC IsoId=Q3ZB98-1; Sequence=Displayed;
CC Name=2; Synonyms=PMES-2E;
CC IsoId=Q3ZB98-2; Sequence=VSP_018551;
CC Name=3; Synonyms=PMES-2C;
CC IsoId=Q3ZB98-3; Sequence=VSP_018548, VSP_018550;
CC Name=4; Synonyms=PMES-2D;
CC IsoId=Q3ZB98-4; Sequence=VSP_018548, VSP_018549;
CC Name=5; Synonyms=PMES-2B;
CC IsoId=Q3ZB98-5; Sequence=VSP_018548;
CC Name=6; Synonyms=band83;
CC IsoId=Q3ZB98-6; Sequence=VSP_018548, VSP_018551;
CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex and cerebellum, but
CC not in other organs. {ECO:0000269|PubMed:12427555}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC01271.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC01271.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD69785.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD69785.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD69786.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD69786.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD69787.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD69787.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD69788.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD69788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AABR07054732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094306; AAH94306.1; -; mRNA.
DR EMBL; BC103480; AAI03481.1; -; mRNA.
DR EMBL; AB029897; BAC01271.1; ALT_SEQ; mRNA.
DR EMBL; AB180269; BAD69785.1; ALT_SEQ; mRNA.
DR EMBL; AB180270; BAD69786.1; ALT_SEQ; mRNA.
DR EMBL; AB180271; BAD69787.1; ALT_SEQ; mRNA.
DR EMBL; AB180272; BAD69788.1; ALT_SEQ; mRNA.
DR RefSeq; NP_663703.3; NM_145670.4. [Q3ZB98-1]
DR AlphaFoldDB; Q3ZB98; -.
DR STRING; 10116.ENSRNOP00000051984; -.
DR iPTMnet; Q3ZB98; -.
DR PhosphoSitePlus; Q3ZB98; -.
DR SwissPalm; Q3ZB98; -.
DR PaxDb; Q3ZB98; -.
DR PRIDE; Q3ZB98; -.
DR Ensembl; ENSRNOT00000055111; ENSRNOP00000051984; ENSRNOG00000012906. [Q3ZB98-1]
DR Ensembl; ENSRNOT00000115742; ENSRNOP00000094246; ENSRNOG00000012906. [Q3ZB98-2]
DR GeneID; 246755; -.
DR KEGG; rno:246755; -.
DR CTD; 8537; -.
DR RGD; 628644; Bcas1.
DR eggNOG; ENOG502QTR2; Eukaryota.
DR GeneTree; ENSGT00390000003167; -.
DR HOGENOM; CLU_031051_0_0_1; -.
DR InParanoid; Q3ZB98; -.
DR OMA; EPAQCAE; -.
DR OrthoDB; 1009953at2759; -.
DR PhylomeDB; Q3ZB98; -.
DR PRO; PR:Q3ZB98; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012906; Expressed in Ammon's horn and 12 other tissues.
DR ExpressionAtlas; Q3ZB98; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR InterPro; IPR026115; NABC1.
DR PANTHER; PTHR15016; PTHR15016; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..589
FT /note="Breast carcinoma-amplified sequence 1 homolog"
FT /id="PRO_0000235985"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..589
FT /note="Interacts with DYNLL1 AND DYNLL2"
FT /evidence="ECO:0000269|PubMed:16133941"
FT COMPBIAS 194..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YN3"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 309
FT /note="T -> MKATKADSVCDGHAGQKMSETQAKSKKKRLDSPRLGLSFRKFFRHK
FT (in isoform 3, isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12427555,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16133941"
FT /id="VSP_018548"
FT VAR_SEQ 381..472
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16133941"
FT /id="VSP_018549"
FT VAR_SEQ 395..472
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16133941"
FT /id="VSP_018550"
FT VAR_SEQ 395..450
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12427555,
FT ECO:0000303|PubMed:16133941"
FT /id="VSP_018551"
FT CONFLICT 309
FT /note="T -> M (in Ref. 4; BAD69788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 62382 MW; 6919B3C87C0898F6 CRC64;
MGNQMSVPLR PGDQEHDPEA DTYKVTSDNE CVQNGIPVVV STRVIQHYEE VDLGINSLKD
NVPASSPETM EAHAVADASG KNLGKGSKPK APAARSHFFL TLSRPVPGRP GDQGTDSSAA
SGRLDVSPGT APENKDPSEH GALPVAAAPG PAPDKTPGCT EAKQQTLPAT SPLAPSPPES
QAEAPSRPKD FSFLNRLFKL DKGRESAPAD SPPEEGKGSK SQERAIEAPA VPGNPHGVSA
GKDIVDSEER KQEVDTLSYS VPADPEVLGT TKEDPQVVDA TENSNSIMSF FKTLVSPNKT
ETKKDPEDTD AENSPTTPAN LKSDKADLTP QETQGTAKSS KGSSQPGQAP SAGTSDTARE
GGKEKAGPTS LPLGKLFWKK SVKEDSLSTG AEENAVCEPP VETVRLEEVE STLQTVDLTE
KETQTEPTDV KVKEESKPRR TPLMAFLRQM SVRGSEGITR SEESNGKDSS CQTSNSTEKT
PSPPEPEPAG TAQKNKETSS KDKKSVDKKS AAESNKQKNG KPEAREPAPC VQQPTVEVNA
LQTGDKTPKR SEKRRQSLGG FLKGLGPKRM LDAQVQTDPV SIGPVGKSK
