BRK1_MOUSE
ID BRK1_MOUSE Reviewed; 75 AA.
AC Q91VR8; Q3TLB8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein BRICK1;
DE Short=BRK1;
GN Name=Brk1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, and Wolffian duct;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [4]
RP FUNCTION OF WAVE1 COMPLEX.
RX PubMed=27605705; DOI=10.1091/mbc.e16-05-0326;
RA Xu C., Fu X., Zhu S., Liu J.J.;
RT "Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-induced
RT TrkB endocytosis and dendrite outgrowth.";
RL Mol. Biol. Cell 27:3342-3356(2016).
CC -!- FUNCTION: Involved in regulation of actin and microtubule organization.
CC Part of a WAVE complex that activates the Arp2/3 complex (By
CC similarity). As component of the WAVE1 complex, required for BDNF-NTRK2
CC endocytic trafficking and signaling from early endosomes
CC (PubMed:27605705). {ECO:0000250|UniProtKB:Q8WUW1,
CC ECO:0000269|PubMed:27605705}.
CC -!- SUBUNIT: Homotrimer when in free form. Directly interacts with WASF2.
CC Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2,
CC BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1 (By similarity). {ECO:0000250|UniProtKB:Q8WUW1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRK1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK020128; BAC25616.1; -; mRNA.
DR EMBL; AK150689; BAE29768.1; -; mRNA.
DR EMBL; AK163236; BAE37248.1; -; mRNA.
DR EMBL; AK166585; BAE38874.1; -; mRNA.
DR EMBL; BC010582; AAH10582.1; -; mRNA.
DR CCDS; CCDS39595.1; -.
DR RefSeq; NP_598698.1; NM_133937.1.
DR AlphaFoldDB; Q91VR8; -.
DR SMR; Q91VR8; -.
DR BioGRID; 221634; 10.
DR IntAct; Q91VR8; 3.
DR MINT; Q91VR8; -.
DR STRING; 10090.ENSMUSP00000041644; -.
DR iPTMnet; Q91VR8; -.
DR PhosphoSitePlus; Q91VR8; -.
DR EPD; Q91VR8; -.
DR MaxQB; Q91VR8; -.
DR PaxDb; Q91VR8; -.
DR PeptideAtlas; Q91VR8; -.
DR PRIDE; Q91VR8; -.
DR ProteomicsDB; 273703; -.
DR Antibodypedia; 53142; 97 antibodies from 23 providers.
DR DNASU; 101314; -.
DR Ensembl; ENSMUST00000035725; ENSMUSP00000041644; ENSMUSG00000033940.
DR GeneID; 101314; -.
DR KEGG; mmu:101314; -.
DR UCSC; uc009dgz.1; mouse.
DR CTD; 55845; -.
DR MGI; MGI:1915406; Brk1.
DR VEuPathDB; HostDB:ENSMUSG00000033940; -.
DR eggNOG; ENOG502S3PY; Eukaryota.
DR GeneTree; ENSGT00390000011082; -.
DR HOGENOM; CLU_175202_0_0_1; -.
DR InParanoid; Q91VR8; -.
DR OMA; MPCCCWE; -.
DR OrthoDB; 1579787at2759; -.
DR PhylomeDB; Q91VR8; -.
DR TreeFam; TF324876; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 101314; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Brk1; mouse.
DR PRO; PR:Q91VR8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91VR8; protein.
DR Bgee; ENSMUSG00000033940; Expressed in renal medulla collecting duct and 256 other tissues.
DR Genevisible; Q91VR8; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR033378; BRICK1.
DR PANTHER; PTHR33668; PTHR33668; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WUW1"
FT CHAIN 2..75
FT /note="Protein BRICK1"
FT /id="PRO_0000283647"
FT COILED 41..72
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUW1"
FT CONFLICT 71
FT /note="G -> D (in Ref. 1; BAE38874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 75 AA; 8761 MW; 637B43D779A36587 CRC64;
MAGQEDPVQR EIHQDWANRE YIEIITSSIK KISDFLNSFD MSCRSRLATL NEKLTALERR
IEYIEARVTK GETLT
