BIN3_MOUSE
ID BIN3_MOUSE Reviewed; 253 AA.
AC Q9JI08;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Bridging integrator 3;
GN Name=Bin3;
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=11274158; DOI=10.1074/jbc.m101096200;
RA Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F.,
RA Prendergast G.C.;
RT "Human BIN3 complements the F-actin localization defects caused by loss of
RT Hob3p, the fission yeast homolog of Rvs161p.";
RL J. Biol. Chem. 276:21670-21677(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Marcucci M.J., Slepnev V.I., De Camilli P.V.;
RT "A mouse homolog of Saccharomyces cerevisiae RVS161 gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Testis, and Vein;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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).
CC -!- FUNCTION: Involved in cytokinesis and septation where it has a role in
CC the localization of F-actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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DR EMBL; AF271733; AAF76219.1; -; mRNA.
DR EMBL; AF244361; AAK28356.1; -; mRNA.
DR EMBL; AK005992; BAB24356.1; -; mRNA.
DR EMBL; AK040685; BAC30666.1; -; mRNA.
DR EMBL; BC026543; AAH26543.1; -; mRNA.
DR CCDS; CCDS27247.1; -.
DR RefSeq; NP_067303.1; NM_021328.3.
DR AlphaFoldDB; Q9JI08; -.
DR SMR; Q9JI08; -.
DR STRING; 10090.ENSMUSP00000022680; -.
DR iPTMnet; Q9JI08; -.
DR PhosphoSitePlus; Q9JI08; -.
DR EPD; Q9JI08; -.
DR MaxQB; Q9JI08; -.
DR PaxDb; Q9JI08; -.
DR PRIDE; Q9JI08; -.
DR ProteomicsDB; 273614; -.
DR Antibodypedia; 5285; 361 antibodies from 26 providers.
DR DNASU; 57784; -.
DR Ensembl; ENSMUST00000022680; ENSMUSP00000022680; ENSMUSG00000022089.
DR GeneID; 57784; -.
DR KEGG; mmu:57784; -.
DR UCSC; uc007une.1; mouse.
DR CTD; 55909; -.
DR MGI; MGI:1929883; Bin3.
DR VEuPathDB; HostDB:ENSMUSG00000022089; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_090113_1_0_1; -.
DR InParanoid; Q9JI08; -.
DR OMA; TRFCAYF; -.
DR OrthoDB; 1172471at2759; -.
DR PhylomeDB; Q9JI08; -.
DR TreeFam; TF331711; -.
DR BioGRID-ORCS; 57784; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Bin3; mouse.
DR PRO; PR:Q9JI08; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JI08; protein.
DR Bgee; ENSMUSG00000022089; Expressed in granulocyte and 247 other tissues.
DR ExpressionAtlas; Q9JI08; baseline and differential.
DR Genevisible; Q9JI08; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IMP:MGI.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR GO; GO:0009826; P:unidimensional cell growth; ISS:UniProtKB.
DR CDD; cd07590; BAR_Bin3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR037428; Bin3_BAR.
DR Pfam; PF03114; BAR; 1.
DR SMART; SM00721; BAR; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51021; BAR; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; Septation.
FT CHAIN 1..253
FT /note="Bridging integrator 3"
FT /id="PRO_0000192956"
FT DOMAIN 9..232
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..57
FT /evidence="ECO:0000255"
FT COILED 120..151
FT /evidence="ECO:0000255"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 29651 MW; 051928DAB0CB7274 CRC64;
MSWIPFKIGQ PKKQIVSKTV ERDFEREYGK LQQLEEQTKR LQKDMKKSTD ADLAMSKSAV
KISQDLLSNP LCEQDQDFLH MVTALDTAMK RMDAFNQEKV NQIQKTVIEP LKKFSSIFPS
LNMAVKRREQ ALQDYGRLQA KVEKYEEKEK TGPVLAKLHQ AREELRPVRE DFEAKNKQLL
DEMPRFYGSR LDYFQPSFES LIRAQVIYYS EMHKIFGDLT QQLDQPGHSD EQRERENETK
LSELRALSIV ADD
