ABRA_MOUSE
ID ABRA_MOUSE Reviewed; 375 AA.
AC Q8BUZ1; Q0VB05; Q3UU01; Q8BLH3; Q8K431;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Actin-binding Rho-activating protein;
DE AltName: Full=Striated muscle activator of Rho-dependent signaling;
DE Short=STARS;
GN Name=Abra {ECO:0000312|MGI:MGI:2444891};
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] {ECO:0000305, ECO:0000312|EMBL:AAM28877.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ACTIN, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11983702; DOI=10.1074/jbc.m202216200;
RA Arai A., Spencer J.A., Olson E.N.;
RT "STARS, a striated muscle activator of Rho signaling and serum response
RT factor-dependent transcription.";
RL J. Biol. Chem. 277:24453-24459(2002).
RN [2] {ECO:0000312|EMBL:BAC38297.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38297.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC32252.1}, and
RC Embryonic head {ECO:0000312|EMBL:BAC38297.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15798203; DOI=10.1128/mcb.25.8.3173-3181.2005;
RA Kuwahara K., Barrientos T., Teg Pipes G.C., Li S., Olson E.N.;
RT "Muscle-specific signaling mechanism that links actin dynamics to serum
RT response factor.";
RL Mol. Cell. Biol. 25:3173-3181(2005).
RN [5]
RP INTERACTION WITH ABLIM1; ABLIM2 AND ABLIM3.
RX PubMed=17194709; DOI=10.1074/jbc.m607549200;
RA Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT "Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate
RT with STARS and directly bind F-actin.";
RL J. Biol. Chem. 282:8393-8403(2007).
CC -!- FUNCTION: Acts as an activator of serum response factor (SRF)-dependent
CC transcription possibly by inducing nuclear translocation of MKL1 or
CC MKL2 and through a mechanism requiring Rho-actin signaling.
CC {ECO:0000269|PubMed:11983702, ECO:0000269|PubMed:15798203}.
CC -!- SUBUNIT: Binds F-actin and ABLIM1, ABLIM2 AND ABLIM3. Interaction with
CC ABLIM2 AND ABLIM3 enhances activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized to the I-band of
CC the sarcomere and to a lesser extent to the sarcomeric structure
CC between Z-lines. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in heart and skeletal
CC muscle. {ECO:0000269|PubMed:11983702}.
CC -!- DEVELOPMENTAL STAGE: At 8.75 dpc, expressed in the primitive heart
CC tube. Thereafter, expression is maintained in heart and is also
CC detected in skeletal muscle after 10.5 dpc.
CC {ECO:0000269|PubMed:11983702}.
CC -!- DOMAIN: The actin-binding domain 1 (ABD1) is intrinsically disordered,
CC and binds to F-actin with higher affinity than ABD2. {ECO:0000250}.
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DR EMBL; AF504061; AAM28877.1; -; mRNA.
DR EMBL; AK045186; BAC32252.1; -; mRNA.
DR EMBL; AK081696; BAC38297.1; -; mRNA.
DR EMBL; AK138943; BAE23828.1; -; mRNA.
DR EMBL; BC119198; AAI19199.1; -; mRNA.
DR EMBL; BC120842; AAI20843.1; -; mRNA.
DR CCDS; CCDS27449.1; -.
DR RefSeq; NP_780665.1; NM_175456.4.
DR AlphaFoldDB; Q8BUZ1; -.
DR SMR; Q8BUZ1; -.
DR STRING; 10090.ENSMUSP00000051973; -.
DR iPTMnet; Q8BUZ1; -.
DR PhosphoSitePlus; Q8BUZ1; -.
DR PaxDb; Q8BUZ1; -.
DR PRIDE; Q8BUZ1; -.
DR ProteomicsDB; 286064; -.
DR Antibodypedia; 2925; 94 antibodies from 19 providers.
DR Ensembl; ENSMUST00000054742; ENSMUSP00000051973; ENSMUSG00000042895.
DR GeneID; 223513; -.
DR KEGG; mmu:223513; -.
DR UCSC; uc007vpb.1; mouse.
DR CTD; 137735; -.
DR MGI; MGI:2444891; Abra.
DR VEuPathDB; HostDB:ENSMUSG00000042895; -.
DR eggNOG; KOG3376; Eukaryota.
DR GeneTree; ENSGT00390000015984; -.
DR HOGENOM; CLU_062244_0_0_1; -.
DR InParanoid; Q8BUZ1; -.
DR OMA; DEPKWRS; -.
DR OrthoDB; 782922at2759; -.
DR PhylomeDB; Q8BUZ1; -.
DR TreeFam; TF328879; -.
DR BioGRID-ORCS; 223513; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BUZ1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BUZ1; protein.
DR Bgee; ENSMUSG00000042895; Expressed in interventricular septum and 49 other tissues.
DR Genevisible; Q8BUZ1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HGNC-UCL.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISS:HGNC.
DR GO; GO:0003779; F:actin binding; IDA:HGNC-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:HGNC-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:HGNC-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 1.10.10.1540; -; 1.
DR InterPro; IPR026111; Abra.
DR InterPro; IPR027817; Costars_dom.
DR InterPro; IPR038095; Costars_sf.
DR PANTHER; PTHR22739; PTHR22739; 1.
DR Pfam; PF14705; Costars; 1.
DR SMART; SM01283; Costars; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Activator; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport.
FT CHAIN 1..375
FT /note="Actin-binding Rho-activating protein"
FT /id="PRO_0000247740"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..293
FT /note="Actin-binding 1"
FT /evidence="ECO:0000250"
FT REGION 234..279
FT /note="Interaction with actin"
FT /evidence="ECO:0000269|PubMed:11983702"
FT REGION 294..375
FT /note="Actin-binding 2"
FT /evidence="ECO:0000250"
FT REGION 346..375
FT /note="Interaction with actin"
FT /evidence="ECO:0000269|PubMed:11983702"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K7"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K7"
FT CONFLICT 59
FT /note="L -> V (in Ref. 1; AAM28877)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> H (in Ref. 1; AAM28877)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="T -> P (in Ref. 1; AAM28877)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="L -> V (in Ref. 1; AAM28877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42831 MW; D554BB31F80601F1 CRC64;
MAPGEREREA GPAKSALRKV RTATLVINLA RGWQQWANEN STKQAQEPAG WLPGATHDLP
NAPKEAGPYQ HAPKTLSPKP DRDGEGQHSE EATEVSHIKR KEVTRTVVSK AYERGGDVNY
LSHRYENDGG VSEAIQPEND IDRILLSHDS PTRRRKCTNL VSELTKGWKV MEQEEPTWKS
DSVDTEDSGY GGDMEERPEQ DAAPVAPARI KRPLLSQANR YSETLNCKAH RKYSQVDNLK
GRWQQWADEH VQSQKLNPFS DEFDYDLAMS TRLHKGDEGY GRPKEGSKTA ERAKRAEEHI
YREIMELCFV IRTMARHRRD GKIQVTFGEL FDRYVRISDK VVGILMRARK HGLVHFEGEM
LWQGRDDHVV ITLLE
