ABRA_RAT
ID ABRA_RAT Reviewed; 375 AA.
AC Q8K4K7; B0BMV2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Actin-binding Rho-activating protein;
DE AltName: Full=MS1;
DE AltName: Full=Striated muscle activator of Rho-dependent signaling;
DE Short=STARS;
GN Name=Abra {ECO:0000312|RGD:708493}; Synonyms=Ms1 {ECO:0000312|RGD:708493};
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] {ECO:0000305, ECO:0000312|EMBL:AAM94370.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=Wistar Kyoto {ECO:0000312|EMBL:AAM94370.1};
RX PubMed=12067735; DOI=10.1016/s0014-5793(02)02833-8;
RA Mahadeva H., Brooks G., Lodwick D., Chong N.W., Samani N.J.;
RT "ms1, a novel stress-responsive, muscle-specific gene that is up-regulated
RT in the early stages of pressure overload-induced left ventricular
RT hypertrophy.";
RL FEBS Lett. 521:100-104(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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] {ECO:0000305}
RP SUBCELLULAR LOCATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [5]
RP STRUCTURE BY NMR OF 295-375, SUBUNIT, AND ACTIN-BINDING DOMAINS.
RX PubMed=22081479; DOI=10.1002/prot.23201;
RA Fogl C., Puckey L., Hinssen U., Zaleska M., El-Mezgueldi M., Croasdale R.,
RA Bowman A., Matsukawa A., Samani N.J., Savva R., Pfuhl M.;
RT "A structural and functional dissection of the cardiac stress response
RT factor MS1.";
RL Proteins 80:398-409(2012).
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:0000250|UniProtKB:Q8BUZ1}.
CC -!- SUBUNIT: Binds F-actin and ABLIM1, ABLIM2 AND ABLIM3. Interaction with
CC ABLIM2 AND ABLIM3 enhances activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:11983702}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11983702}. Note=Localized to the I-band of the
CC sarcomere and to a lesser extent to the sarcomeric structure between Z-
CC lines.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart and skeletal
CC muscle, and expressed at lower levels in adrenal gland, brain, kidney,
CC liver, and testis. {ECO:0000269|PubMed:12067735}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the left ventricle of embryonic heart
CC and is postnatally up-regulated through to adulthood.
CC {ECO:0000269|PubMed:12067735}.
CC -!- INDUCTION: Up-regulated within 1 hour in the left ventricle following
CC the application of pressure overload by aortic banding.
CC {ECO:0000269|PubMed:12067735}.
CC -!- DOMAIN: The actin-binding domain 1 (ABD1) is intrinsically disordered,
CC and binds to F-actin with higher affinity than ABD2.
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; AF336113; AAM94370.1; -; mRNA.
DR EMBL; BC158575; AAI58576.1; -; mRNA.
DR RefSeq; NP_787038.1; NM_175844.3.
DR PDB; 2KRH; NMR; -; A=295-375.
DR PDBsum; 2KRH; -.
DR AlphaFoldDB; Q8K4K7; -.
DR SMR; Q8K4K7; -.
DR STRING; 10116.ENSRNOP00000010539; -.
DR iPTMnet; Q8K4K7; -.
DR PhosphoSitePlus; Q8K4K7; -.
DR PaxDb; Q8K4K7; -.
DR PRIDE; Q8K4K7; -.
DR Ensembl; ENSRNOT00000010539; ENSRNOP00000010539; ENSRNOG00000007999.
DR GeneID; 286965; -.
DR KEGG; rno:286965; -.
DR UCSC; RGD:708493; rat.
DR CTD; 137735; -.
DR RGD; 708493; Abra.
DR eggNOG; KOG3376; Eukaryota.
DR GeneTree; ENSGT00390000015984; -.
DR HOGENOM; CLU_062244_0_0_1; -.
DR InParanoid; Q8K4K7; -.
DR OMA; DEPKWRS; -.
DR OrthoDB; 782922at2759; -.
DR PhylomeDB; Q8K4K7; -.
DR TreeFam; TF328879; -.
DR EvolutionaryTrace; Q8K4K7; -.
DR PRO; PR:Q8K4K7; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007999; Expressed in skeletal muscle tissue and 9 other tissues.
DR Genevisible; Q8K4K7; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:HGNC.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030017; C:sarcomere; IDA:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; ISS:HGNC.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:HGNC.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:HGNC.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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 3D-structure; Actin-binding; Activator; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport.
FT CHAIN 1..375
FT /note="Actin-binding Rho-activating protein"
FT /id="PRO_0000247741"
FT REGION 37..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..293
FT /note="Actin-binding 1"
FT REGION 234..279
FT /note="Interaction with actin"
FT /evidence="ECO:0000250|UniProtKB:Q8BUZ1"
FT REGION 294..375
FT /note="Actin-binding 2"
FT REGION 346..375
FT /note="Interaction with actin"
FT /evidence="ECO:0000250|UniProtKB:Q8BUZ1"
FT COMPBIAS 76..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 7
FT /note="E -> V (in Ref. 1; AAM94370)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> K (in Ref. 1; AAM94370)"
FT /evidence="ECO:0000305"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2KRH"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:2KRH"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2KRH"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2KRH"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:2KRH"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:2KRH"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:2KRH"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2KRH"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2KRH"
SQ SEQUENCE 375 AA; 42901 MW; 3DFEAEB9970B466F CRC64;
MAPGETEREA GPAKSALQKV RRATLVINLA RGWQQWANEN STRQAQEPAG WLPGATQDLP
HTPKEPGPRQ HAPKPPSPKP DGDREGRGSE EATEVSHIKR KEVTRTVVSK AYERGGDVNY
LSHRYEHDGG VSEAVQPDND IDRILLSHDS PTRRRKCTNL VSELTKGWKV MEQEEPKWKS
DSIDTEDSGY GGDMEERPEQ DVAQVAAARI KRPLHSQANR YSETLNCKAH RKYSQVDNLK
GRWQQWADEH IQSQKLNPFS DEFDYDLAMS TRLHKGDEGY GRPKEGSKTA ERAKRAEEHI
YREIMELCFV IRTMARHRRD GKIQVTFGEL FDRYVRISDK VVGILMRARK HGLVHFEGEM
LWQGKDDHVV ITLLE
