ABRA_PIG
ID ABRA_PIG Reviewed; 384 AA.
AC B5SNZ6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Actin-binding Rho-activating protein;
DE AltName: Full=Striated muscle activator of Rho-dependent signaling;
DE Short=STARS;
GN Name=ABRA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=18726684; DOI=10.1007/s10528-008-9178-2;
RA Peng Y.B., Guan H.P., Fan B., Zhao S.H., Xu X.W., Li K., Zhu M.J.,
RA Yerle M., Liu B.;
RT "Molecular characterization and expression pattern of the porcine STARS, a
RT striated muscle-specific expressed gene.";
RL Biochem. Genet. 46:644-651(2008).
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}.
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 {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: Specifically expressed in heart and skeletal
CC muscles. {ECO:0000269|PubMed:18726684}.
CC -!- DEVELOPMENTAL STAGE: Expression increase gradually from 33 dpc (days
CC post-coitum) to postnatal muscles, and peaks at 28 days postnatal.
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; DQ536197; ABG00262.1; -; mRNA.
DR RefSeq; NP_001129432.1; NM_001135960.2.
DR AlphaFoldDB; B5SNZ6; -.
DR SMR; B5SNZ6; -.
DR IntAct; B5SNZ6; 1.
DR STRING; 9823.ENSSSCP00000006449; -.
DR PaxDb; B5SNZ6; -.
DR Ensembl; ENSSSCT00005021245; ENSSSCP00005012715; ENSSSCG00005013617.
DR Ensembl; ENSSSCT00015048398; ENSSSCP00015019244; ENSSSCG00015036376.
DR Ensembl; ENSSSCT00025089178; ENSSSCP00025039006; ENSSSCG00025064982.
DR Ensembl; ENSSSCT00030018633; ENSSSCP00030008252; ENSSSCG00030013589.
DR Ensembl; ENSSSCT00035084200; ENSSSCP00035035006; ENSSSCG00035062655.
DR Ensembl; ENSSSCT00045040820; ENSSSCP00045028372; ENSSSCG00045023911.
DR Ensembl; ENSSSCT00060044091; ENSSSCP00060018809; ENSSSCG00060032554.
DR Ensembl; ENSSSCT00070017535; ENSSSCP00070014531; ENSSSCG00070009047.
DR GeneID; 100154546; -.
DR KEGG; ssc:100154546; -.
DR CTD; 137735; -.
DR eggNOG; KOG3376; Eukaryota.
DR InParanoid; B5SNZ6; -.
DR OrthoDB; 782922at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 4.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Actin-binding; Activator; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport.
FT CHAIN 1..384
FT /note="Actin-binding Rho-activating protein"
FT /id="PRO_0000367810"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..302
FT /note="Actin-binding 1"
FT /evidence="ECO:0000250"
FT REGION 243..288
FT /note="Interaction with actin"
FT /evidence="ECO:0000250"
FT REGION 303..384
FT /note="Actin-binding 2"
FT /evidence="ECO:0000250"
FT REGION 355..384
FT /note="Interaction with actin"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K7"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K7"
SQ SEQUENCE 384 AA; 43569 MW; B9567FD832675C3B CRC64;
MARGEKGRGE GPAKSALRKV RTATLVINLA RGWQQWANEN STRQAQEPTG WMPGGARESD
QPSGPVIHPT THQKVQSAPK SPSPKPGGYG AGQSSEGATE VSPIKRKEVT KTIVSKAYER
GGDVSHLSHR YEKDGDEPEP EQPESDIDRL LRSHGSPTRR RKCANLVSEL TKGWKEMEQE
EQEELKCRSD SIDTEDSGYG GETEERPEQD GEQVAIARIK RPLPSQANRF TEKLNCKAQR
KYSQVGHLKG RWQQWADEHI QSQKLNPFSD EFDYELAMST RLHKGDEGYG RPKEGTRTAE
RAKRAEEHIY REIMDMCFII RTMAHPRRDG KIQVTFGDLF DRYVRISDKV VGILMRARKH
GLVDFEGEML WQGRDDHVVI TLLK
