ID ABRA_HUMAN Reviewed; 381 AA.
AC Q8N0Z2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 146.
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|EMBL:AAI05106.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:AAM27268.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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:BAC03948.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:BAC03948.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4] {ECO:0000312|EMBL:AAI05104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 -!- INTERACTION:
CC Q8N0Z2; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-3893380, EBI-2557469;
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 -!- 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; AF503617; AAM27268.1; -; mRNA.
DR EMBL; AK092694; BAC03948.1; -; mRNA.
DR EMBL; AL833422; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC105103; AAI05104.1; -; mRNA.
DR EMBL; BC105105; AAI05106.1; -; mRNA.
DR CCDS; CCDS6305.1; -.
DR RefSeq; NP_631905.1; NM_139166.4.
DR AlphaFoldDB; Q8N0Z2; -.
DR SMR; Q8N0Z2; -.
DR BioGRID; 126483; 36.
DR IntAct; Q8N0Z2; 3.
DR STRING; 9606.ENSP00000311436; -.
DR iPTMnet; Q8N0Z2; -.
DR PhosphoSitePlus; Q8N0Z2; -.
DR BioMuta; ABRA; -.
DR DMDM; 74728477; -.
DR MassIVE; Q8N0Z2; -.
DR PaxDb; 9606-ENSP00000311436; -.
DR PeptideAtlas; Q8N0Z2; -.
DR ProteomicsDB; 71491; -.
DR Antibodypedia; 2925; 102 antibodies from 20 providers.
DR DNASU; 137735; -.
DR Ensembl; ENST00000311955.4; ENSP00000311436.3; ENSG00000174429.4.
DR GeneID; 137735; -.
DR KEGG; hsa:137735; -.
DR MANE-Select; ENST00000311955.4; ENSP00000311436.3; NM_139166.5; NP_631905.1.
DR UCSC; uc003ymm.5; human.
DR AGR; HGNC:30655; -.
DR CTD; 137735; -.
DR DisGeNET; 137735; -.
DR GeneCards; ABRA; -.
DR HGNC; HGNC:30655; ABRA.
DR HPA; ENSG00000174429; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MIM; 609747; gene.
DR neXtProt; NX_Q8N0Z2; -.
DR OpenTargets; ENSG00000174429; -.
DR PharmGKB; PA143485290; -.
DR VEuPathDB; HostDB:ENSG00000174429; -.
DR eggNOG; KOG3376; Eukaryota.
DR GeneTree; ENSGT00390000015984; -.
DR HOGENOM; CLU_062244_0_0_1; -.
DR InParanoid; Q8N0Z2; -.
DR OMA; DEPKWRS; -.
DR OrthoDB; 4166202at2759; -.
DR PhylomeDB; Q8N0Z2; -.
DR TreeFam; TF328879; -.
DR PathwayCommons; Q8N0Z2; -.
DR SignaLink; Q8N0Z2; -.
DR BioGRID-ORCS; 137735; 12 hits in 1146 CRISPR screens.
DR GeneWiki; ABRA_(gene); -.
DR GenomeRNAi; 137735; -.
DR Pharos; Q8N0Z2; Tbio.
DR PRO; PR:Q8N0Z2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8N0Z2; Protein.
DR Bgee; ENSG00000174429; Expressed in skeletal muscle tissue of rectus abdominis and 106 other cell types or tissues.
DR Genevisible; Q8N0Z2; HS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR GO; GO:0030017; C:sarcomere; ISS:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; ISS:HGNC-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:HGNC-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:HGNC-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.10.1540; Costar domain; 1.
DR InterPro; IPR026111; Abra.
DR InterPro; IPR027817; Costars_dom.
DR InterPro; IPR038095; Costars_sf.
DR PANTHER; PTHR22739:SF20; ACTIN-BINDING RHO-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR22739; STRIATED MUSCLE ACTIVATOR OF RHO-DEPENDENT SIGNALING-RELATED; 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..381
FT /note="Actin-binding Rho-activating protein"
FT /id="PRO_0000247739"
FT REGION 39..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..299
FT /note="Actin-binding 1"
FT /evidence="ECO:0000250"
FT REGION 240..285
FT /note="Interaction with actin"
FT /evidence="ECO:0000250|UniProtKB:Q8BUZ1"
FT REGION 300..381
FT /note="Actin-binding 2"
FT /evidence="ECO:0000250"
FT REGION 352..381
FT /note="Interaction with actin"
FT /evidence="ECO:0000250|UniProtKB:Q8BUZ1"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..154
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 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K7"
SQ SEQUENCE 381 AA; 43117 MW; AC5B8D4D9A267C46 CRC64;
MAPGEKESGE GPAKSALRKI RTATLVISLA RGWQQWANEN SIRQAQEPTG WLPGGTQDSP
QAPKPITPPT SHQKAQSAPK SPPRLPEGHG DGQSSEKAPE VSHIKKKEVS KTVVSKTYER
GGDVSHLSHR YERDAGVLEP GQPENDIDRI LHSHGSPTRR RKCANLVSEL TKGWRVMEQE
EPTWRSDSVD TEDSGYGGEA EERPEQDGVQ VAVVRIKRPL PSQVNRFTEK LNCKAQQKYS
PVGNLKGRWQ QWADEHIQSQ KLNPFSEEFD YELAMSTRLH KGDEGYGRPK EGTKTAERAK
RAEEHIYREM MDMCFIICTM ARHRRDGKIQ VTFGDLFDRY VRISDKVVGI LMRARKHGLV
DFEGEMLWQG RDDHVVITLL K
//
