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   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.
DR   Genevisible; Q8N0Z2; HS.
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
//