ABITM_MOUSE
ID ABITM_MOUSE Reviewed; 193 AA.
AC Q80ZQ9; Q8BWF9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein Abitram {ECO:0000305};
DE AltName: Full=Actin-binding transcription modulator;
DE AltName: Full=Protein Simiate {ECO:0000303|PubMed:24349419};
GN Name=Abitram;
GN Synonyms=Fam206a {ECO:0000312|MGI:MGI:2677850},
GN Simiate {ECO:0000303|PubMed:24349419};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Kidney;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24349419; DOI=10.1371/journal.pone.0083007;
RA Derlig K., Giessl A., Brandstatter J.H., Enz R., Dahlhaus R.;
RT "Identification and characterisation of Simiate, a novel protein linked to
RT the fragile X syndrome.";
RL PLoS ONE 8:E83007-E83007(2013).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN AND G-ACTIN, AND FUNCTION.
RX PubMed=24782708; DOI=10.3389/fncel.2014.00099;
RA Derlig K., Ehrhardt T., Giessl A., Brandstaetter J.H., Enz R., Dahlhaus R.;
RT "Simiate is an Actin binding protein involved in filopodia dynamics and
RT arborization of neurons.";
RL Front. Cell. Neurosci. 8:99-99(2014).
CC -!- FUNCTION: Actin-binding protein that regulates actin polymerization,
CC filopodia dynamics and increases the branching of proximal dendrites of
CC developing neurons. {ECO:0000269|PubMed:24782708}.
CC -!- SUBUNIT: Interacts with F-actin (PubMed:24782708). Interacts with G-
CC actin (PubMed:24782708). {ECO:0000269|PubMed:24782708}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24349419}.
CC Cell projection, lamellipodium {ECO:0000269|PubMed:24782708}. Nucleus
CC {ECO:0000269|PubMed:24782708}. Cell projection, growth cone
CC {ECO:0000269|PubMed:24782708}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24782708}. Note=Localizes to somata and dendrites
CC in cortical neurons. Colocalizes with G- and F-actin in growth cones
CC and proximal dendrites (PubMed:24782708). Colocalizes in the nucleus
CC with PTK2 (PubMed:24782708). {ECO:0000269|PubMed:24782708}.
CC -!- TISSUE SPECIFICITY: Detected (at protein level) in liver, lung, heart,
CC spleen, kidney, and ovaries. In brain expression is higher in the
CC hippocampus, the nuclear layer of the cerebellum, the cortex and the
CC caudoputamen. {ECO:0000269|PubMed:24349419}.
CC -!- SIMILARITY: Belongs to the ABITRAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35079.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK052647; BAC35079.1; ALT_INIT; mRNA.
DR EMBL; AL929577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026590; AAH26590.1; -; mRNA.
DR EMBL; BC048548; AAH48548.2; -; mRNA.
DR CCDS; CCDS38766.1; -.
DR RefSeq; NP_001074889.1; NM_001081420.1.
DR AlphaFoldDB; Q80ZQ9; -.
DR SMR; Q80ZQ9; -.
DR STRING; 10090.ENSMUSP00000047275; -.
DR iPTMnet; Q80ZQ9; -.
DR PhosphoSitePlus; Q80ZQ9; -.
DR EPD; Q80ZQ9; -.
DR MaxQB; Q80ZQ9; -.
DR PaxDb; Q80ZQ9; -.
DR PeptideAtlas; Q80ZQ9; -.
DR PRIDE; Q80ZQ9; -.
DR ProteomicsDB; 277018; -.
DR Antibodypedia; 29387; 54 antibodies from 9 providers.
DR Ensembl; ENSMUST00000045368; ENSMUSP00000047275; ENSMUSG00000038827.
DR GeneID; 230234; -.
DR KEGG; mmu:230234; -.
DR UCSC; uc008sxs.1; mouse.
DR CTD; 54942; -.
DR MGI; MGI:2677850; Abitram.
DR VEuPathDB; HostDB:ENSMUSG00000038827; -.
DR eggNOG; KOG3266; Eukaryota.
DR GeneTree; ENSGT00450000040303; -.
DR HOGENOM; CLU_107323_1_0_1; -.
DR InParanoid; Q80ZQ9; -.
DR OMA; GRPCEDF; -.
DR OrthoDB; 1277002at2759; -.
DR PhylomeDB; Q80ZQ9; -.
DR TreeFam; TF313930; -.
DR BioGRID-ORCS; 230234; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q80ZQ9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80ZQ9; protein.
DR Bgee; ENSMUSG00000038827; Expressed in ear vesicle and 210 other tissues.
DR ExpressionAtlas; Q80ZQ9; baseline and differential.
DR Genevisible; Q80ZQ9; MM.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:UniProtKB.
DR InterPro; IPR039169; Abitram.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR13651; PTHR13651; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Nucleus; Reference proteome.
FT CHAIN 1..193
FT /note="Protein Abitram"
FT /id="PRO_0000291929"
SQ SEQUENCE 193 AA; 21597 MW; 0E9799C058B149E4 CRC64;
MEELRCPEAK LAPPEVVIAT EAPPPSLVDR YFTRWYKADV KGKPCEDHCI LQHSNRICVI
TLAGSHPVLQ SGKAIQRISY QISNNCSRLE NKVSGKFKRG AQFLTELAPL CKIYCSDGEE
YTISSCVRGR LMEVNENILH QPSLLQEKPS TEGYIAVVLP KFEESKSVTE GLLTQQQYEE
VVVKRTNATA TTP
