F107A_MOUSE
ID F107A_MOUSE Reviewed; 144 AA.
AC Q78TU8;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Actin-associated protein FAM107A {ECO:0000305};
GN Name=Fam107a {ECO:0000312|MGI:MGI:3041256};
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=Retina;
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 TISSUE=Brain {ECO:0000312|EMBL:AAH55107.1};
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 FUNCTION, INTERACTION WITH ACTB; F-ACTIN AND PRDX1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21969592; DOI=10.1073/pnas.1103318108;
RA Schmidt M.V., Schuelke J.P., Liebl C., Stiess M., Avrabos C., Bock J.,
RA Wochnik G.M., Davies H.A., Zimmermann N., Scharf S.H., Truembach D.,
RA Wurst W., Zieglgaensberger W., Turck C., Holsboer F., Stewart M.G.,
RA Bradke F., Eder M., Mueller M.B., Rein T.;
RT "Tumor suppressor down-regulated in renal cell carcinoma 1 (DRR1) is a
RT stress-induced actin bundling factor that modulates synaptic efficacy and
RT cognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17213-17218(2011).
RN [5]
RP INDUCTION.
RX PubMed=25637808; DOI=10.1016/j.neuroscience.2015.01.026;
RA Masana M., Jukic M.M., Kretzschmar A., Wagner K.V., Westerholz S.,
RA Schmidt M.V., Rein T., Brodski C., Mueller M.B.;
RT "Deciphering the spatio-temporal expression and stress regulation of
RT Fam107B, the paralog of the resilience-promoting protein DRR1 in the mouse
RT brain.";
RL Neuroscience 290:147-158(2015).
CC -!- FUNCTION: Stress-inducible actin-binding protein that plays a role in
CC synaptic and cognitive functions by modulating actin filamentous (F-
CC actin) dynamics (PubMed:21969592). Mediates polymerization of globular
CC actin to F-actin (PubMed:21969592). Also binds to, stabilizes and
CC bundles F-actin (PubMed:21969592). Involved in synaptic function by
CC regulating neurite outgrowth in an actin-dependent manner and for the
CC acquisition of hippocampus-dependent cognitive function, such as
CC learning and long-term memory (PubMed:21969592). Plays a role in the
CC actin and microtubule cytoskeleton organization; negatively regulates
CC focal adhesion (FA) assembly promoting malignant glial cell migration
CC in an actin-, microtubule- and MAP1A-dependent manner. Also involved in
CC neuroblastoma G1/S phase cell cycle progression and cell proliferation
CC inhibition by stimulating ubiquitination of NF-kappa-B subunit RELA and
CC NF-kappa-B degradation in a COMMD1- and actin-dependent manner. May
CC play a role in tumor development (By similarity).
CC {ECO:0000250|UniProtKB:O95990, ECO:0000269|PubMed:21969592}.
CC -!- SUBUNIT: Interacts with ACTB (PubMed:21969592). Interacts with F-actin
CC (PubMed:21969592). Interacts with PRDX1 (PubMed:21969592). Interacts
CC with COMMD1; this interaction stabilizes COMMD1 in the nucleus (By
CC similarity). Interacts with MAP1A (By similarity).
CC {ECO:0000250|UniProtKB:O95990, ECO:0000269|PubMed:21969592}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95990}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:21969592}.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:O95990}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:O95990}. Synapse
CC {ECO:0000269|PubMed:21969592}. Note=Colocalizes with F-actin
CC (PubMed:21969592). Colocalizes with F-actin and COMMD1 in the nucleus.
CC Colocalizes with MAP1A along actin stress fibers and membrane ruffles
CC (By similarity). {ECO:0000250|UniProtKB:O95990,
CC ECO:0000269|PubMed:21969592}.
CC -!- TISSUE SPECIFICITY: Expressed in septum, the neocortex, the CA3 region
CC of the hippocampus and the cerebellum (at protein level).
CC {ECO:0000269|PubMed:21969592}.
CC -!- INDUCTION: Up-regulated in the hypothalamic paraventricular nucleus
CC (PVN) and the CA3 region of the hippocampus of the brain in response to
CC postnatal maternal separation or food deprivation and glucocorticoids
CC stimulation in adult animals (PubMed:21969592). Up-regulated in CA1,
CC CA3 and dente gyrus regions of the hippocampus in response to acute
CC social defeat stress or glucocorticoids stimulation (PubMed:25637808).
CC {ECO:0000269|PubMed:21969592, ECO:0000269|PubMed:25637808}.
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; AK044219; BAC31824.1; -; mRNA.
DR EMBL; CT025547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055107; AAH55107.1; -; mRNA.
DR CCDS; CCDS26813.1; -.
DR RefSeq; NP_899010.1; NM_183187.3.
DR RefSeq; XP_006518083.1; XM_006518020.2.
DR RefSeq; XP_006518084.1; XM_006518021.2.
DR RefSeq; XP_006518085.1; XM_006518022.2.
DR RefSeq; XP_006518086.1; XM_006518023.2.
DR AlphaFoldDB; Q78TU8; -.
DR SMR; Q78TU8; -.
DR STRING; 10090.ENSMUSP00000045513; -.
DR PhosphoSitePlus; Q78TU8; -.
DR PaxDb; Q78TU8; -.
DR PRIDE; Q78TU8; -.
DR ProteomicsDB; 338990; -.
DR Antibodypedia; 31675; 137 antibodies from 21 providers.
DR Ensembl; ENSMUST00000036070; ENSMUSP00000045513; ENSMUSG00000021750.
DR Ensembl; ENSMUST00000121887; ENSMUSP00000114015; ENSMUSG00000021750.
DR GeneID; 268709; -.
DR KEGG; mmu:268709; -.
DR UCSC; uc007sfa.1; mouse.
DR CTD; 11170; -.
DR MGI; MGI:3041256; Fam107a.
DR VEuPathDB; HostDB:ENSMUSG00000021750; -.
DR eggNOG; ENOG502RZJK; Eukaryota.
DR GeneTree; ENSGT00390000011228; -.
DR InParanoid; Q78TU8; -.
DR OMA; MNHRRGI; -.
DR OrthoDB; 1491333at2759; -.
DR PhylomeDB; Q78TU8; -.
DR TreeFam; TF325943; -.
DR BioGRID-ORCS; 268709; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fam107a; mouse.
DR PRO; PR:Q78TU8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q78TU8; protein.
DR Bgee; ENSMUSG00000021750; Expressed in otolith organ and 199 other tissues.
DR ExpressionAtlas; Q78TU8; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IMP:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:UniProtKB.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR InterPro; IPR009533; FAM107.
DR PANTHER; PTHR16768; PTHR16768; 1.
DR Pfam; PF06625; DUF1151; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell cycle; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Growth regulation; Membrane; Nucleus;
KW Reference proteome; Stress response; Synapse.
FT CHAIN 1..144
FT /note="Actin-associated protein FAM107A"
FT /id="PRO_0000444955"
FT REGION 104..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..90
FT /evidence="ECO:0000255"
FT MOTIF 74..84
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O95990"
SQ SEQUENCE 144 AA; 17510 MW; BFD0BB9754817054 CRC64;
MYSEIQRERA DIEGLMARPE YREWNSELIK PKKLLNPVKA SRSHQELHRE LLMNHKRGLG
MDSKPELQRV LEHRRRNQLI KKKEEELEAK RMQCPFKQEL LRRQQRLNQL ENPPQRDEDH
APEFIKVREN LRRITTLTSE ERAL
