ID   F107A_RAT               Reviewed;         131 AA.
AC   M0R3K6;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 2.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Actin-associated protein FAM107A {ECO:0000305};
GN   Name=Fam107a {ECO:0000312|RGD:1306327};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   SUBCELLULAR LOCATION.
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).
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. Mediates polymerization of globular actin to F-actin.
CC       Also binds to, stabilizes and bundles F-actin. Involved in synaptic
CC       function by regulating neurite outgrowth in an actin-dependent manner
CC       and for the acquisition of hippocampus-dependent cognitive function,
CC       such as learning and long-term memory (By similarity). Plays a role in
CC       the actin and microtubule cytoskeleton organization; negatively
CC       regulates focal adhesion (FA) assembly promoting malignant glial cell
CC       migration in an actin-, microtubule- and MAP1A-dependent manner. Also
CC       involved in neuroblastoma G1/S phase cell cycle progression and cell
CC       proliferation inhibition by stimulating ubiquitination of NF-kappa-B
CC       subunit RELA and NF-kappa-B degradation in a COMMD1- and actin-
CC       dependent manner. May play a role in tumor development (By similarity).
CC       {ECO:0000250|UniProtKB:O95990, ECO:0000250|UniProtKB:Q78TU8}.
CC   -!- SUBUNIT: Interacts with ACTB. Interacts with COMMD1; this interaction
CC       stabilizes COMMD1 in the nucleus. Interacts with MAP1A. Interacts with
CC       PRDX1 (By similarity). Interacts with F-actin (By similarity).
CC       {ECO:0000250|UniProtKB:O95990, ECO:0000250|UniProtKB:Q78TU8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95990}.
CC       Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O95990}.
CC       Cell junction, focal adhesion {ECO:0000250|UniProtKB:O95990}. Cell
CC       projection, ruffle membrane {ECO:0000250|UniProtKB:O95990}. Synapse
CC       {ECO:0000250|UniProtKB:Q78TU8}. Cell projection
CC       {ECO:0000269|PubMed:21969592}. Note=Colocalizes with F-actin and COMMD1
CC       in the nucleus. Colocalizes with MAP1A along actin stress fibers and
CC       membrane ruffles. {ECO:0000250|UniProtKB:O95990}.
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DR   EMBL; AABR07017233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07017234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M0R3K6; -.
DR   STRING; 10116.ENSRNOP00000063922; -.
DR   PaxDb; M0R3K6; -.
DR   RGD; 1306327; Fam107a.
DR   VEuPathDB; HostDB:ENSRNOG00000033261; -.
DR   eggNOG; ENOG502RZJK; Eukaryota.
DR   HOGENOM; CLU_122902_2_0_1; -.
DR   InParanoid; M0R3K6; -.
DR   PRO; PR:M0R3K6; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000033261; Expressed in Ammon's horn and 18 other tissues.
DR   ExpressionAtlas; M0R3K6; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS: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; IEA:Ensembl.
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; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR   GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0050890; P:cognition; ISS: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; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
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:RGD.
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   3: Inferred from homology;
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..131
FT                   /note="Actin-associated protein FAM107A"
FT                   /id="PRO_0000444956"
FT   COILED          57..77
FT                   /evidence="ECO:0000255"
FT   MOTIF           61..71
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:O95990"
SQ   SEQUENCE   131 AA;  15930 MW;  179636B120FECC89 CRC64;
     MARAGPEYRE WNSELIKPKK LLNPVKASRS HQELHRELLM NHKRGLGMDR KPELQRVLEH
     RRRNQLIKKK EEELEAKRMQ CPFEQELLRR QQRLNQLENP PQREEDHAPE FIKVRENLRR
     ITTLTSEERA L