FRS1L_MOUSE
ID FRS1L_MOUSE Reviewed; 293 AA.
AC B1AXV0; A3KMM1; Q8BYS5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DOMON domain-containing protein FRRS1L;
DE AltName: Full=Ferric-chelate reductase 1-like protein;
DE Flags: Precursor;
GN Name=Frrs1l;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-293.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 IDENTIFICATION IN AMPAR COMPLEX, TOPOLOGY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27236917; DOI=10.1016/j.ajhg.2016.04.008;
RA Madeo M., Stewart M., Sun Y., Sahir N., Wiethoff S., Chandrasekar I.,
RA Yarrow A., Rosenfeld J.A., Yang Y., Cordeiro D., McCormick E.M.,
RA Muraresku C.C., Jepperson T.N., McBeth L.J., Seidahmed M.Z.,
RA El Khashab H.Y., Hamad M., Azzedine H., Clark K., Corrochano S., Wells S.,
RA Elting M.W., Weiss M.M., Burn S., Myers A., Landsverk M., Crotwell P.L.,
RA Waisfisz Q., Wolf N.I., Nolan P.M., Padilla-Lopez S., Houlden H.,
RA Lifton R., Mane S., Singh B.B., Falk M.J., Mercimek-Mahmutoglu S.,
RA Bilguvar K., Salih M.A., Acevedo-Arozena A., Kruer M.C.;
RT "Loss-of-function mutations in FRRS1L lead to an epileptic-dyskinetic
RT encephalopathy.";
RL Am. J. Hum. Genet. 98:1249-1255(2016).
CC -!- FUNCTION: Important modulator of glutamate signaling pathway.
CC {ECO:0000250|UniProtKB:Q9P0K9}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents. Alone or in combination, these auxiliary
CC subunits control the gating and pharmacology of the AMPAR complex and
CC profoundly impact their biogenesis and protein processing.
CC {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22632720}.
CC Synapse {ECO:0000305|PubMed:22632720}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:22632720). In embryos expression is evident in the ventral
CC forebrain, but a lower level is seen in the remainder of the embryos.
CC In the adult brain, expressed in the cortex, cerebellum, hippocampus
CC and basal ganglia (PubMed:27236917). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:27236917}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 12.5 dpc embryos.
CC {ECO:0000269|PubMed:27236917}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI32346.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL831761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132345; AAI32346.1; ALT_INIT; mRNA.
DR EMBL; AK038461; BAC30008.1; -; mRNA.
DR CCDS; CCDS51179.1; -.
DR RefSeq; NP_001136437.1; NM_001142965.1.
DR AlphaFoldDB; B1AXV0; -.
DR BioGRID; 230949; 3.
DR STRING; 10090.ENSMUSP00000052507; -.
DR iPTMnet; B1AXV0; -.
DR PhosphoSitePlus; B1AXV0; -.
DR SwissPalm; B1AXV0; -.
DR PaxDb; B1AXV0; -.
DR PeptideAtlas; B1AXV0; -.
DR PRIDE; B1AXV0; -.
DR ProteomicsDB; 267525; -.
DR Antibodypedia; 71944; 74 antibodies from 17 providers.
DR Ensembl; ENSMUST00000053681; ENSMUSP00000052507; ENSMUSG00000045589.
DR GeneID; 230235; -.
DR KEGG; mmu:230235; -.
DR UCSC; uc008sxx.2; mouse.
DR CTD; 23732; -.
DR MGI; MGI:2442704; Frrs1l.
DR VEuPathDB; HostDB:ENSMUSG00000045589; -.
DR eggNOG; KOG4293; Eukaryota.
DR GeneTree; ENSGT00940000159043; -.
DR HOGENOM; CLU_069383_1_0_1; -.
DR InParanoid; B1AXV0; -.
DR OMA; HDIDNPP; -.
DR OrthoDB; 1060739at2759; -.
DR PhylomeDB; B1AXV0; -.
DR TreeFam; TF316169; -.
DR BRENDA; 1.16.1.10; 3474.
DR BioGRID-ORCS; 230235; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Frrs1l; mouse.
DR PRO; PR:B1AXV0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AXV0; protein.
DR Bgee; ENSMUSG00000045589; Expressed in cerebellar vermis and 131 other tissues.
DR ExpressionAtlas; B1AXV0; baseline and differential.
DR Genevisible; B1AXV0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045505; F:dynein intermediate chain binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IMP:MGI.
DR GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR042789; FRRS1L.
DR PANTHER; PTHR46902; PTHR46902; 1.
DR SMART; SM00664; DoH; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..293
FT /note="DOMON domain-containing protein FRRS1L"
FT /id="PRO_0000420688"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 119..234
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32507 MW; D9E9C806D57915AA CRC64;
MAGQPLRRPA WVPLLLRLLL AGIAACDASP ADDSAGPGGR GPRGRARGDA GADEAVPRHD
SSYGTFASEF YDLRYLSEEG YPFPTAPPVD PFAKIKVEDC GRTKGCFRYG KPGCNAETCD
YFLSYRMIGA DVEFELSADT DGWVAVGFSS DKKMGGDDVM ACVHDDNGRV RIQHFYNVGQ
WAKEVQRNPA RDEEGVFENN RVTCRFKRPV NVPRDETIVD LHLSWYYLFA WGPAIQGAIT
RHDIDSPPAS ERVVSIYKYE DIFMPSAAYQ TFSSPFCLLL IVALTFYLLM GTP
