FRPD4_MOUSE
ID FRPD4_MOUSE Reviewed; 1320 AA.
AC A2AFR3; B9EIG4; Q3UHE4; Q3UHI9; Q80U41;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=FERM and PDZ domain-containing protein 4;
DE AltName: Full=PDZ domain-containing protein 10;
DE AltName: Full=PSD-95-interacting regulator of spine morphogenesis;
DE Short=Preso;
GN Name=Frmpd4; Synonyms=Gm196, Kiaa0316, Pdzd10, Pdzk10;
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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-1320.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [6]
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).
CC -!- FUNCTION: Positive regulator of dendritic spine morphogenesis and
CC density. Required for the maintenance of excitatory synaptic
CC transmission. Binds phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000250|UniProtKB:Q14CM0}.
CC -!- SUBUNIT: Interacts (via C-terminus) with DLG1, DLG2, DLG3 and
CC DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the interaction is
CC mediated by the PDZ domain. Interacts with GPSM2 (via TPR repeat
CC region). {ECO:0000250|UniProtKB:Q14CM0}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q14CM0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AFR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AFR3-2; Sequence=VSP_028581;
CC Name=3;
CC IsoId=A2AFR3-3; Sequence=VSP_028582;
CC -!- TISSUE SPECIFICITY: Expressed in various regions of the brain,
CC including cortex, hippocampus, cerebellum, olfactory bulb and medial
CC habenular nucleus. {ECO:0000269|PubMed:19118189}.
CC -!- DOMAIN: The FERM domain mediates the interaction with
CC phosphatidylinositol 4,5-bisphosphate. {ECO:0000250|UniProtKB:Q14CM0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65526.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK147370; BAE27868.1; -; mRNA.
DR EMBL; AK147440; BAE27913.1; -; mRNA.
DR EMBL; AL672186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX546498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139429; AAI39430.1; -; mRNA.
DR EMBL; AK122244; BAC65526.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS41210.1; -. [A2AFR3-3]
DR CCDS; CCDS72470.1; -. [A2AFR3-2]
DR RefSeq; NP_001028502.1; NM_001033330.3. [A2AFR3-3]
DR RefSeq; NP_001277356.1; NM_001290427.1. [A2AFR3-3]
DR RefSeq; NP_001277357.1; NM_001290428.1. [A2AFR3-2]
DR AlphaFoldDB; A2AFR3; -.
DR SMR; A2AFR3; -.
DR IntAct; A2AFR3; 1.
DR STRING; 10090.ENSMUSP00000107777; -.
DR iPTMnet; A2AFR3; -.
DR PhosphoSitePlus; A2AFR3; -.
DR PaxDb; A2AFR3; -.
DR PeptideAtlas; A2AFR3; -.
DR PRIDE; A2AFR3; -.
DR ProteomicsDB; 266862; -. [A2AFR3-1]
DR ProteomicsDB; 266863; -. [A2AFR3-2]
DR ProteomicsDB; 266864; -. [A2AFR3-3]
DR Antibodypedia; 49701; 42 antibodies from 18 providers.
DR Ensembl; ENSMUST00000112145; ENSMUSP00000107773; ENSMUSG00000049176. [A2AFR3-3]
DR Ensembl; ENSMUST00000112149; ENSMUSP00000107777; ENSMUSG00000049176. [A2AFR3-1]
DR Ensembl; ENSMUST00000238211; ENSMUSP00000158917; ENSMUSG00000049176. [A2AFR3-2]
DR Ensembl; ENSMUST00000239138; ENSMUSP00000159190; ENSMUSG00000049176. [A2AFR3-3]
DR GeneID; 333605; -.
DR KEGG; mmu:333605; -.
DR UCSC; uc009uxf.2; mouse. [A2AFR3-1]
DR UCSC; uc009uxg.2; mouse. [A2AFR3-3]
DR CTD; 9758; -.
DR MGI; MGI:3042378; Frmpd4.
DR VEuPathDB; HostDB:ENSMUSG00000049176; -.
DR eggNOG; KOG3552; Eukaryota.
DR GeneTree; ENSGT00950000183035; -.
DR HOGENOM; CLU_002690_0_0_1; -.
DR InParanoid; A2AFR3; -.
DR OrthoDB; 57420at2759; -.
DR PhylomeDB; A2AFR3; -.
DR TreeFam; TF316497; -.
DR BioGRID-ORCS; 333605; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Frmpd4; mouse.
DR PRO; PR:A2AFR3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AFR3; protein.
DR Bgee; ENSMUSG00000049176; Expressed in dentate gyrus of hippocampal formation granule cell and 32 other tissues.
DR ExpressionAtlas; A2AFR3; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13183; FERM_C_FRMPD1_FRMPD3_FRMPD4; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041779; FRMPD1/3/4_FERM_C.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Lipid-binding; Reference proteome;
KW Synapse.
FT CHAIN 1..1320
FT /note="FERM and PDZ domain-containing protein 4"
FT /id="PRO_0000307133"
FT DOMAIN 33..66
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 78..155
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 204..519
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 809..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028581"
FT VAR_SEQ 1..14
FT /note="MDVFSFVKIPKLSS -> MRSHSC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028582"
SQ SEQUENCE 1320 AA; 144978 MW; B8E9FE340BBF7475 CRC64;
MDVFSFVKIP KLSSHRTKSS GWPPPSGTWG LNQVPPYGWE MMTNRDGRDY FINHMTQAIP
FDDPRFDSCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI
VMINDEAVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF
SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK
GIEHFSLMLE QRIEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR
DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW
GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG
GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFTEEESLV
RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN AGTQDTGSEN
KGKHNLLGPD WNCMPQMTTF IGEGEQEAQI TYIDSKQKTV EMTDSTLCPK EHRHLYIDNS
YSSDELNQPL TQPGDAPCEA DYRSLAQRSL LTLSGPDTLK KAQESPRGAK VSFIFGDLAL
DDGMSPPTIG YERMLEENPE MLEKQRNLYI SSANDMKNLD LTPDTDSIQF VANSVYANIG
DVKNFEAPEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LDLSGSSDDI
IDLTTLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDTQSQATSF HEDKEQGSSL
QNEEIPVSLI DAVPTSAEGK CEKGLDPAVV STLEALEALS EEQQKSENSG VAILRAYSPE
SSSDSGNETN SSEMTEGSEL AAAQKQSESL SRMFLATHEG YHPLAEEQTE FPTSKAPSVG
LPPKSSHGLA ARPATDLPPK VVPSKQILHS DHMEMEPETM ETKSVTDYFS KLHMGSVAYS
CTSKRKSKLP EGEGKSPLSG NIPGKKQQGT KIAEIEEDTK GKAGTVSSRD NPHLSTFNLE
RTAFRKDSQR WYVASDGGVV EKSGMEAPAM KVFPRGPGLG NREAEGKEDG TVEGGADDAS
VLGQGDRFLT DMACVASAKD LDNPEDTDSP SCDHATKLSE AEDNVARLCD YHLAKRMSSL
QSEGHFSLQS SQGSSVDTGC GPGSSSSACA TPVESPLCPS MGKHMIPDAS GKGGRYISPE
ERAPGHPNHG ATFEELHPQT EGMCPRMTVP ALHTAINADP LFGTLRDGCH RLPKIKETTV
