FRPD1_MOUSE
ID FRPD1_MOUSE Reviewed; 1549 AA.
AC A2AKB4; Q80TN2; Q80XK5; Q8K0C0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FERM and PDZ domain-containing protein 1;
GN Name=Frmpd1; Synonyms=Kiaa0967;
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] OF 107-1549.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-1549.
RC TISSUE=Eye;
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 INTERACTION WITH GPSM2.
RX PubMed=23318951; DOI=10.1016/j.jmb.2013.01.003;
RA Pan Z., Shang Y., Jia M., Zhang L., Xia C., Zhang M., Wang W., Wen W.;
RT "Structural and biochemical characterization of the interaction between LGN
RT and Frmpd1.";
RL J. Mol. Biol. 425:1039-1049(2013).
CC -!- FUNCTION: Stabilizes membrane-bound GPSM1, and thereby promotes its
CC interaction with GNAI1. {ECO:0000250|UniProtKB:Q5SYB0}.
CC -!- SUBUNIT: Interacts with GPSM1 (By similarity). Interacts with GPSM2
CC (PubMed:23318951). {ECO:0000250|UniProtKB:Q5SYB0,
CC ECO:0000269|PubMed:23318951}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5SYB0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5SYB0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5SYB0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q5SYB0}. Note=Found both in the cytoplasm and
CC associated with the cell membrane. {ECO:0000250|UniProtKB:Q5SYB0}.
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DR EMBL; AL772285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122409; BAC65691.1; -; mRNA.
DR EMBL; BC031840; AAH31840.1; -; mRNA.
DR EMBL; BC046469; AAH46469.1; -; mRNA.
DR EMBL; BC051097; AAH51097.1; -; mRNA.
DR CCDS; CCDS38753.1; -.
DR RefSeq; NP_001074641.1; NM_001081172.2.
DR RefSeq; XP_006538238.1; XM_006538175.2.
DR RefSeq; XP_006538239.1; XM_006538176.3.
DR RefSeq; XP_006538240.1; XM_006538177.3.
DR RefSeq; XP_006538241.1; XM_006538178.3.
DR RefSeq; XP_011248387.1; XM_011250085.2.
DR AlphaFoldDB; A2AKB4; -.
DR SMR; A2AKB4; -.
DR BioGRID; 577902; 1.
DR IntAct; A2AKB4; 1.
DR STRING; 10090.ENSMUSP00000103434; -.
DR iPTMnet; A2AKB4; -.
DR PhosphoSitePlus; A2AKB4; -.
DR PaxDb; A2AKB4; -.
DR PeptideAtlas; A2AKB4; -.
DR PRIDE; A2AKB4; -.
DR ProteomicsDB; 271606; -.
DR Antibodypedia; 26299; 108 antibodies from 24 providers.
DR Ensembl; ENSMUST00000044773; ENSMUSP00000047232; ENSMUSG00000035615.
DR Ensembl; ENSMUST00000107804; ENSMUSP00000103434; ENSMUSG00000035615.
DR GeneID; 666060; -.
DR KEGG; mmu:666060; -.
DR UCSC; uc008ssi.1; mouse.
DR CTD; 22844; -.
DR MGI; MGI:2446274; Frmpd1.
DR VEuPathDB; HostDB:ENSMUSG00000035615; -.
DR eggNOG; KOG3552; Eukaryota.
DR GeneTree; ENSGT00950000183035; -.
DR HOGENOM; CLU_003698_0_0_1; -.
DR InParanoid; A2AKB4; -.
DR OMA; ESMDDVC; -.
DR OrthoDB; 30821at2759; -.
DR PhylomeDB; A2AKB4; -.
DR TreeFam; TF316497; -.
DR BioGRID-ORCS; 666060; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Frmpd1; mouse.
DR PRO; PR:A2AKB4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AKB4; protein.
DR Bgee; ENSMUSG00000035615; Expressed in lumbar dorsal root ganglion and 83 other tissues.
DR ExpressionAtlas; A2AKB4; baseline and differential.
DR Genevisible; A2AKB4; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13183; FERM_C_FRMPD1_FRMPD3_FRMPD4; 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; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
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; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..1549
FT /note="FERM and PDZ domain-containing protein 1"
FT /id="PRO_0000306806"
FT DOMAIN 57..135
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 181..496
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 554..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..931
FT /note="Important for interaction with GPSM2"
FT /evidence="ECO:0000250|UniProtKB:Q5SYB0"
FT REGION 1097..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 501
FT /note="H -> L (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="S -> G (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="G -> E (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="V -> L (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1000
FT /note="T -> S (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="V -> VQ (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160
FT /note="Q -> R (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="S -> P (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="V -> A (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="A -> V (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="Missing (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="Q -> H (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="L -> P (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
FT CONFLICT 1431
FT /note="S -> N (in Ref. 2; BAC65691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1549 AA; 169208 MW; 809B6E0EC046CE2D CRC64;
MEELDGSLSQ TRKAHRIEQM VARWLRRSRD SSARAKVAAA DGPPGNPAQA LTPVRHTVTL
DKDVLLQNYG FHISETLPLT VVAVTAGGSA HGKLFPGDQI LQMNNELAED LSCERAADIL
RETEDALSIT VVRCTSGVPK SSFLTEEKRA RLKSNPVKVH FAEEVLVSGH SQGNSLLCMP
NVLKVYLENG QTKAFKFEAN TTVKDIILTV KEKLSIRSIE YFALALEEQY SISRLHLLHE
EELVQQVVER EESQDSRCLF RVSFVPKDPL DLLKEDPVAF EYLYLQSCSD VLQERFAVEM
KCNSALRLAA LHIQERIYAC AQPQKISLKY IEKDWGIENF ISPTLLRNMK GKDIKKAISF
HMKRNQNLLE PRQKQLISAA QLRLNYLQIL GELKTYGGKV FNATLMLQDR ESYIALLVGA
KYGISQIINS KLNIISTLAE FANISRVELT EESEKVSMVK VYLQDVKVLT LLLESSSAKD
LACLIAGYYR LFVDPANSVF HWSGNRRPTH RVSAEEGYES RACSDSEESS EVDCVLEPLS
DRCLVKLSLC RPFAREEQPP GDSPTPEATR RGPSTCGASS MTDSAESEAS DSANTESRGC
RTSGSSESMD ALEEDDLDAC SSSGTSFFHF GPPGFSKGLE TNSQEENSRV ETSGFLCLLD
LGQNANPQCQ KIDGPQGLAS EACSWGPELS MGRLDPRLYE GSRTDYYNLC SSISPGSHLS
DSGSESTASR QGAAPPQWCQ QGWMEAQSGS MLESLGLPAL PPLAFEGGSS DEEYYDAADK
LTPPDTLSGP RAADPSAMRL QSQSRTRGSE ESLHPGPEGG EPSRQGGVKK YAKSLRKRRS
FLQTDHTSQV SFPLEASASQ ENTDDVCYYD REPYLTLTAP SPTVSSLQDM QGEPGLLETK
ALGLLASLRE TKSTNPASRI MEMEPETMET KSVIDSRVSS ISAIRLRIDP SNTENPVTTD
GSSASIPHSP HHSNPGSSSP QAAQVRPFPI VSPDQDPGGT TPKELTAEPE DSTFPLSSDH
PNPDNPGPHH VSQGDTSELG EVRSEIGSES FLINHVQEVI PQITGPLCPG DGPTSGECEV
NSEETALAAD EVQGQLSLDS DREVMHRNGP SLFQKGSGKD LGDSKGDRLD NVPQALDVRA
PAGEINSSLC SEPPATGTGQ TSSDSEGENR EAQEQELLTE LDLAPDFLLP SAFPPETIKA
EQLDRVIGED SVPVSTSQQV CVHTVPSLPK LSPCQEEPRS ADSGHGSPAE SKGDDSPIIC
LPPERSFLCF APESHPEGST SLSRVTSFSF AGINEVAPAE IGIEHCRCQF SYATCFRGLQ
PETEEEDGDP QTHPAAPLTS PPSAGSQVTL PWRAARAYSC TTPLSRKSHI WPEFCSRALR
QLKTTPTNAP EGFVQLTESL LELQDILEAS WGVGNKHPPD KCTLHFSESR SRLCMGSQKL
LASCQHVIRM DQSPEEMQGA VRVTFQHLVQ LAGLCFQFTD CSRCSTRHRE VAGNLRDVVY
TYHQFVEAAK LTCERGYHDF SVKLLARQCT ALTAAVFCLT QKFRASTAL
