FTM_MOUSE
ID FTM_MOUSE Reviewed; 1264 AA.
AC Q8CG73; G3X958;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein fantom;
DE AltName: Full=Nephrocystin-8;
DE AltName: Full=RPGR-interacting protein 1-like protein;
DE Short=RPGRIP1-like protein;
GN Name=Rpgrip1l; Synonyms=Ftm, Nphp8;
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 [MRNA], AND FUNCTION.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11956760; DOI=10.1007/s00335-001-2142-7;
RA Peters T., Ausmeier K., Dildrop R., Ruether U.;
RT "The mouse Fused toes (Ft) mutation is the result of a 1.6-Mb deletion
RT including the entire Iroquois B gene cluster.";
RL Mamm. Genome 13:186-188(2002).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10501967; DOI=10.1007/s003359901144;
RA Peters T., Ausmeier K., Ruether U.;
RT "Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft) mouse
RT mutation.";
RL Mamm. Genome 10:983-986(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NPHP4 AND IQCB1.
RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K.,
RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D.,
RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A.,
RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B.,
RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.;
RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes
RT and pathways.";
RL Cell 145:513-528(2011).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22927466; DOI=10.1083/jcb.201111009;
RA Mahuzier A., Gaude H.M., Grampa V., Anselme I., Silbermann F.,
RA Leroux-Berger M., Delacour D., Ezan J., Montcouquiol M., Saunier S.,
RA Schneider-Maunoury S., Vesque C.;
RT "Dishevelled stabilization by the ciliopathy protein Rpgrip1l is essential
RT for planar cell polarity.";
RL J. Cell Biol. 198:927-940(2012).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH PSMD2.
RX PubMed=26150391; DOI=10.1083/jcb.201408060;
RA Gerhardt C., Lier J.M., Burmuehl S., Struchtrup A., Deutschmann K.,
RA Vetter M., Leu T., Reeg S., Grune T., Ruether U.;
RT "The transition zone protein Rpgrip1l regulates proteasomal activity at the
RT primary cilium.";
RL J. Cell Biol. 210:115-133(2015).
CC -!- FUNCTION: Negatively regulates signaling through the G-protein coupled
CC thromboxane A2 receptor (TBXA2R) (By similarity). May be involved in
CC mechanisms like programmed cell death, craniofacial development,
CC patterning of the limbs, and formation of the left-right axis. Involved
CC in the organization of apical junctions; the function is proposed to
CC implicate a NPHP1-4-8 module. Does not seem to be strictly required for
CC ciliogenesis (By similarity). Involved in establishment of planar cell
CC polarity such as in cochlear sensory epithelium and is proposed to
CC implicate stabilization of disheveled proteins (PubMed:22927466).
CC Involved in regulation of proteasomal activity at the primary cilium
CC probably implicating association with PSDM2 (PubMed:26150391).
CC {ECO:0000250|UniProtKB:Q68CZ1, ECO:0000269|PubMed:10501967,
CC ECO:0000269|PubMed:11956760, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:22927466, ECO:0000269|PubMed:26150391}.
CC -!- SUBUNIT: Interacts with NPHP4 and NPHP1; NPHP1, NPHP4 and RPGRIP1L are
CC proposed to form a functional NPHP1-4-8 module localized to cell-cell
CC contacts and the ciliary transition zone; NPHP4 mediates the
CC interaction between NPHP1 and RPGRIP1L. Interacts with IQCB1; the
CC interaction likely requires additional interactors (PubMed:21565611).
CC Interacts with TBXA2R (via C-terminus), RPGR, NEK4. Interacts with
CC NPHP4, INVS and DVL2; proposed to form a complex involved in DVL2
CC stabilization (By similarity). Interacts with PSMD2 (PubMed:26150391).
CC {ECO:0000250|UniProtKB:Q68CZ1, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:26150391}.
CC -!- INTERACTION:
CC Q8CG73; Q8BP00: Iqcb1; NbExp=2; IntAct=EBI-4281130, EBI-4282243;
CC Q8CG73; P59240: Nphp4; NbExp=4; IntAct=EBI-4281130, EBI-4281265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:21565611}. Cytoplasm, cytoskeleton, cilium
CC axoneme. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000269|PubMed:26150391}. Cell junction, tight junction
CC {ECO:0000269|PubMed:21565611}. Note=In cultured renal cells, it
CC localizes diffusely in the cytoplasm but, as cells approach confluence,
CC it accumulates to basolateral tight junctions. Localizes to the ciliary
CC transition zone. {ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:22927466, ECO:0000269|PubMed:26150391}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Not found in heart and
CC skin. {ECO:0000269|PubMed:10501967}.
CC -!- DEVELOPMENTAL STAGE: Expression was detected throughout embryonic
CC development as early as 8.5 dpc. {ECO:0000269|PubMed:10501967}.
CC -!- SIMILARITY: Belongs to the RPGRIP1 family. {ECO:0000305}.
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DR EMBL; AJ344253; CAC87257.1; -; mRNA.
DR EMBL; AC139351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11076.1; -; Genomic_DNA.
DR CCDS; CCDS22520.1; -.
DR RefSeq; NP_775607.2; NM_173431.2.
DR AlphaFoldDB; Q8CG73; -.
DR SMR; Q8CG73; -.
DR BioGRID; 232664; 43.
DR CORUM; Q8CG73; -.
DR IntAct; Q8CG73; 279.
DR STRING; 10090.ENSMUSP00000042702; -.
DR iPTMnet; Q8CG73; -.
DR PhosphoSitePlus; Q8CG73; -.
DR EPD; Q8CG73; -.
DR MaxQB; Q8CG73; -.
DR PaxDb; Q8CG73; -.
DR PeptideAtlas; Q8CG73; -.
DR PRIDE; Q8CG73; -.
DR ProteomicsDB; 267530; -.
DR Antibodypedia; 28413; 112 antibodies from 28 providers.
DR DNASU; 244585; -.
DR Ensembl; ENSMUST00000047783; ENSMUSP00000042702; ENSMUSG00000033282.
DR GeneID; 244585; -.
DR KEGG; mmu:244585; -.
DR UCSC; uc009msp.1; mouse.
DR CTD; 23322; -.
DR MGI; MGI:1920563; Rpgrip1l.
DR VEuPathDB; HostDB:ENSMUSG00000033282; -.
DR eggNOG; ENOG502QSQG; Eukaryota.
DR GeneTree; ENSGT00520000055620; -.
DR HOGENOM; CLU_002108_0_0_1; -.
DR InParanoid; Q8CG73; -.
DR OMA; MKFFNQE; -.
DR OrthoDB; 152378at2759; -.
DR PhylomeDB; Q8CG73; -.
DR TreeFam; TF328883; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 244585; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Rpgrip1l; mouse.
DR PRO; PR:Q8CG73; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CG73; protein.
DR Bgee; ENSMUSG00000033282; Expressed in animal zygote and 66 other tissues.
DR ExpressionAtlas; Q8CG73; baseline and differential.
DR GO; GO:0005879; C:axonemal microtubule; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035253; C:ciliary rootlet; ISO:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031870; F:thromboxane A2 receptor binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0022038; P:corpus callosum development; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0060322; P:head development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0021670; P:lateral ventricle development; IMP:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0021532; P:neural tube patterning; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0043584; P:nose development; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0060039; P:pericardium development; IMP:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR021656; C2-C2_1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041091; RPGRIP1_C.
DR InterPro; IPR031139; RPGRIP1_fam.
DR InterPro; IPR031136; RPGRIP1L.
DR PANTHER; PTHR14240; PTHR14240; 1.
DR PANTHER; PTHR14240:SF4; PTHR14240:SF4; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF11618; C2-C2_1; 1.
DR Pfam; PF18111; RPGR1_C; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1264
FT /note="Protein fantom"
FT /id="PRO_0000291268"
FT DOMAIN 577..714
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 773..897
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 979..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..143
FT /evidence="ECO:0000255"
FT COILED 196..268
FT /evidence="ECO:0000255"
FT COILED 299..454
FT /evidence="ECO:0000255"
FT COILED 488..555
FT /evidence="ECO:0000255"
FT COMPBIAS 1058..1076
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 759
FT /note="N -> S (in Ref. 1; CAC87257)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="K -> R (in Ref. 1; CAC87257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1264 AA; 145000 MW; AA1A5A7F9AC2AD1E CRC64;
MSGPSDETAG DLPVKDTGLN LFGVGGLQET STARTVKTRQ AVSRVSREEL EDRFLRLHDE
NILLKQHARK QEDKIKRMAT KLIRLVNDKK RYERVGGGPK RLGRDVEMEE MIEQLQEKVH
ELERQNEVLK NRLISAKQQL QVQGHRQTSY SRVQARVNTG RRRASASAGS QECPGKGLRF
QNVDEAETVQ PTLTKYSNSL LEEARGEIRN LENVIQSQRG QIEELEHLAE ILKTQLKRKE
NEIELSLLQL REQQATDQRS NIRDNVETIK LHKQLVEKSN ALSVIEGKFI QLQEKQRTLR
ISHDALMANG DELNKQLKEQ RLKCCSLEKQ LHSVRFSERR VEELQDRIND LEKERELLKE
NYDKLYNSAF SAAHEEQWKL KEQQMKVQIA QLETALKSDL TDKTEVLDKL KTERDQNEKL
VQENRDLQLQ CLQQKQRLHE LQSRLKFFNQ ESDINADDLS EALLLIKAQK EQKNGDLSFL
EKVDSKINKD LDRSMKELQA THAETVQELE KTRNMLIMQH KINKDYQMEV ETVTQKMENL
QQDYELKVEQ YVHLLDIRAA RIQKLEAQLK DIAYGTKQYK FKPEIMPDDS VDEFDETIHL
ERGENLFEIH INKVTFSSEV LRASGDKELV TFCTYAFYDF ELQTTPIVRG LYPEYNFTSQ
YLVHVNDLFL QYIQKNTVTL ELHQAHSTDY ETIAACQLRF HEILEKSGRI FCTTSLVGTK
GDIPNFGTVE YWFRLRVPMD QAIRLYRERA KALGYITSNF KKPEKMQLSS QQAATTAQIS
PAESTDGNLN ELHVTVKCCT GLQSRASYLQ PHAYVVYKFF DFPDHDTAIV PSSNDPQFDD
HMCFPVPMNM DLDRYLKSES LSFYVFDDSD TQENIYMGKV NVPLISLAHD KCISGIFELM
DKEKHAAGTI QVILKWKFTY LPPSGSITTE DLGKFVCREE PEAVQRLPPK SSDVTSVVAP
KPKPRQRLTF VDKKVSFADT ISHPSPETSP PPKDIKDSSP EVGPKPENGL SAVAYPSKES
GVAKVEENVG EMQQGKEDDI SFLSEGQLAS GSVASSEDET EITEELEPED EDRSASDSDD
CIIPSSVSTN TKQPSEEIRI EIIALNLNDS QITREDTIQR LFIECRFYSL PAEETPMSLP
KPQSGQWVYY NYSNVIYLDK ENNPAVRDIL KAILQRRELP HRSVRFTVVS DPPEDEQDLE
CEDIGVAHVD LADLFQKGRD IIEQDIDVLD ARTDGGTIGK LKVTVEALHA LRSVYEQNRK
DLEA
