OFD1_MOUSE
ID OFD1_MOUSE Reviewed; 1017 AA.
AC Q80Z25;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Centriole and centriolar satellite protein OFD1 {ECO:0000305};
DE AltName: Full=Oral-facial-digital syndrome 1 protein homolog;
GN Name=Ofd1;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12782125; DOI=10.1016/s0888-7543(03)00091-0;
RA Ferrante M.I., Barra A., Truong J.P., Banfi S., Disteche C.M., Franco B.;
RT "Characterization of the OFD1/Ofd1 genes on the human and mouse sex
RT chromosomes and exclusion of Ofd1 for the Xpl mouse mutant.";
RL Genomics 81:560-569(2003).
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 DISRUPTION PHENOTYPE.
RX PubMed=16311594; DOI=10.1038/ng1684;
RA Ferrante M.I., Zullo A., Barra A., Bimonte S., Messaddeq N., Studer M.,
RA Dolle P., Franco B.;
RT "Oral-facial-digital type I protein is required for primary cilia formation
RT and left-right axis specification.";
RL Nat. Genet. 38:112-117(2006).
RN [4]
RP FUNCTION.
RX PubMed=18084282; DOI=10.1038/ncb1670;
RA Corbit K.C., Shyer A.E., Dowdle W.E., Gaulden J., Singla V., Chen M.H.,
RA Chuang P.T., Reiter J.F.;
RT "Kif3a constrains beta-catenin-dependent Wnt signalling through dual
RT ciliary and non-ciliary mechanisms.";
RL Nat. Cell Biol. 10:70-76(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670; SER-747 AND SER-791, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Testis;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-73; ALA-78; GLY-137;
RP 358-LYS--ASP-360 AND SER-435.
RX PubMed=20230748; DOI=10.1016/j.devcel.2009.12.022;
RA Singla V., Romaguera-Ros M., Garcia-Verdugo J.M., Reiter J.F.;
RT "Ofd1, a human disease gene, regulates the length and distal structure of
RT centrioles.";
RL Dev. Cell 18:410-424(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [8]
RP INTERACTION WITH CEP20; KIAA0753 AND PCM1.
RX PubMed=26643951; DOI=10.1093/hmg/ddv488;
RA Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M., Lembo F.,
RA Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P., Kuentz P.,
RA Thevenon J., Burglen L., Faivre L., Riviere J.B., Huynen M.A., Birnbaum D.,
RA Rosnet O., Thauvin-Robinet C.;
RT "OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
RT satellites and centrosomes and is mutated in one individual with oral-
RT facial-digital syndrome.";
RL Hum. Mol. Genet. 25:497-513(2016).
CC -!- FUNCTION: Component of the centrioles controlling mother and daughter
CC centrioles length. Recruits to the centriole IFT88 and centriole distal
CC appendage-specific proteins including CEP164. Involved in the
CC biogenesis of the cilium, a centriole-associated function. The cilium
CC is a cell surface projection found in many vertebrate cells required to
CC transduce signals important for development and tissue homeostasis.
CC Plays an important role in development by regulating Wnt signaling and
CC the specification of the left-right axis. Only OFD1 localized at the
CC centriolar satellites is removed by autophagy, which is an important
CC step in the ciliogenesis regulation. {ECO:0000269|PubMed:18084282,
CC ECO:0000269|PubMed:20230748}.
CC -!- SUBUNIT: Homooligomer. Interacts with LCA5. Interacts with RUVBL1; the
CC interaction is direct and may mediate interaction with the NuA4 histone
CC acetyltransferase complex. Interacts with SDCCAG8; the interaction is
CC direct. Interacts with MAP1LC3B. Interacts with C2CD3; OFD1 may act as
CC a negative regulator of C2CD3. Forms a complex with KIAA0753/OFIP and
CC CEP20/FOR20; the interaction with CEP20 is detected only in the
CC presence of KIAA0753. Interacts with PCM1; this interaction may be
CC mediated by KIAA0753/OFIP (PubMed:26643951). {ECO:0000250,
CC ECO:0000269|PubMed:26643951}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:20230748}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000269|PubMed:24089205}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250|UniProtKB:O75665}. Nucleus
CC {ECO:0000250|UniProtKB:O75665}. Note=Localizes to centriole distal ends
CC and to centriolar satellites (PubMed:20230748, PubMed:24089205).
CC Localization to centrioles and pericentriolar satellites may be
CC mediated by KIAA0753/OFIP (By similarity).
CC {ECO:0000250|UniProtKB:O75665}.
CC -!- DISRUPTION PHENOTYPE: Females die at birth and display severe
CC craniofacial and limb abnormalities associated with disorganization of
CC the brain, reduction of the lungs, defects in the great vessels and
CC cystic kidney. Primary cilia are absent on the luminal surface of
CC glomerular and tubular cells of kidneys. Males die earlier during
CC development of the embryo, display failure of left right axis
CC specification associated with a lack of cilia in the embryonic node.
CC {ECO:0000269|PubMed:16311594}.
CC -!- SIMILARITY: Belongs to the OFD1 family. {ECO:0000305}.
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DR EMBL; AJ438159; CAD27225.1; -; mRNA.
DR EMBL; BC119070; AAI19071.1; -; mRNA.
DR EMBL; BC120487; AAI20488.1; -; mRNA.
DR RefSeq; NP_803178.2; NM_177429.3.
DR AlphaFoldDB; Q80Z25; -.
DR SMR; Q80Z25; -.
DR BioGRID; 231852; 3.
DR IntAct; Q80Z25; 1.
DR STRING; 10090.ENSMUSP00000041744; -.
DR iPTMnet; Q80Z25; -.
DR PhosphoSitePlus; Q80Z25; -.
DR EPD; Q80Z25; -.
DR jPOST; Q80Z25; -.
DR MaxQB; Q80Z25; -.
DR PaxDb; Q80Z25; -.
DR PRIDE; Q80Z25; -.
DR ProteomicsDB; 294271; -.
DR DNASU; 237222; -.
DR GeneID; 237222; -.
DR KEGG; mmu:237222; -.
DR CTD; 8481; -.
DR MGI; MGI:1350328; Ofd1.
DR eggNOG; ENOG502S109; Eukaryota.
DR InParanoid; Q80Z25; -.
DR OrthoDB; 294646at2759; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 237222; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ofd1; mouse.
DR PRO; PR:Q80Z25; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80Z25; protein.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035082; P:axoneme assembly; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:UniProtKB.
DR GO; GO:2000314; P:negative regulation of fibroblast growth factor receptor signaling pathway involved in neural plate anterior/posterior pattern formation; IMP:UniProtKB.
DR InterPro; IPR006594; LisH.
DR Pfam; PF16045; LisH_2; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1017
FT /note="Centriole and centriolar satellite protein OFD1"
FT /id="PRO_0000278573"
FT DOMAIN 69..101
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 609..666
FT /note="Mediates homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..557
FT /evidence="ECO:0000255"
FT COILED 626..659
FT /evidence="ECO:0000255"
FT COILED 895..966
FT /evidence="ECO:0000255"
FT COMPBIAS 725..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75665"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75665"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75665"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75665"
FT MUTAGEN 73
FT /note="S->A: Induces centriole elongation. Impaired IFT88
FT recruitment. Impaired ciliogenesis."
FT /evidence="ECO:0000269|PubMed:20230748"
FT MUTAGEN 78
FT /note="A->T: Induces centriole elongation. Impaired CEP164
FT and IFT88 recruitment. Impaired ciliogenesis."
FT /evidence="ECO:0000269|PubMed:20230748"
FT MUTAGEN 137
FT /note="G->S: Induces centriole elongation. Reduced
FT ciliogenesis."
FT /evidence="ECO:0000269|PubMed:20230748"
FT MUTAGEN 358..360
FT /note="KDD->FSY: Shortened centrioles. Reduced
FT ciliogenesis."
FT /evidence="ECO:0000269|PubMed:20230748"
FT MUTAGEN 435
FT /note="S->R: Induces centriole elongation. Impaired IFT88
FT recruitment. Reduced ciliogenesis."
FT /evidence="ECO:0000269|PubMed:20230748"
SQ SEQUENCE 1017 AA; 117345 MW; F262319D90A4925B CRC64;
MAQSNMPHKS DVLSQDELRK KLYQTFKDRG VLDTLQTQLR NQLIHELMHP VLSGEVKPPS
ISVEGSALLI GASNSLVADH LQRCGYEYSL SVFFPESGLA KEKIFTMQDL LQLIRINPSS
SLYKSLISGF DKENKKGFLM SFLKELAEYY QAKESCDAET QTSTTFPSQV SLAEKFQLID
AQFADGFPHR SKLESLETKL NEYKKEVQHQ LQVEMCHKLK YFREAEITKV KMEERRKYEK
ELAEFQNEFE RTCQAKNEAL ISQEKNSLER IKKHREMESK EIYAQRQLLL NDIALLRGRE
AELKERIETF ELTQKLQEEK IKSEAEALER REQNLKNIED TYDQKLKTEL LKYQLELKDD
YITRTNKLLE EERKNKEKTI HLQEELTVIN SKKEELSKSV KHMKEVELEL ESVKAQFLAI
SKQNHLLNEK VREMSDYSQL KEEKVELQAQ NKLLKLQLEE TRNENLRLLD RITQPPPELV
IFQKELQKTE KAMELEHKDF ETHRQALEKQ LQSEIENSAQ LRTQIAEYDA SVKRLTVQVA
ELKSQLKQTQ IALENEVYRN PKHSLIHSLS GLLLSGKMAP HSEDKSGDFL NVPLEQNKVI
AGAVMSRVPP YVNTATEASS PESDFEFIAS STKAKVRELE QEAERLEKAF RTYYQRATQN
PSTSPQPAKS PPSVNSVAAL RSIASSSMDR PVSAEDRVVS EQPLGDMLKE EMSDMSKAFM
GSVVSRPRRT SSSTRLSSTP HPKSRRSLDN EMYLEGLGRL HMTSSSPLLD RVSASPAASP
SPCPERTAQA SPVPSRHSFS GLPEQNACLY QRQTETQDKS ELSNVDKQSL KDEKFEPPFR
WNKTEQFEAE GLHPAGDMPG IDFAVATQSS RLISYDYPSA VQSQTGEQDE QELWELHMKE
RRQREEQRHN ERQEALERER RELGKLEQER RMIEESLKME MEEELEKSVQ DQKDKSAHCE
NTLEKYMKII QQRQEESNAD KSSKKSGKEC SLVDMMMPSD KDESSPGFSH EEPDDMW
