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Oral-facial-digital syndrome 1 protein homolog

 OFD1_MOUSE              Reviewed;        1017 AA.
Q80Z25;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
28-FEB-2018, entry version 98.
RecName: Full=Oral-facial-digital syndrome 1 protein homolog;
Name=Ofd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=12782125; DOI=10.1016/S0888-7543(03)00091-0;
Ferrante M.I., Barra A., Truong J.P., Banfi S., Disteche C.M.,
Franco B.;
"Characterization of the OFD1/Ofd1 genes on the human and mouse sex
chromosomes and exclusion of Ofd1 for the Xpl mouse mutant.";
Genomics 81:560-569(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
DISRUPTION PHENOTYPE.
PubMed=16311594; DOI=10.1038/ng1684;
Ferrante M.I., Zullo A., Barra A., Bimonte S., Messaddeq N.,
Studer M., Dolle P., Franco B.;
"Oral-facial-digital type I protein is required for primary cilia
formation and left-right axis specification.";
Nat. Genet. 38:112-117(2006).
[4]
FUNCTION.
PubMed=18084282; DOI=10.1038/ncb1670;
Corbit K.C., Shyer A.E., Dowdle W.E., Gaulden J., Singla V.,
Chen M.H., Chuang P.T., Reiter J.F.;
"Kif3a constrains beta-catenin-dependent Wnt signalling through dual
ciliary and non-ciliary mechanisms.";
Nat. Cell Biol. 10:70-76(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670; SER-747 AND
SER-791, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-73; ALA-78;
GLY-137; 358-LYS--ASP-360 AND SER-435.
PubMed=20230748; DOI=10.1016/j.devcel.2009.12.022;
Singla V., Romaguera-Ros M., Garcia-Verdugo J.M., Reiter J.F.;
"Ofd1, a human disease gene, regulates the length and distal structure
of centrioles.";
Dev. Cell 18:410-424(2010).
[7]
SUBCELLULAR LOCATION.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
[8]
INTERACTION WITH FOPNL; KIAA0753 AND PCM1.
PubMed=26643951; DOI=10.1093/hmg/ddv488;
Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M.,
Lembo F., Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P.,
Kuentz P., Thevenon J., Burglen L., Faivre L., Riviere J.B.,
Huynen M.A., Birnbaum D., Rosnet O., Thauvin-Robinet C.;
"OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
satellites and centrosomes and is mutated in one individual with oral-
facial-digital syndrome.";
Hum. Mol. Genet. 25:497-513(2016).
-!- FUNCTION: Component of the centrioles controlling mother and
daughter centrioles length. Recruits to the centriole IFT88 and
centriole distal appendage-specific proteins including CEP164.
Involved in the biogenesis of the cilium, a centriole-associated
function. The cilium is a cell surface projection found in many
vertebrate cells required to transduce signals important for
development and tissue homeostasis. Plays an important role in
development by regulating Wnt signaling and the specification of
the left-right axis. Only OFD1 localized at the centriolar
satellites is removed by autophagy, which is an important step in
the ciliogenesis regulation. {ECO:0000269|PubMed:18084282,
ECO:0000269|PubMed:20230748}.
-!- SUBUNIT: Homooligomer. Interacts with LCA5. Interacts with RUVBL1;
the interaction is direct and may mediate interaction with the
NuA4 histone acetyltransferase complex. Interacts with SDCCAG8;
the interaction is direct. Interacts with MAP1LC3B. Interacts with
C2CD3; OFD1 may act as a egative regulator of C2CD3. Forms a
complex with KIAA0753/OFIP and FOPNL/FOR20; the interaction with
FOPNL is detected only in the presence of KIAA0753. Interacts with
PCM1; this interaction may be mediated by KIAA0753/OFIP
(PubMed:26643951). {ECO:0000250, ECO:0000269|PubMed:26643951}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:20230748}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriolar satellite
{ECO:0000269|PubMed:24089205}. Cytoplasm, cytoskeleton, cilium
basal body {ECO:0000250|UniProtKB:O75665}. Nucleus
{ECO:0000250|UniProtKB:O75665}. Note=Localizes to centriole distal
ends and to centriolar satellites (PubMed:20230748,
PubMed:24089205). Localization to centrioles and pericentriolar
satellites may be mediated by KIAA0753/OFIP (By similarity).
{ECO:0000250|UniProtKB:O75665}.
-!- DISRUPTION PHENOTYPE: Females die at birth and display severe
craniofacial and limb abnormalities associated with
disorganization of the brain, reduction of the lungs, defects in
the great vessels and cystic kidney. Primary cilia are absent on
the luminal surface of glomerular and tubular cells of kidneys.
Males die earlier during development of the embryo, display
failure of left right axis specification associated with a lack of
cilia in the embryonic node. {ECO:0000269|PubMed:16311594}.
-!- SIMILARITY: Belongs to the OFD1 family. {ECO:0000305}.
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EMBL; AJ438159; CAD27225.1; -; mRNA.
EMBL; BC119070; AAI19071.1; -; mRNA.
EMBL; BC120487; AAI20488.1; -; mRNA.
RefSeq; NP_803178.2; NM_177429.3.
UniGene; Mm.247480; -.
ProteinModelPortal; Q80Z25; -.
SMR; Q80Z25; -.
IntAct; Q80Z25; 1.
STRING; 10090.ENSMUSP00000041744; -.
iPTMnet; Q80Z25; -.
PhosphoSitePlus; Q80Z25; -.
EPD; Q80Z25; -.
MaxQB; Q80Z25; -.
PaxDb; Q80Z25; -.
PRIDE; Q80Z25; -.
GeneID; 237222; -.
KEGG; mmu:237222; -.
CTD; 8481; -.
MGI; MGI:1350328; Ofd1.
eggNOG; ENOG410IJF2; Eukaryota.
eggNOG; ENOG41112K2; LUCA.
HOVERGEN; HBG080238; -.
InParanoid; Q80Z25; -.
KO; K16480; -.
PRO; PR:Q80Z25; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0035082; P:axoneme assembly; IMP:MGI.
GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:UniProtKB.
GO; GO:2000314; P:negative regulation of fibroblast growth factor receptor signaling pathway involved in neural plate anterior/posterior pattern formation; IMP:UniProtKB.
InterPro; IPR006594; LisH.
Pfam; PF16045; LisH_2; 1.
SMART; SM00667; LisH; 1.
PROSITE; PS50896; LISH; 1.
1: Evidence at protein level;
Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 1017 Oral-facial-digital syndrome 1 protein
homolog.
/FTId=PRO_0000278573.
DOMAIN 69 101 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
REGION 609 666 Mediates homooligomerization.
{ECO:0000250}.
COILED 188 557 {ECO:0000255}.
COILED 626 659 {ECO:0000255}.
COILED 895 966 {ECO:0000255}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:O75665}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000250|UniProtKB:O75665}.
MOD_RES 722 722 Phosphoserine.
{ECO:0000250|UniProtKB:O75665}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 791 791 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000250|UniProtKB:O75665}.
MUTAGEN 73 73 S->A: Induces centriole elongation.
Impaired IFT88 recruitment. Impaired
ciliogenesis.
{ECO:0000269|PubMed:20230748}.
MUTAGEN 78 78 A->T: Induces centriole elongation.
Impaired CEP164 and IFT88 recruitment.
Impaired ciliogenesis.
{ECO:0000269|PubMed:20230748}.
MUTAGEN 137 137 G->S: Induces centriole elongation.
Reduced ciliogenesis.
{ECO:0000269|PubMed:20230748}.
MUTAGEN 358 360 KDD->FSY: Shortened centrioles. Reduced
ciliogenesis.
{ECO:0000269|PubMed:20230748}.
MUTAGEN 435 435 S->R: Induces centriole elongation.
Impaired IFT88 recruitment. Reduced
ciliogenesis.
{ECO:0000269|PubMed:20230748}.
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


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