MOONR_HUMAN
ID MOONR_HUMAN Reviewed; 967 AA.
AC Q2KHM9; A8KA11; B7Z479; O94853; Q05D97; Q2KHN0; Q9UG45;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein moonraker {ECO:0000303|PubMed:26297806};
DE Short=MNR {ECO:0000303|PubMed:26297806};
DE AltName: Full=OFD1- and FOPNL-interacting protein {ECO:0000303|PubMed:26643951};
GN Name=KIAA0753;
GN Synonyms=MNR {ECO:0000303|PubMed:26297806},
GN OFIP {ECO:0000303|PubMed:26643951};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ASN-444; PRO-466 AND ARG-896.
RC TISSUE=Tongue, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ASN-444; PRO-466 AND ARG-896.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-967, AND VARIANTS ASN-444;
RP PRO-466 AND ARG-896.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-409; SER-700 AND
RP SER-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
RX PubMed=24613305; DOI=10.1016/j.cub.2014.01.067;
RA Firat-Karalar E.N., Rauniyar N., Yates J.R. III, Stearns T.;
RT "Proximity interactions among centrosome components identify regulators of
RT centriole duplication.";
RL Curr. Biol. 24:664-670(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WDR62 AND PCM1.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [10]
RP INVOLVEMENT IN OFD15, INTERACTION WITH CEP20; OFD1 AND PCM1, SUBCELLULAR
RP LOCATION, AND VARIANT OFD15 631-LYS--THR-967 DEL.
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).
RN [11]
RP INVOLVEMENT IN JBTS38, VARIANT JBTS38 GLY-257, AND FUNCTION.
RX PubMed=28220259; DOI=10.1007/s00439-017-1765-z;
RG NISC Comparative Sequencing Program;
RA Stephen J., Vilboux T., Mian L., Kuptanon C., Sinclair C.M., Yildirimli D.,
RA Maynard D.M., Bryant J., Fischer R., Vemulapalli M., Mullikin J.C.,
RA Huizing M., Gahl W.A., Malicdan M.C.V., Gunay-Aygun M.;
RT "Mutations in KIAA0753 cause Joubert syndrome associated with growth
RT hormone deficiency.";
RL Hum. Genet. 136:399-408(2017).
RN [12]
RP INVOLVEMENT IN SRTD21, AND VARIANTS SRTD21 315-GLN--THR-967 AND
RP 324-ARG--THR-967 DEL.
RX PubMed=29138412; DOI=10.1038/s41598-017-15442-1;
RA Hammarsjoe A., Wang Z., Vaz R., Taylan F., Sedghi M., Girisha K.M.,
RA Chitayat D., Neethukrishna K., Shannon P., Godoy R., Gowrishankar K.,
RA Lindstrand A., Nasiri J., Baktashian M., Newton P.T., Guo L.,
RA Hofmeister W., Pettersson M., Chagin A.S., Nishimura G., Yan L.,
RA Matsumoto N., Nordgren A., Miyake N., Grigelioniene G., Ikegawa S.;
RT "Novel KIAA0753 mutations extend the phenotype of skeletal ciliopathies.";
RL Sci. Rep. 7:15585-15585(2017).
RN [13]
RP VARIANT SRTD21 315-GLN--THR-967 DEL.
RX PubMed=31816441; DOI=10.1016/j.ejmg.2019.103823;
RA Faudi E., Brischoux-Boucher E., Huber C., Dabudyk T., Lenoir M., Baujat G.,
RA Michot C., Van Maldergem L., Cormier-Daire V., Piard J.;
RT "A new case of KIAA0753-related variant of Jeune asphyxiating thoracic
RT dystrophy.";
RL Eur. J. Med. Genet. 63:103823-103823(2020).
RN [14]
RP VARIANT SRTD21 324-ARG--THR-967 DEL.
RX PubMed=33875766; DOI=10.1038/s10038-021-00925-x;
RA Hammarsjoe A., Pettersson M., Chitayat D., Handa A., Anderlid B.M.,
RA Bartocci M., Basel D., Batkovskyte D., Beleza-Meireles A., Conner P.,
RA Eisfeldt J., Girisha K.M., Chung B.H., Horemuzova E., Hyodo H.,
RA Kornejeva L., Lagerstedt-Robinson K., Lin A.E., Magnusson M., Moosa S.,
RA Nayak S.S., Nilsson D., Ohashi H., Ohashi-Fukuda N., Stranneheim H.,
RA Taylan F., Traberg R., Voss U., Wirta V., Nordgren A., Nishimura G.,
RA Lindstrand A., Grigelioniene G.;
RT "High diagnostic yield in skeletal ciliopathies using massively parallel
RT genome sequencing, structural variant screening and RNA analyses.";
RL J. Hum. Genet. 66:995-1008(2021).
CC -!- FUNCTION: Involved in centriole duplication (PubMed:24613305,
CC PubMed:26297806). Positively regulates CEP63 centrosomal localization
CC (PubMed:24613305, PubMed:26297806). Required for WDR62 centrosomal
CC localization and promotes the centrosomal localization of CDK2
CC (PubMed:24613305, PubMed:26297806). May play a role in cilium assembly.
CC {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:28220259}.
CC -!- SUBUNIT: Interacts with CEP63 (PubMed:24613305). Interacts with WDR62
CC (PubMed:26297806). Forms a complex with OFD1 and CEP20/FOR20
CC (PubMed:26643951). Interacts with PCM1 (PubMed:26297806,
CC PubMed:26643951). {ECO:0000269|PubMed:24613305,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26643951}.
CC -!- INTERACTION:
CC Q2KHM9; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-2805604, EBI-5463075;
CC Q2KHM9; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-2805604, EBI-17508719;
CC Q2KHM9; P55201-2: BRPF1; NbExp=3; IntAct=EBI-2805604, EBI-12065306;
CC Q2KHM9; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2805604, EBI-8643161;
CC Q2KHM9; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-2805604, EBI-10175300;
CC Q2KHM9; Q8WUE5: CT55; NbExp=3; IntAct=EBI-2805604, EBI-6873363;
CC Q2KHM9; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2805604, EBI-719941;
CC Q2KHM9; Q96CN9: GCC1; NbExp=3; IntAct=EBI-2805604, EBI-746252;
CC Q2KHM9; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-2805604, EBI-16429135;
CC Q2KHM9; O14964: HGS; NbExp=3; IntAct=EBI-2805604, EBI-740220;
CC Q2KHM9; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2805604, EBI-14069005;
CC Q2KHM9; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-2805604, EBI-743811;
CC Q2KHM9; Q15154: PCM1; NbExp=7; IntAct=EBI-2805604, EBI-741421;
CC Q2KHM9; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-2805604, EBI-16428950;
CC Q2KHM9; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-2805604, EBI-1378139;
CC Q2KHM9; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2805604, EBI-358489;
CC Q2KHM9; P51687: SUOX; NbExp=3; IntAct=EBI-2805604, EBI-3921347;
CC Q2KHM9; Q9BT92: TCHP; NbExp=4; IntAct=EBI-2805604, EBI-740781;
CC Q2KHM9; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-2805604, EBI-10176734;
CC Q2KHM9; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2805604, EBI-739895;
CC Q2KHM9; O43379: WDR62; NbExp=3; IntAct=EBI-2805604, EBI-714790;
CC Q2KHM9; Q8NC26: ZNF114; NbExp=3; IntAct=EBI-2805604, EBI-10265237;
CC Q2KHM9; Q9ULD5: ZNF777; NbExp=3; IntAct=EBI-2805604, EBI-11975599;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:26643951}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:26643951}.
CC Note=Localization to centrioles and pericentriolar satellites may be
CC mediated by interaction with PCM1. {ECO:0000269|PubMed:26643951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2KHM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KHM9-2; Sequence=VSP_023539;
CC -!- DISEASE: Orofaciodigital syndrome 15 (OFD15) [MIM:617127]: A form of
CC orofaciodigital syndrome, a group of heterogeneous disorders
CC characterized by malformations of the oral cavity, face and digits, and
CC associated phenotypic abnormalities that lead to the delineation of
CC various subtypes. OFD15 features include facial dysmorphism, lobulated
CC tongue, clefting of the alveolar ridges, left hand postaxial
CC polydactyly, broad right hallux and left hallux duplication, and
CC intermittent respiratory difficulty. Brain anomalies include vermis
CC hypoplasia with molar tooth sign, agenesis of corpus callosum, and
CC ventricular dilation. OFD15 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:26643951}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Joubert syndrome 38 (JBTS38) [MIM:619476]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS38 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:28220259}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Short-rib thoracic dysplasia 21 without polydactyly (SRTD21)
CC [MIM:619479]: A form of short-rib thoracic dysplasia, a group of
CC autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:29138412, ECO:0000269|PubMed:31816441,
CC ECO:0000269|PubMed:33875766}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34473.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018296; BAA34473.2; ALT_INIT; mRNA.
DR EMBL; AK292876; BAF85565.1; -; mRNA.
DR EMBL; AK296971; BAH12465.1; -; mRNA.
DR EMBL; AC004706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113016; AAI13017.1; -; mRNA.
DR EMBL; BC113017; AAI13018.1; -; mRNA.
DR EMBL; AL080108; CAB45712.1; -; mRNA.
DR CCDS; CCDS42247.1; -. [Q2KHM9-1]
DR CCDS; CCDS86564.1; -. [Q2KHM9-2]
DR PIR; T12550; T12550.
DR RefSeq; NP_055619.2; NM_014804.2. [Q2KHM9-1]
DR RefSeq; XP_006721675.1; XM_006721612.2. [Q2KHM9-2]
DR RefSeq; XP_016880945.1; XM_017025456.1.
DR AlphaFoldDB; Q2KHM9; -.
DR SMR; Q2KHM9; -.
DR BioGRID; 115185; 173.
DR CORUM; Q2KHM9; -.
DR DIP; DIP-61716N; -.
DR IntAct; Q2KHM9; 124.
DR MINT; Q2KHM9; -.
DR STRING; 9606.ENSP00000355250; -.
DR iPTMnet; Q2KHM9; -.
DR PhosphoSitePlus; Q2KHM9; -.
DR BioMuta; KIAA0753; -.
DR DMDM; 296439322; -.
DR OGP; O94853; -.
DR EPD; Q2KHM9; -.
DR jPOST; Q2KHM9; -.
DR MassIVE; Q2KHM9; -.
DR MaxQB; Q2KHM9; -.
DR PaxDb; Q2KHM9; -.
DR PeptideAtlas; Q2KHM9; -.
DR PRIDE; Q2KHM9; -.
DR ProteomicsDB; 61302; -. [Q2KHM9-1]
DR ProteomicsDB; 61303; -. [Q2KHM9-2]
DR Antibodypedia; 5845; 20 antibodies from 8 providers.
DR DNASU; 9851; -.
DR Ensembl; ENST00000361413.8; ENSP00000355250.3; ENSG00000198920.11. [Q2KHM9-1]
DR Ensembl; ENST00000572370.5; ENSP00000460050.1; ENSG00000198920.11. [Q2KHM9-2]
DR GeneID; 9851; -.
DR KEGG; hsa:9851; -.
DR MANE-Select; ENST00000361413.8; ENSP00000355250.3; NM_014804.3; NP_055619.2.
DR UCSC; uc002gde.5; human. [Q2KHM9-1]
DR CTD; 9851; -.
DR DisGeNET; 9851; -.
DR GeneCards; KIAA0753; -.
DR HGNC; HGNC:29110; KIAA0753.
DR HPA; ENSG00000198920; Low tissue specificity.
DR MalaCards; KIAA0753; -.
DR MIM; 617112; gene.
DR MIM; 617127; phenotype.
DR MIM; 619476; phenotype.
DR MIM; 619479; phenotype.
DR neXtProt; NX_Q2KHM9; -.
DR OpenTargets; ENSG00000198920; -.
DR Orphanet; 2754; Orofaciodigital syndrome type 6.
DR PharmGKB; PA142671615; -.
DR VEuPathDB; HostDB:ENSG00000198920; -.
DR eggNOG; ENOG502QQYJ; Eukaryota.
DR GeneTree; ENSGT00390000009714; -.
DR HOGENOM; CLU_012839_0_0_1; -.
DR InParanoid; Q2KHM9; -.
DR OMA; QDACEDY; -.
DR OrthoDB; 651659at2759; -.
DR PhylomeDB; Q2KHM9; -.
DR TreeFam; TF331402; -.
DR PathwayCommons; Q2KHM9; -.
DR SignaLink; Q2KHM9; -.
DR BioGRID-ORCS; 9851; 7 hits in 1085 CRISPR screens.
DR ChiTaRS; KIAA0753; human.
DR GenomeRNAi; 9851; -.
DR Pharos; Q2KHM9; Tdark.
DR PRO; PR:Q2KHM9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q2KHM9; protein.
DR Bgee; ENSG00000198920; Expressed in cortical plate and 177 other tissues.
DR ExpressionAtlas; Q2KHM9; baseline and differential.
DR Genevisible; Q2KHM9; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0007099; P:centriole replication; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0061824; P:cytosolic ciliogenesis; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
DR InterPro; IPR031447; MNR.
DR PANTHER; PTHR15732; PTHR15732; 2.
DR Pfam; PF15718; MNR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Alternative splicing; Ciliopathy; Coiled coil; Cytoplasm;
KW Cytoskeleton; Disease variant; Iron; Iron-sulfur; Joubert syndrome;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..967
FT /note="Protein moonraker"
FT /id="PRO_0000280109"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..967
FT /note="Necessary and sufficient for CEP20-binding"
FT /evidence="ECO:0000269|PubMed:26643951"
FT COILED 616..642
FT /evidence="ECO:0000255"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..299
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023539"
FT VARIANT 201
FT /note="H -> Q (in dbSNP:rs16955985)"
FT /id="VAR_031065"
FT VARIANT 257
FT /note="R -> G (in JBTS38; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28220259"
FT /id="VAR_079381"
FT VARIANT 315..967
FT /note="Missing (in SRTD21)"
FT /evidence="ECO:0000269|PubMed:29138412,
FT ECO:0000269|PubMed:31816441"
FT /id="VAR_086266"
FT VARIANT 324..967
FT /note="Missing (in SRTD21)"
FT /evidence="ECO:0000269|PubMed:29138412,
FT ECO:0000269|PubMed:33875766"
FT /id="VAR_086267"
FT VARIANT 375
FT /note="E -> D (in dbSNP:rs9889363)"
FT /id="VAR_031066"
FT VARIANT 375
FT /note="E -> G (in dbSNP:rs17794522)"
FT /id="VAR_031067"
FT VARIANT 444
FT /note="D -> N (in dbSNP:rs2289643)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031068"
FT VARIANT 466
FT /note="L -> P (in dbSNP:rs2289642)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031069"
FT VARIANT 501
FT /note="V -> M (in dbSNP:rs11868877)"
FT /id="VAR_031070"
FT VARIANT 566
FT /note="P -> L (in dbSNP:rs2304977)"
FT /id="VAR_031071"
FT VARIANT 631..967
FT /note="Missing (in OFD15)"
FT /evidence="ECO:0000269|PubMed:26643951"
FT /id="VAR_086268"
FT VARIANT 896
FT /note="Q -> R (in dbSNP:rs1443417)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031072"
FT CONFLICT 250
FT /note="E -> K (in Ref. 3; BAF85565)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="S -> G (in Ref. 1; BAA34473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 967 AA; 109407 MW; 2245C5246165B8AA CRC64;
MGPGQPASTC VHLAPRTQLD GRSDPKVLQT QNQLQFNRNV PTHSSNLAIR YSCPHAIRIE
KLKHSYNESY HCKDADCRVG PDLGSSVSFS VISQERLSYA VHLARRDVKR RQFEKHIKEH
HLRSQPQSSQ KCGHTKYKIP DHRVERKESK SQAACQCSHQ PSKVEISSSG AKVYLYSSHP
GQSDLTVPNS PPTHDPGLQP HPRIGDHKNI SEQKSLLEVQ RLQKELSSCI HKIEEVTKKD
RLEEALDPDE ERRIRIRRQE QAARSARMLY VLQQQVKEIQ EELDKLSPHK IKHTKKSWAM
SKLAAAHRGA IRALQMFVTQ FTDRGEHPLP ARCKELGSLI RQLSLCSVKL DADPSVPDVV
IDILQQIEAL ESLLEKKLSP KKVKKCFSEI RSRFPIGSQK ALERWPSTSP KGERRPLTAK
DTFPQETSRP SVAKQLLADK YQPDTELPET QRLQSELDVL DADIVLEEGP FILDQSASFK
DEVLAVAKTK AGKKKPVTEN VPFRKKDTLA PARQQGLRKA ERGRQSQPHS KSRVQQTTVS
SRLKMNRQPV KDRKAPWIPP NPTSPPASPK CAAWLKVKTS PRDATKEPLQ QEDPQEESHL
TGAVEHEAAR LAWLDAETSK RLKELEELKA KEIDSMQKQR LDWLDAETSR RTKELNELKA
EEMYRLQQLS VSATHLADKV EEAVLDRLKP LLVKAQRVNS TTEANIHLKD GSSVNTAKAQ
PAQEVAAVDF ESNNIRQLDD FLEDCASELW AVTHAKILGS ETLATVEDSK DSPDLEIMMR
RMEEMEKYQE SVRQRYNKIA YADPRLWMQE ENNDQKISAI SEKPLSPHPI RITKTVDRKD
PAVNIMLERP CNGNSLDESV GTEEGSEKRE APLLSLAEDS QQKEGRAPLF VPPGMQHSIG
DYCSRFEQYL RIISHEAVGS FNPWLIAESF SEELVDEALG AVAAELQDMC EDYAEAVFTS
EFLEAAT
