MKS1_MOUSE
ID MKS1_MOUSE Reviewed; 561 AA.
AC Q5SW45; Q3V3W3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Tectonic-like complex member MKS1 {ECO:0000305};
DE AltName: Full=Meckel syndrome type 1 protein homolog;
GN Name=Mks1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 TISSUE SPECIFICITY.
RX PubMed=16415886; DOI=10.1038/ng1714;
RA Kyttaelae M., Tallila J., Salonen R., Kopra O., Kohlschmidt N.,
RA Paavola-Sakki P., Peltonen L., Kestilae M.;
RT "MKS1, encoding a component of the flagellar apparatus basal body proteome,
RT is mutated in Meckel syndrome.";
RL Nat. Genet. 38:155-157(2006).
RN [4]
RP FUNCTION.
RX PubMed=17185389; DOI=10.1093/hmg/ddl459;
RA Dawe H.R., Smith U.M., Cullinane A.R., Gerrelli D., Cox P., Badano J.L.,
RA Blair-Reid S., Sriram N., Katsanis N., Attie-Bitach T., Afford S.C.,
RA Copp A.J., Kelly D.A., Gull K., Johnson C.A.;
RT "The Meckel-Gruber syndrome proteins MKS1 and meckelin interact and are
RT required for primary cilium formation.";
RL Hum. Mol. Genet. 16:173-186(2007).
RN [5]
RP FUNCTION.
RX PubMed=19515853; DOI=10.1093/hmg/ddp272;
RA Tammachote R., Hommerding C.J., Sinders R.M., Miller C.A., Czarnecki P.G.,
RA Leightner A.C., Salisbury J.L., Ward C.J., Torres V.E., Gattone V.H. II,
RA Harris P.C.;
RT "Ciliary and centrosomal defects associated with mutation and depletion of
RT the Meckel syndrome genes MKS1 and MKS3.";
RL Hum. Mol. Genet. 18:3311-3323(2009).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH B9D1 AND B9D2.
RX PubMed=21763481; DOI=10.1016/j.ajhg.2011.06.003;
RA Dowdle W.E., Robinson J.F., Kneist A., Sirerol-Piquer M.S., Frints S.G.,
RA Corbit K.C., Zaghloul N.A., van Lijnschoten G., Mulders L., Verver D.E.,
RA Zerres K., Reed R.R., Attie-Bitach T., Johnson C.A., Garcia-Verdugo J.M.,
RA Katsanis N., Bergmann C., Reiter J.F.;
RT "Disruption of a ciliary B9 protein complex causes Meckel syndrome.";
RL Am. J. Hum. Genet. 89:94-110(2011).
RN [7]
RP INTERACTION WITH TCTN1; TCTN2; TCTN3; CC2D2A; AHI1 AND B9D1.
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 [8]
RP IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, AND FUNCTION.
RX PubMed=22179047; DOI=10.1038/ncb2410;
RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
RA Sandoval W., Peterson A.S.;
RT "A ciliopathy complex at the transition zone protects the cilia as a
RT privileged membrane domain.";
RL Nat. Cell Biol. 14:61-72(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE TECTONIC-LIKE
RP COMPLEX.
RX PubMed=21725307; DOI=10.1038/ng.891;
RA Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G.,
RA Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L.,
RA Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F.,
RA Reiter J.F.;
RT "A transition zone complex regulates mammalian ciliogenesis and ciliary
RT membrane composition.";
RL Nat. Genet. 43:776-784(2011).
CC -!- FUNCTION: Component of the tectonic-like complex, a complex localized
CC at the transition zone of primary cilia and acting as a barrier that
CC prevents diffusion of transmembrane proteins between the cilia and
CC plasma membranes. Involved in centrosome migration to the apical cell
CC surface during early ciliogenesis. Required for ciliary structure and
CC function, including a role in regulating length and appropriate number
CC through modulating centrosome duplication. Required for cell branching
CC morphology. {ECO:0000269|PubMed:17185389, ECO:0000269|PubMed:19515853,
CC ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex)
CC (PubMed:22179047, PubMed:21725307). Interacts with TMEM107 (By
CC similarity). Interacts with TCTN3, AHI1, TCTN1, TCTN2, CC2D2A
CC (PubMed:21565611). Interacts with FLNA. Interacts with TMEM67 (By
CC similarity). Interacts with B9D1 and B9D2 (PubMed:21763481,
CC PubMed:21565611). {ECO:0000250|UniProtKB:Q9NXB0,
CC ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307,
CC ECO:0000269|PubMed:21763481, ECO:0000269|PubMed:22179047}.
CC -!- INTERACTION:
CC Q5SW45; Q9R1S0: B9d1; NbExp=4; IntAct=EBI-4281059, EBI-5652050;
CC Q5SW45; Q3UK10: B9d2; NbExp=3; IntAct=EBI-4281059, EBI-5652008;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:21725307}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Note=Localizes at the
CC transition zone, a region between the basal body and the ciliary
CC axoneme.
CC -!- TISSUE SPECIFICITY: Widely expressed in embryo at 15.5 dpc, with a
CC relatively strong expression in brain, liver, kidney and digits of the
CC upper limbs. Highly expressed in bronchiolar epithelium.
CC {ECO:0000269|PubMed:16415886}.
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DR EMBL; AK030982; BAE20467.1; -; mRNA.
DR EMBL; AL606805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36271.1; -.
DR RefSeq; NP_001034773.2; NM_001039684.2.
DR AlphaFoldDB; Q5SW45; -.
DR SMR; Q5SW45; -.
DR BioGRID; 237616; 37.
DR CORUM; Q5SW45; -.
DR IntAct; Q5SW45; 22.
DR STRING; 10090.ENSMUSP00000043790; -.
DR iPTMnet; Q5SW45; -.
DR PhosphoSitePlus; Q5SW45; -.
DR MaxQB; Q5SW45; -.
DR PaxDb; Q5SW45; -.
DR PRIDE; Q5SW45; -.
DR ProteomicsDB; 295914; -.
DR Antibodypedia; 18351; 109 antibodies from 20 providers.
DR Ensembl; ENSMUST00000038196; ENSMUSP00000043790; ENSMUSG00000034121.
DR GeneID; 380718; -.
DR KEGG; mmu:380718; -.
DR UCSC; uc007kut.1; mouse.
DR CTD; 54903; -.
DR MGI; MGI:3584243; Mks1.
DR VEuPathDB; HostDB:ENSMUSG00000034121; -.
DR eggNOG; KOG4446; Eukaryota.
DR GeneTree; ENSGT00510000047471; -.
DR HOGENOM; CLU_026711_0_1_1; -.
DR InParanoid; Q5SW45; -.
DR OMA; YEHVLCI; -.
DR OrthoDB; 1091079at2759; -.
DR PhylomeDB; Q5SW45; -.
DR TreeFam; TF323812; -.
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; 380718; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q5SW45; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SW45; protein.
DR Bgee; ENSMUSG00000034121; Expressed in retinal neural layer and 170 other tissues.
DR ExpressionAtlas; Q5SW45; baseline and differential.
DR Genevisible; Q5SW45; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:UniProtKB.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0061009; P:common bile duct development; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:MGI.
DR GO; GO:0060322; P:head development; IMP:MGI.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:1901620; P:regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:MGI.
DR GO; GO:0003271; P:smoothened signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IMP:MGI.
DR InterPro; IPR010796; C2_B9-type_dom.
DR PANTHER; PTHR12968; PTHR12968; 1.
DR Pfam; PF07162; B9-C2; 1.
DR PROSITE; PS51381; C2_B9; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..561
FT /note="Tectonic-like complex member MKS1"
FT /id="PRO_0000225687"
FT DOMAIN 314..442
FT /note="C2 B9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00713"
FT CONFLICT 145
FT /note="T -> N (in Ref. 1; BAE20467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 64416 MW; 2FAD4BAA10B997B3 CRC64;
MAEAVWSTDT GEAVYRSRDP VRNLRLRVHL QRITSSNFLH YQPAAQMGKD LIDLATFRPP
QAASGHRPDE EEEEEVVIGW QEKLFSQFEV DLYQNESACQ SPLDHQYRQE ILKLENSGGR
KNRRIFTYTD SDRYTDLEEY CQKITTSASE VPSFLAERMA NVRRRRQDRR GVEGSKLKSR
IVTWEPSEDF IKNNHAINTP LQTMYIMADL GPYGKLGYKV HEHVLCILKV DSNGVITVKP
DFTGIKGPYR IETEGEKQEH TSAWKYTIDN VSSLAQPEEE EREQRVFKDL YGRHKEYLSS
LVGTDFEMIA PGALRLFVNG EVVSAQGYEY DNLYVHFFVE LPAANWSSPP FQQLSGVTQA
CATKSLGMDK VAYFSFPFTF EAFFLHEDES AESLPEWPVL YCKVLSLDFW QRYRVEGYGA
VVLPATPGSH TLTVSTWRPM ELGLVAELRR FFIGGSLELE DPSYVRIPGT FKGERLSRFG
FRTETTGTVT FRLHCLQQSR AFMESNSLQK QMRSVLDRLE GFSQQSSTHN VLEAFRRARR
RMQEARESLP QDLVSPTGTL T
