TM107_MOUSE
ID TM107_MOUSE Reviewed; 140 AA.
AC Q9CPV0; B2RPS9; Q5SUQ6; Q9CZ71;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transmembrane protein 107 {ECO:0000250|UniProtKB:Q6UX40};
GN Name=Tmem107 {ECO:0000312|MGI:MGI:1914160};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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 [4]
RP FUNCTION, INVOLVEMENT IN SCHLEI, AND VARIANT SCHLEI GLY-125.
RX PubMed=22698544; DOI=10.1016/j.ydbio.2012.06.008;
RA Christopher K.J., Wang B., Kong Y., Weatherbee S.D.;
RT "Forward genetics uncovers Transmembrane protein 107 as a novel factor
RT required for ciliogenesis and Sonic hedgehog signaling.";
RL Dev. Biol. 368:382-392(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT SCHLEI
RP GLY-125.
RX PubMed=26518474; DOI=10.1002/humu.22925;
RA Shylo N.A., Christopher K.J., Iglesias A., Daluiski A., Weatherbee S.D.;
RT "TMEM107 Is a Critical Regulator of Ciliary Protein Composition and Is
RT Mutated in Orofaciodigital Syndrome.";
RL Hum. Mutat. 37:155-159(2016).
RN [6]
RP FUNCTION.
RX PubMed=26595381; DOI=10.1038/ncb3273;
RA Lambacher N.J., Bruel A.L., van Dam T.J., Szymanska K., Slaats G.G.,
RA Kuhns S., McManus G.J., Kennedy J.E., Gaff K., Wu K.M., van der Lee R.,
RA Burglen L., Doummar D., Riviere J.B., Faivre L., Attie-Bitach T.,
RA Saunier S., Curd A., Peckham M., Giles R.H., Johnson C.A., Huynen M.A.,
RA Thauvin-Robinet C., Blacque O.E.;
RT "TMEM107 recruits ciliopathy proteins to subdomains of the ciliary
RT transition zone and causes Joubert syndrome.";
RL Nat. Cell Biol. 18:122-131(2016).
CC -!- FUNCTION: Plays a role in cilia formation and embryonic patterning.
CC Requires for normal Sonic hedgehog (Shh) signaling in the neural tube
CC and acts in combination with GLI2 and GLI3 to pattern ventral and
CC intermediate neuronal cell types. During ciliogenesis regulates the
CC ciliary transition zone localization of some MKS complex proteins
CC (PubMed:26595381, PubMed:26518474). {ECO:0000269|PubMed:22698544,
CC ECO:0000269|PubMed:26518474, ECO:0000269|PubMed:26595381}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC Interacts with TMEM237, TMEM231, MKS1 and TMEM216.
CC {ECO:0000250|UniProtKB:Q6UX40}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell projection, cilium. Note=Localizes at the
CC transition zone, a region between the basal body and the ciliary
CC axoneme. {ECO:0000269|PubMed:26518474}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CPV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CPV0-2; Sequence=VSP_021214;
CC -!- DISEASE: Note=Defect in TMEM107 is the cause of the schlei phenotype.
CC Schlei mice display Shh-related defects including, preaxial
CC polydactyly, exencephaly, and disrupted ventral neural tube patterning.
CC Mice shown decreased numbers of cilia in several developing tissues and
CC organs. However, nodal cilia appear normal in schlei mutants and
CC subsequently, no left-right defects are observed.
CC {ECO:0000269|PubMed:22698544}.
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DR EMBL; AK003403; BAB22768.1; -; mRNA.
DR EMBL; AK012938; BAB28560.1; -; mRNA.
DR EMBL; AK154279; BAE32485.1; -; mRNA.
DR EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096686; AAH96686.1; -; mRNA.
DR EMBL; BC120499; AAI20500.1; -; mRNA.
DR EMBL; BC137584; AAI37585.1; -; mRNA.
DR CCDS; CCDS24879.1; -. [Q9CPV0-1]
DR CCDS; CCDS24880.1; -. [Q9CPV0-2]
DR RefSeq; NP_080114.1; NM_025838.2. [Q9CPV0-1]
DR RefSeq; NP_082612.2; NM_028336.3. [Q9CPV0-2]
DR AlphaFoldDB; Q9CPV0; -.
DR IntAct; Q9CPV0; 1.
DR STRING; 10090.ENSMUSP00000091624; -.
DR GlyGen; Q9CPV0; 1 site.
DR PaxDb; Q9CPV0; -.
DR PRIDE; Q9CPV0; -.
DR ProteomicsDB; 259209; -. [Q9CPV0-1]
DR ProteomicsDB; 259210; -. [Q9CPV0-2]
DR Antibodypedia; 42946; 50 antibodies from 18 providers.
DR Ensembl; ENSMUST00000075980; ENSMUSP00000075363; ENSMUSG00000020895. [Q9CPV0-1]
DR Ensembl; ENSMUST00000094081; ENSMUSP00000091624; ENSMUSG00000020895. [Q9CPV0-2]
DR GeneID; 66910; -.
DR KEGG; mmu:66910; -.
DR UCSC; uc007jpc.2; mouse. [Q9CPV0-1]
DR UCSC; uc007jpd.2; mouse. [Q9CPV0-2]
DR CTD; 84314; -.
DR MGI; MGI:1914160; Tmem107.
DR VEuPathDB; HostDB:ENSMUSG00000020895; -.
DR eggNOG; ENOG502RZG7; Eukaryota.
DR GeneTree; ENSGT00390000014827; -.
DR HOGENOM; CLU_127745_0_0_1; -.
DR InParanoid; Q9CPV0; -.
DR OMA; ERWECTM; -.
DR OrthoDB; 1508335at2759; -.
DR PhylomeDB; Q9CPV0; -.
DR TreeFam; TF328441; -.
DR BioGRID-ORCS; 66910; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9CPV0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CPV0; protein.
DR Bgee; ENSMUSG00000020895; Expressed in nasal cavity epithelium and 226 other tissues.
DR Genevisible; Q9CPV0; MM.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:MGI.
DR GO; GO:0003127; P:detection of nodal flow; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
DR GO; GO:0021532; P:neural tube patterning; IMP:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:1904491; P:protein localization to ciliary transition zone; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR InterPro; IPR029248; TMEM107.
DR PANTHER; PTHR34341; PTHR34341; 1.
DR Pfam; PF14995; TMEM107; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Developmental protein; Disease variant; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..140
FT /note="Transmembrane protein 107"
FT /id="PRO_0000254542"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 118..140
FT /note="SAFPAVTETALFIAVFGLKKKPF -> RCPSTQYFGMGGGGGKSIPNLKVSP
FT T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021214"
FT VARIANT 125
FT /note="E -> G (in Schlei; decreases cilium assembly; loss
FT of protein localization to cilium)"
FT /evidence="ECO:0000269|PubMed:22698544,
FT ECO:0000269|PubMed:26518474"
FT CONFLICT 74
FT /note="G -> R (in Ref. 1; BAB28560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 15593 MW; F3A38A2835DAD676 CRC64;
MGRISGLVPS RFLTLLAHLV VVITLFWSRE SNIQACLPLK FTPEEYEKQD NQLVAALCLT
LGLFAVELAG FLSGVSMFNS TQSLLSIAAH CSASVALSFF VFERWECTTY WYIFTFCSAF
PAVTETALFI AVFGLKKKPF
