TM231_MOUSE
ID TM231_MOUSE Reviewed; 315 AA.
AC Q3U284; Q497S7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transmembrane protein 231;
GN Name=Tmem231;
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=NOD;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryonic germ cell;
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 IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Transmembrane component of the tectonic-like complex, a
CC complex localized at the transition zone of primary cilia and acting as
CC a barrier that prevents diffusion of transmembrane proteins between the
CC cilia and plasma membranes. Required for ciliogenesis and sonic
CC hedgehog/SHH signaling. {ECO:0000269|PubMed:22179047}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex)
CC (PubMed:22179047). Interacts with TMEM107 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6L2, ECO:0000269|PubMed:22179047}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:22179047}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22179047}. Note=Localizes to the transition zone of
CC primary cilia; SEPT2 is required for localization to the transition
CC zone.
CC -!- DISRUPTION PHENOTYPE: Embryos die around 15.5 dpc with severe vascular
CC defects. 10.5 dpc mutant embryos have defects in patterning of the
CC ventral spinal cord that are characteristic of defects in Shh
CC signaling. 14.5 dpc embryos exhibit microphthalmia and polydactyly,
CC consistent with disruptions in Shh signaling.
CC {ECO:0000269|PubMed:22179047}.
CC -!- SIMILARITY: Belongs to the TMEM231 family. {ECO:0000305}.
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DR EMBL; AK155425; BAE33258.1; -; mRNA.
DR EMBL; BC100402; AAI00403.2; -; mRNA.
DR EMBL; BC132428; AAI32429.1; -; mRNA.
DR EMBL; BC132430; AAI32431.1; -; mRNA.
DR CCDS; CCDS52676.1; -.
DR RefSeq; NP_001028493.1; NM_001033321.1.
DR AlphaFoldDB; Q3U284; -.
DR BioGRID; 231574; 2.
DR CORUM; Q3U284; -.
DR IntAct; Q3U284; 5.
DR STRING; 10090.ENSMUSP00000034429; -.
DR GlyGen; Q3U284; 3 sites.
DR PhosphoSitePlus; Q3U284; -.
DR MaxQB; Q3U284; -.
DR PaxDb; Q3U284; -.
DR PeptideAtlas; Q3U284; -.
DR PRIDE; Q3U284; -.
DR ProteomicsDB; 259555; -.
DR Antibodypedia; 8257; 53 antibodies from 20 providers.
DR DNASU; 234740; -.
DR Ensembl; ENSMUST00000034429; ENSMUSP00000034429; ENSMUSG00000031951.
DR GeneID; 234740; -.
DR KEGG; mmu:234740; -.
DR UCSC; uc009nna.1; mouse.
DR CTD; 79583; -.
DR MGI; MGI:2685024; Tmem231.
DR VEuPathDB; HostDB:ENSMUSG00000031951; -.
DR eggNOG; KOG4838; Eukaryota.
DR GeneTree; ENSGT00390000015366; -.
DR HOGENOM; CLU_070969_0_0_1; -.
DR InParanoid; Q3U284; -.
DR OMA; QLPARYH; -.
DR OrthoDB; 1247968at2759; -.
DR PhylomeDB; Q3U284; -.
DR TreeFam; TF312969; -.
DR BioGRID-ORCS; 234740; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem231; mouse.
DR PRO; PR:Q3U284; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3U284; protein.
DR Bgee; ENSMUSG00000031951; Expressed in blastocyst and 183 other tissues.
DR ExpressionAtlas; Q3U284; baseline and differential.
DR Genevisible; Q3U284; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
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:0016020; C:membrane; IDA:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR InterPro; IPR019306; TMEM231.
DR PANTHER; PTHR14605; PTHR14605; 1.
DR Pfam; PF10149; TM231; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..315
FT /note="Transmembrane protein 231"
FT /id="PRO_0000317521"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 315 AA; 36261 MW; 4489CA8EFC253EB8 CRC64;
MALYHLFSHP IERAYRAGLC SKAALFLLLT TALTYIPPLL VAFRSHGFWL KRSSYEEQPN
VRFQHQVLLV ALLGPEPEAF LAWSTFPTFN RLQGAHLRVP LVSSREEDRN QDGKMDVLYF
KLELPLQPTE HVLGVQLILT FSYQLHRMST FEMQSMAFLQ SSFAVPGSQL YVNGDLRLQQ
KQPLSYRGLD IRYNVSVING TSPFAQDYDL THIVAAYQER NVTTVLSDPN PIWLVGRAAE
APFVIHAVIR YPTEVISYQP GFWEMIKFAW IQYVSILLIF LWVFERIKIF VFQNQVVTSI
PVAVPQGEIR KEHLS
