TM216_MOUSE
ID TM216_MOUSE Reviewed; 141 AA.
AC Q9CQC4; D3YUA1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transmembrane protein 216;
DE AltName: Full=Thymus atrophy-related protein;
GN Name=Tmem216;
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 [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RA Lee Y., He W., Lu X.;
RT "A new gene related to mouse thymus atrophy.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
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: Part of the tectonic-like complex which is required for
CC tissue-specific ciliogenesis and may regulate ciliary membrane
CC composition. {ECO:0000269|PubMed:21725307}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex)
CC (PubMed:21725307). Interacts with TMEM107 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P0N5, ECO:0000269|PubMed:21725307}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition zone, a
CC region between the basal body and the ciliary axoneme.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQC4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQC4-2; Sequence=VSP_040297;
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DR EMBL; AF332866; AAK17992.1; -; mRNA.
DR EMBL; AK003740; BAB22973.1; -; mRNA.
DR EMBL; AK014997; BAB29662.1; -; mRNA.
DR EMBL; AC125093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052053; AAH52053.1; -; mRNA.
DR CCDS; CCDS37913.1; -. [Q9CQC4-2]
DR CCDS; CCDS70934.1; -. [Q9CQC4-1]
DR RefSeq; NP_001264789.1; NM_001277860.1. [Q9CQC4-1]
DR RefSeq; NP_001264790.1; NM_001277861.1. [Q9CQC4-2]
DR RefSeq; NP_081074.1; NM_026798.3. [Q9CQC4-2]
DR RefSeq; XP_006527381.1; XM_006527318.2. [Q9CQC4-1]
DR RefSeq; XP_006527382.1; XM_006527319.3. [Q9CQC4-2]
DR AlphaFoldDB; Q9CQC4; -.
DR CORUM; Q9CQC4; -.
DR STRING; 10090.ENSMUSP00000025569; -.
DR PaxDb; Q9CQC4; -.
DR PRIDE; Q9CQC4; -.
DR Ensembl; ENSMUST00000025569; ENSMUSP00000025569; ENSMUSG00000024667. [Q9CQC4-2]
DR Ensembl; ENSMUST00000059582; ENSMUSP00000059878; ENSMUSG00000024667. [Q9CQC4-2]
DR Ensembl; ENSMUST00000123788; ENSMUSP00000119596; ENSMUSG00000024667. [Q9CQC4-1]
DR Ensembl; ENSMUST00000145210; ENSMUSP00000123397; ENSMUSG00000024667. [Q9CQC4-2]
DR Ensembl; ENSMUST00000154383; ENSMUSP00000115319; ENSMUSG00000024667. [Q9CQC4-1]
DR Ensembl; ENSMUST00000236561; ENSMUSP00000158207; ENSMUSG00000024667. [Q9CQC4-2]
DR GeneID; 68642; -.
DR KEGG; mmu:68642; -.
DR UCSC; uc008gqc.2; mouse. [Q9CQC4-1]
DR CTD; 51259; -.
DR MGI; MGI:1920020; Tmem216.
DR VEuPathDB; HostDB:ENSMUSG00000024667; -.
DR eggNOG; KOG4502; Eukaryota.
DR GeneTree; ENSGT00940000153899; -.
DR HOGENOM; CLU_187017_1_0_1; -.
DR InParanoid; Q9CQC4; -.
DR OMA; QFPWGLK; -.
DR OrthoDB; 1584392at2759; -.
DR PhylomeDB; Q9CQC4; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 68642; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9CQC4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CQC4; protein.
DR Bgee; ENSMUSG00000024667; Expressed in granulocyte and 202 other tissues.
DR Genevisible; Q9CQC4; MM.
DR GO; GO:0035869; C:ciliary transition zone; IMP:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR InterPro; IPR019184; Uncharacterised_TM-17.
DR PANTHER; PTHR13531; PTHR13531; 1.
DR Pfam; PF09799; Transmemb_17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..141
FT /note="Transmembrane protein 216"
FT /id="PRO_0000318956"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_040297"
SQ SEQUENCE 141 AA; 16160 MW; 844CFD26380F0D93 CRC64;
MAPRDKRLSS TPLEVLFFLN GWYYATYFLL ELLIFLYKGL LLPYPTANLV LDVVMLLLYL
GIEVIRLFFG TKGNLCQRKM PLGISVALTF PSAMMASYYL LLQTYVLRLE AIMNSILLFF
CGSELLLEML TLATFSSMDR I
