TACAN_MOUSE
ID TACAN_MOUSE Reviewed; 343 AA.
AC Q8C1E7; Q8BWP7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ion channel TACAN {ECO:0000303|PubMed:32084332};
DE AltName: Full=Transmembrane protein 120A {ECO:0000303|PubMed:26024229};
GN Name=Tmem120a {ECO:0000303|PubMed:26024229, ECO:0000312|MGI:MGI:2686991};
GN Synonyms=Net29 {ECO:0000303|PubMed:20091084},
GN Tacan {ECO:0000303|PubMed:32084332};
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=Liver, and Small intestine;
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;
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 SUBCELLULAR LOCATION.
RX PubMed=20091084; DOI=10.1007/s00018-010-0257-2;
RA Malik P., Korfali N., Srsen V., Lazou V., Batrakou D.G., Zuleger N.,
RA Kavanagh D.M., Wilkie G.S., Goldberg M.W., Schirmer E.C.;
RT "Cell-specific and lamin-dependent targeting of novel transmembrane
RT proteins in the nuclear envelope.";
RL Cell. Mol. Life Sci. 67:1353-1369(2010).
RN [4]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=26024229; DOI=10.1371/journal.pone.0127712;
RA Batrakou D.G., de Las Heras J.I., Czapiewski R., Mouras R., Schirmer E.C.;
RT "TMEM120A and B: nuclear envelope transmembrane proteins important for
RT adipocyte differentiation.";
RL PLoS ONE 10:E0127712-E0127712(2015).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32084332; DOI=10.1016/j.cell.2020.01.033;
RA Beaulieu-Laroche L., Christin M., Donoghue A., Agosti F., Yousefpour N.,
RA Petitjean H., Davidova A., Stanton C., Khan U., Dietz C., Faure E.,
RA Fatima T., MacPherson A., Mouchbahani-Constance S., Bisson D.G.,
RA Haglund L., Ouellet J.A., Stone L.S., Samson J., Smith M.J., Ask K.,
RA Ribeiro-da-Silva A., Blunck R., Poole K., Bourinet E., Sharif-Naeini R.;
RT "TACAN is an ion channel involved in sensing mechanical pain.";
RL Cell 0:0-0(2020).
CC -!- FUNCTION: Ion channel involved in sensing mechanical pain
CC (PubMed:32084332). Contributes to mechanosensitive currents in
CC nocireceptors and detecting mechanical pain stimuli (PubMed:32084332).
CC May also be required for efficient adipogenesis (PubMed:26024229).
CC {ECO:0000269|PubMed:26024229, ECO:0000269|PubMed:32084332}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with TMEM120B.
CC {ECO:0000269|PubMed:26024229}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32084332};
CC Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane
CC {ECO:0000269|PubMed:20091084}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression in the
CC heart, kidneys, colon and sensory neurons of the dorsal root ganglia
CC (PubMed:32084332). Expressed in nociceptors (PubMed:32084332). Highly
CC expressed in white adipose tissue (at protein level) (PubMed:26024229).
CC Highly expressed in brown adipose tissue and expressed at low levels in
CC liver (PubMed:26024229). {ECO:0000269|PubMed:26024229,
CC ECO:0000269|PubMed:32084332}.
CC -!- INDUCTION: Up-regulated during adipocyte differentiation.
CC {ECO:0000269|PubMed:26024229}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:32084332).
CC Conditional knockout in nociceptors decreases the mechanosensitivity of
CC nociceptors and reduces behavioral responses to painful mechanical
CC stimuli but not to thermal or touch stimuli (PubMed:32084332).
CC {ECO:0000269|PubMed:32084332}.
CC -!- MISCELLANEOUS: TACAN means movement in Farsi.
CC {ECO:0000303|PubMed:32084332}.
CC -!- SIMILARITY: Belongs to the TMEM120 family. {ECO:0000305}.
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DR EMBL; AK028119; BAC25759.1; -; mRNA.
DR EMBL; AK050367; BAC34212.1; -; mRNA.
DR EMBL; BC046757; AAH46757.1; -; mRNA.
DR CCDS; CCDS19744.1; -.
DR RefSeq; NP_766129.1; NM_172541.2.
DR PDB; 7N0K; EM; 3.50 A; A/B=1-343.
DR PDB; 7N0L; EM; 2.80 A; A/B=1-343.
DR PDBsum; 7N0K; -.
DR PDBsum; 7N0L; -.
DR AlphaFoldDB; Q8C1E7; -.
DR SMR; Q8C1E7; -.
DR BioGRID; 229606; 1.
DR STRING; 10090.ENSMUSP00000045252; -.
DR iPTMnet; Q8C1E7; -.
DR PhosphoSitePlus; Q8C1E7; -.
DR SwissPalm; Q8C1E7; -.
DR EPD; Q8C1E7; -.
DR jPOST; Q8C1E7; -.
DR MaxQB; Q8C1E7; -.
DR PaxDb; Q8C1E7; -.
DR PeptideAtlas; Q8C1E7; -.
DR PRIDE; Q8C1E7; -.
DR ProteomicsDB; 263211; -.
DR Antibodypedia; 29220; 33 antibodies from 14 providers.
DR Ensembl; ENSMUST00000043378; ENSMUSP00000045252; ENSMUSG00000039886.
DR GeneID; 215210; -.
DR KEGG; mmu:215210; -.
DR UCSC; uc008zyu.1; mouse.
DR CTD; 83862; -.
DR MGI; MGI:2686991; Tmem120a.
DR VEuPathDB; HostDB:ENSMUSG00000039886; -.
DR eggNOG; KOG4758; Eukaryota.
DR GeneTree; ENSGT00390000007848; -.
DR HOGENOM; CLU_048749_1_1_1; -.
DR InParanoid; Q8C1E7; -.
DR OMA; TVNCALL; -.
DR OrthoDB; 916768at2759; -.
DR PhylomeDB; Q8C1E7; -.
DR TreeFam; TF313552; -.
DR BioGRID-ORCS; 215210; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8C1E7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C1E7; protein.
DR Bgee; ENSMUSG00000039886; Expressed in white adipose tissue and 74 other tissues.
DR ExpressionAtlas; Q8C1E7; baseline and differential.
DR Genevisible; Q8C1E7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005216; F:ion channel activity; IDA:UniProtKB.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR InterPro; IPR012926; TACAN/TMEM120B.
DR PANTHER; PTHR21433; PTHR21433; 1.
DR Pfam; PF07851; TMPIT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..343
FT /note="Ion channel TACAN"
FT /id="PRO_0000309340"
FT TOPO_DOM 1..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 136..156
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..162
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 163..183
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 191..211
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..222
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 223..240
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 274..294
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..305
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:32084332"
FT TRANSMEM 306..326
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32084332"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 23..66
FT /evidence="ECO:0007829|PDB:7N0L"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 123..153
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 159..184
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:7N0L"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 216..249
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:7N0L"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 276..295
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:7N0L"
FT HELIX 313..334
FT /evidence="ECO:0007829|PDB:7N0L"
SQ SEQUENCE 343 AA; 40751 MW; 7AC1BE2A31E0A6C1 CRC64;
MQSPPPDPLG DCLRNWEDLQ QDFQGIQETH RLYRLKLEEL TKLQANCTNS ITRQKKRLQE
LALVLKKCRP SLPSESMEAA QELENQMKER QGLFFDMEAY LPKKNGLYLS LVLGNVNVTL
LSKQAKFAYK DEYEKFKLYL TIILIVISFT CRFLLNSRVT DAAFNFLLVW YYCTLTIRES
ILINNGSRIK GWWVFHHYVS TFLSGVMLTW PDGLMYQKFR NQFLSFSMYQ SFVQFLQYYY
QSGCLYRLRA LGERHTMDLT VEGFQSWMWR GLTFLLPFLF FGHFWQLFNA LTLFNLARDP
ECKEWQVLMC GFPFLLLFLG NFFTTLRVVH QKFHSQQHGN KKD
