TACAN_HUMAN
ID TACAN_HUMAN Reviewed; 343 AA.
AC Q9BXJ8; Q86TE9; Q8N6P1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ion channel TACAN {ECO:0000303|PubMed:32084332};
DE AltName: Full=Transmembrane protein 120A {ECO:0000303|PubMed:26024229};
DE AltName: Full=Transmembrane protein induced by tumor necrosis factor alpha {ECO:0000303|Ref.1};
GN Name=TMEM120A {ECO:0000303|PubMed:26024229, ECO:0000312|HGNC:HGNC:21697};
GN Synonyms=TACAN {ECO:0000303|PubMed:32084332}, TMPIT {ECO:0000303|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Murakami T., Mataki C., Hamakubo T., Kodama T.;
RT "Endothelial cell transmembrane protein induced by tumor necrosis factor
RT alpha (TMPIT) mRNA, complete cds.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ARG-86 AND ALA-201.
RC TISSUE=Brain, and PNS;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP FUNCTION, AND SUBUNIT.
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 [6]
RP TISSUE SPECIFICITY.
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. Contributes
CC to mechanosensitive currents in nocireceptors and detecting mechanical
CC pain stimuli (By similarity). May also be required for efficient
CC adipogenesis (PubMed:26024229). {ECO:0000250|UniProtKB:Q8C1E7,
CC ECO:0000269|PubMed:26024229}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with TMEM120B.
CC {ECO:0000269|PubMed:26024229}.
CC -!- INTERACTION:
CC Q9BXJ8; Q13520: AQP6; NbExp=3; IntAct=EBI-727322, EBI-13059134;
CC Q9BXJ8; Q13323: BIK; NbExp=3; IntAct=EBI-727322, EBI-700794;
CC Q9BXJ8; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-727322, EBI-8637742;
CC Q9BXJ8; Q9Y394: DHRS7; NbExp=3; IntAct=EBI-727322, EBI-1387800;
CC Q9BXJ8; Q15125: EBP; NbExp=3; IntAct=EBI-727322, EBI-3915253;
CC Q9BXJ8; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-727322, EBI-18304435;
CC Q9BXJ8; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-727322, EBI-18053395;
CC Q9BXJ8; O15243: LEPROT; NbExp=3; IntAct=EBI-727322, EBI-15672507;
CC Q9BXJ8; Q8N386: LRRC25; NbExp=3; IntAct=EBI-727322, EBI-11304917;
CC Q9BXJ8; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-727322, EBI-11075081;
CC Q9BXJ8; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-727322, EBI-7545592;
CC Q9BXJ8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-727322, EBI-17247926;
CC Q9BXJ8; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-727322, EBI-10819434;
CC Q9BXJ8; Q16623: STX1A; NbExp=3; IntAct=EBI-727322, EBI-712466;
CC Q9BXJ8; P32856-2: STX2; NbExp=3; IntAct=EBI-727322, EBI-11956649;
CC Q9BXJ8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-727322, EBI-8638294;
CC Q9BXJ8; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-727322, EBI-11722971;
CC Q9BXJ8; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-727322, EBI-2548832;
CC Q9BXJ8; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-727322, EBI-17198826;
CC Q9BXJ8; Q9Y320: TMX2; NbExp=3; IntAct=EBI-727322, EBI-6447886;
CC Q9BXJ8; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-727322, EBI-17249488;
CC Q9BXJ8; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-727322, EBI-17670824;
CC Q9BXJ8; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-727322, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8C1E7};
CC Multi-pass membrane protein {ECO:0000255}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q8C1E7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXJ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXJ8-2; Sequence=VSP_029148;
CC -!- TISSUE SPECIFICITY: Expressed in nociceptors.
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; AF327923; AAK16442.1; -; mRNA.
DR EMBL; CH471066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029487; AAH29487.1; -; mRNA.
DR EMBL; BC051850; AAH51850.1; -; mRNA.
DR CCDS; CCDS64688.1; -. [Q9BXJ8-1]
DR RefSeq; NP_114131.1; NM_031925.2. [Q9BXJ8-1]
DR PDB; 7CXR; EM; 3.40 A; A/B=1-343.
DR PDB; 7F3T; EM; 3.69 A; A/B=2-343.
DR PDB; 7F3U; EM; 4.00 A; A/B=2-343.
DR PDB; 7F6V; EM; 3.66 A; A/B=1-343.
DR PDB; 7N7P; EM; 3.24 A; A/B=2-343.
DR PDBsum; 7CXR; -.
DR PDBsum; 7F3T; -.
DR PDBsum; 7F3U; -.
DR PDBsum; 7F6V; -.
DR PDBsum; 7N7P; -.
DR AlphaFoldDB; Q9BXJ8; -.
DR SMR; Q9BXJ8; -.
DR BioGRID; 123777; 67.
DR IntAct; Q9BXJ8; 41.
DR MINT; Q9BXJ8; -.
DR STRING; 9606.ENSP00000473983; -.
DR TCDB; 1.A.119.1.2; the stress-inducible transmembrane protein (tmpit) family.
DR iPTMnet; Q9BXJ8; -.
DR PhosphoSitePlus; Q9BXJ8; -.
DR SwissPalm; Q9BXJ8; -.
DR BioMuta; TMEM120A; -.
DR DMDM; 74717620; -.
DR EPD; Q9BXJ8; -.
DR jPOST; Q9BXJ8; -.
DR MassIVE; Q9BXJ8; -.
DR MaxQB; Q9BXJ8; -.
DR PeptideAtlas; Q9BXJ8; -.
DR PRIDE; Q9BXJ8; -.
DR ProteomicsDB; 79441; -. [Q9BXJ8-1]
DR ProteomicsDB; 79442; -. [Q9BXJ8-2]
DR Antibodypedia; 29220; 33 antibodies from 14 providers.
DR DNASU; 83862; -.
DR Ensembl; ENST00000493111.7; ENSP00000473983.1; ENSG00000189077.11. [Q9BXJ8-1]
DR GeneID; 83862; -.
DR KEGG; hsa:83862; -.
DR MANE-Select; ENST00000493111.7; ENSP00000473983.1; NM_031925.3; NP_114131.1.
DR UCSC; uc032ztu.2; human. [Q9BXJ8-1]
DR CTD; 83862; -.
DR DisGeNET; 83862; -.
DR GeneCards; TMEM120A; -.
DR HGNC; HGNC:21697; TMEM120A.
DR HPA; ENSG00000189077; Low tissue specificity.
DR MIM; 616550; gene.
DR neXtProt; NX_Q9BXJ8; -.
DR OpenTargets; ENSG00000189077; -.
DR PharmGKB; PA162405861; -.
DR VEuPathDB; HostDB:ENSG00000189077; -.
DR eggNOG; KOG4758; Eukaryota.
DR GeneTree; ENSGT00390000007848; -.
DR HOGENOM; CLU_048749_1_1_1; -.
DR InParanoid; Q9BXJ8; -.
DR OMA; TVNCALL; -.
DR OrthoDB; 916768at2759; -.
DR PhylomeDB; Q9BXJ8; -.
DR PathwayCommons; Q9BXJ8; -.
DR SignaLink; Q9BXJ8; -.
DR BioGRID-ORCS; 83862; 10 hits in 647 CRISPR screens.
DR ChiTaRS; TMEM120A; human.
DR GenomeRNAi; 83862; -.
DR Pharos; Q9BXJ8; Tdark.
DR PRO; PR:Q9BXJ8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BXJ8; protein.
DR Bgee; ENSG00000189077; Expressed in right testis and 160 other tissues.
DR ExpressionAtlas; Q9BXJ8; baseline and differential.
DR Genevisible; Q9BXJ8; HS.
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; ISS:UniProtKB.
DR GO; GO:0005216; F:ion channel activity; ISS:UniProtKB.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; ISS: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; Alternative splicing; Cell membrane; Ion channel;
KW Ion transport; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..343
FT /note="Ion channel TACAN"
FT /id="PRO_0000309339"
FT TOPO_DOM 1..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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"
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"
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"
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"
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"
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"
FT VAR_SEQ 189..343
FT /note="IKGWWVFHHYVSTFLSGVMLTWPDGLMYQKFRNQFLSFSMYQSFVQFLQYYY
FT QSGCLYRLRALGERHTMDLTVEGFQSWMWRGLTFLLPFLFFGHFWQLFNALTLFNLAQD
FT PQCKEWQVLMCGFPFLLLFLGNFFTTLRVVHHKFHSQRHGSKKD -> WAGRALREGSM
FT EWGARTLREAGTGAGGDGGSLLQDQRLVGVPSLRVHLPVGSHADVVRRSHVPEIPEPIP
FT LLFHVPELRAVSPVLLPERLPLPPAGAGRAAHHGPHCGGLPVLDVAGPHLPAAFSFLWT
FT LLAAF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029148"
FT VARIANT 86
FT /note="Q -> R (in dbSNP:rs17852664)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_036933"
FT VARIANT 201
FT /note="T -> A (in dbSNP:rs17855697)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_036934"
FT HELIX 9..68
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 123..152
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 158..184
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 214..253
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 262..296
FT /evidence="ECO:0007829|PDB:7N7P"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7N7P"
FT HELIX 306..334
FT /evidence="ECO:0007829|PDB:7N7P"
SQ SEQUENCE 343 AA; 40610 MW; 7A6E241804F59A96 CRC64;
MQPPPPGPLG DCLRDWEDLQ QDFQNIQETH RLYRLKLEEL TKLQNNCTSS ITRQKKRLQE
LALALKKCKP SLPAEAEGAA QELENQMKER QGLFFDMEAY LPKKNGLYLS LVLGNVNVTL
LSKQAKFAYK DEYEKFKLYL TIILILISFT CRFLLNSRVT DAAFNFLLVW YYCTLTIRES
ILINNGSRIK GWWVFHHYVS TFLSGVMLTW PDGLMYQKFR NQFLSFSMYQ SFVQFLQYYY
QSGCLYRLRA LGERHTMDLT VEGFQSWMWR GLTFLLPFLF FGHFWQLFNA LTLFNLAQDP
QCKEWQVLMC GFPFLLLFLG NFFTTLRVVH HKFHSQRHGS KKD