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   28-JUN-2023, entry version 130.
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; 68.
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   ProteomicsDB; 79441; -. [Q9BXJ8-1]
DR   ProteomicsDB; 79442; -. [Q9BXJ8-2]
DR   Antibodypedia; 29220; 55 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   AGR; HGNC:21697; -.
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; AEWQVLI; -.
DR   OrthoDB; 314124at2759; -.
DR   PhylomeDB; Q9BXJ8; -.
DR   PathwayCommons; Q9BXJ8; -.
DR   SignaLink; Q9BXJ8; -.
DR   BioGRID-ORCS; 83862; 11 hits in 704 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: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:monoatomic 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:monoatomic 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:SF1; ION CHANNEL TACAN; 1.
DR   PANTHER; PTHR21433; TRANSMEMBRANE PROTEIN INDUCED BY TUMOR NECROSIS FACTOR ALPHA; 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
//