ID   TLCD1_MOUSE             Reviewed;         247 AA.
AC   Q99JT6; Q3V372; Q5SYM9; Q8CHT9; Q9DCK5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=TLC domain-containing protein 1;
DE   AltName: Full=Calfacilitin;
DE   Flags: Precursor;
GN   Name=Tlcd1;
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] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, Kidney, and Thymus;
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 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Regulates the composition and fluidity of the plasma membrane
CC       (By similarity). Inhibits the incorporation of membrane-fluidizing
CC       phospholipids containing omega-3 long-chain polyunsaturated fatty acids
CC       (LCPUFA) and thereby promotes membrane rigidity (By similarity). Does
CC       not appear to have any effect on LCPUFA synthesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q96CP7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96CP7};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:F1NZP5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q99JT6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JT6-2; Sequence=VSP_024890;
CC       Name=3;
CC         IsoId=Q99JT6-3; Sequence=VSP_024887;
CC       Name=4;
CC         IsoId=Q99JT6-4; Sequence=VSP_024888, VSP_024889;
CC   -!- CAUTION: Was originally proposed to be a calcium channel facilitator
CC       (By similarity). However, a more recent study shows that this protein
CC       regulates membrane phospholipid homeostasis (By similarity). Therefore,
CC       any effects on calcium flux are most likely a secondary consequence of
CC       defects in membrane composition or fluidity (By similarity).
CC       {ECO:0000250|UniProtKB:F1NZP5, ECO:0000250|UniProtKB:Q96CP7}.
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DR   EMBL; AK002703; BAB22297.1; -; mRNA.
DR   EMBL; AK046577; BAE20654.1; -; mRNA.
DR   EMBL; AK161721; BAE36548.1; -; mRNA.
DR   EMBL; AK165432; BAE38185.1; -; mRNA.
DR   EMBL; AL591070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005702; AAH05702.1; -; mRNA.
DR   EMBL; BC039182; AAH39182.1; -; mRNA.
DR   CCDS; CCDS25092.1; -. [Q99JT6-1]
DR   CCDS; CCDS70257.1; -. [Q99JT6-3]
DR   RefSeq; NP_001278165.1; NM_001291236.1. [Q99JT6-3]
DR   RefSeq; NP_001278166.1; NM_001291237.1. [Q99JT6-3]
DR   RefSeq; NP_080984.1; NM_026708.2. [Q99JT6-1]
DR   RefSeq; XP_006534117.1; XM_006534054.2.
DR   AlphaFoldDB; Q99JT6; -.
DR   BioGRID; 212831; 2.
DR   STRING; 10090.ENSMUSP00000114202; -.
DR   PhosphoSitePlus; Q99JT6; -.
DR   SwissPalm; Q99JT6; -.
DR   MaxQB; Q99JT6; -.
DR   PaxDb; 10090-ENSMUSP00000114202; -.
DR   ProteomicsDB; 259397; -. [Q99JT6-1]
DR   ProteomicsDB; 259398; -. [Q99JT6-2]
DR   ProteomicsDB; 259399; -. [Q99JT6-3]
DR   ProteomicsDB; 259400; -. [Q99JT6-4]
DR   Antibodypedia; 51370; 76 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000092880.14; ENSMUSP00000090556.8; ENSMUSG00000019437.18. [Q99JT6-3]
DR   Ensembl; ENSMUST00000098545.12; ENSMUSP00000096145.6; ENSMUSG00000019437.18. [Q99JT6-2]
DR   Ensembl; ENSMUST00000108338.2; ENSMUSP00000103975.2; ENSMUSG00000019437.18. [Q99JT6-4]
DR   Ensembl; ENSMUST00000127587.8; ENSMUSP00000114202.2; ENSMUSG00000019437.18. [Q99JT6-1]
DR   GeneID; 68385; -.
DR   KEGG; mmu:68385; -.
DR   UCSC; uc007kij.2; mouse. [Q99JT6-1]
DR   UCSC; uc007kik.2; mouse. [Q99JT6-3]
DR   AGR; MGI:1915572; -.
DR   CTD; 116238; -.
DR   MGI; MGI:1915572; Tlcd1.
DR   VEuPathDB; HostDB:ENSMUSG00000019437; -.
DR   eggNOG; KOG4474; Eukaryota.
DR   GeneTree; ENSGT01010000222313; -.
DR   HOGENOM; CLU_056440_2_0_1; -.
DR   InParanoid; Q99JT6; -.
DR   OMA; LTWYFVR; -.
DR   OrthoDB; 2942304at2759; -.
DR   PhylomeDB; Q99JT6; -.
DR   TreeFam; TF315115; -.
DR   BioGRID-ORCS; 68385; 8 hits in 80 CRISPR screens.
DR   PRO; PR:Q99JT6; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q99JT6; Protein.
DR   Bgee; ENSMUSG00000019437; Expressed in yolk sac and 230 other cell types or tissues.
DR   ExpressionAtlas; Q99JT6; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0071709; P:membrane assembly; ISO:MGI.
DR   GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR   GO; GO:0007009; P:plasma membrane organization; ISO:MGI.
DR   GO; GO:0097035; P:regulation of membrane lipid distribution; ISO:MGI.
DR   InterPro; IPR006634; TLC-dom.
DR   PANTHER; PTHR13439; CT120 PROTEIN; 1.
DR   PANTHER; PTHR13439:SF5; TLC DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR   SMART; SM00724; TLC; 1.
DR   PROSITE; PS50922; TLC; 1.
DR   Genevisible; Q99JT6; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..247
FT                   /note="TLC domain-containing protein 1"
FT                   /id="PRO_0000285678"
FT   TOPO_DOM        28..46
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   INTRAMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F1NZP5"
FT   DOMAIN          40..234
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT   VAR_SEQ         1..65
FT                   /note="MPLLFHPAWPLLLGATLTFRALRRVLCRLPQPAHVQTDPLRTWRWHNLLVSF
FT                   THSIVSGIWALLC -> MRWPWDLSRGARTGLPLAIPITGEQTPRISPDSVWKTTQPRT
FT                   AVGNPS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024887"
FT   VAR_SEQ         121..127
FT                   /note="AMGAFFS -> VRENPVK (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024888"
FT   VAR_SEQ         128..247
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024889"
FT   VAR_SEQ         170..196
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024890"
FT   CONFLICT        28
FT                   /note="R -> H (in Ref. 1; BAE20654)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  28787 MW;  84AEA3CBE8BE4093 CRC64;
     MPLLFHPAWP LLLGATLTFR ALRRVLCRLP QPAHVQTDPL RTWRWHNLLV SFTHSIVSGI
     WALLCLWQTP EMLVEIETAW SASGYLLVCF SAGYFIHDTV DIVVSKQTRA SWEYLVHHVM
     AMGAFFSGIF WKRFVGGGVL TLLVEVSNIF LTLRMMMKIN NAQDLLLYKV NKYINLVMYF
     LFRLAPQAYL TKFFLQYAGQ RTLGTFLLAI LLMLDLMIII YFSRLLRSDF CPERAPRRQQ
     KDKFLTE
//