TLCD1_CHICK
ID TLCD1_CHICK Reviewed; 252 AA.
AC F1NZP5; F4Y5R7;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=TLC domain-containing protein 1;
DE AltName: Full=Calfacilitin;
DE Flags: Precursor;
GN Name=TLCD1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CACNA1C, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RX PubMed=23673622; DOI=10.1038/ncomms2864;
RA Papanayotou C., De Almeida I., Liao P., Oliveira N.M., Lu S.Q.,
RA Kougioumtzidou E., Zhu L., Shaw A., Sheng G., Streit A., Yu D.,
RA Wah Soong T., Stern C.D.;
RT "Calfacilitin is a calcium channel modulator essential for initiation of
RT neural plate development.";
RL Nat. Commun. 4:1837-1848(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(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 -!- SUBUNIT: Interacts with CACNA1C in vitro; however the relevance of the
CC interaction in vivo is unclear. {ECO:0000269|PubMed:23673622}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23673622};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23673622}.
CC -!- CAUTION: Was originally proposed to be a calcium channel facilitator
CC (PubMed:23673622). 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:Q96CP7, ECO:0000269|PubMed:23673622}.
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DR EMBL; GQ504719; ADE62144.1; -; mRNA.
DR EMBL; AADN03007719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001291994.1; NM_001305065.1.
DR AlphaFoldDB; F1NZP5; -.
DR PaxDb; F1NZP5; -.
DR Ensembl; ENSGALT00000089073; ENSGALP00000059819; ENSGALG00000003973.
DR GeneID; 417575; -.
DR KEGG; gga:417575; -.
DR CTD; 116238; -.
DR VEuPathDB; HostDB:geneid_417575; -.
DR eggNOG; KOG4474; Eukaryota.
DR GeneTree; ENSGT01010000222313; -.
DR HOGENOM; CLU_056440_2_1_1; -.
DR InParanoid; F1NZP5; -.
DR OrthoDB; 1113854at2759; -.
DR TreeFam; TF315115; -.
DR PRO; PR:F1NZP5; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000003973; Expressed in lung and 12 other tissues.
DR ExpressionAtlas; F1NZP5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0071709; P:membrane assembly; IBA:GO_Central.
DR GO; GO:0055091; P:phospholipid homeostasis; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; IBA:GO_Central.
DR InterPro; IPR006634; TLC-dom.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..252
FT /note="TLC domain-containing protein 1"
FT /id="PRO_0000429333"
FT TOPO_DOM 30..47
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:23673622"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23673622"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..124
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:23673622"
FT INTRAMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..174
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:23673622"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23673622"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..252
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:23673622"
FT DOMAIN 41..235
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
SQ SEQUENCE 252 AA; 28348 MW; D28A29A0E0047342 CRC64;
MGPGWRAPSA ALVGGSVALF GALRRAALAL PRPAAVRSRP GRVWRWRNLL VSFAHSVLAG
LWALFSLWQS PELLSDIQDG YSVSGHLLVC FSSGYFIHDS LDIIFNQQSR SSWEYLVHHA
MAISAFVSLI ITGRFLVAAM LLLLVEVSNI FLTIRMLLKM SNVPSPALYE ANKYVNLVMY
FAFRLAPQVY LTWYFVRYVE VQGQGAFLMA NLLLLDAMIL MYFSRLLRSD FFPSLRKGSV
GRDVDGEKFL ID
