FITM1_DANRE
ID FITM1_DANRE Reviewed; 290 AA.
AC Q5CZN0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Fat storage-inducing transmembrane protein 1 {ECO:0000250|UniProtKB:A5D6W6, ECO:0000255|HAMAP-Rule:MF_03229};
DE AltName: Full=FITM1-like protein {ECO:0000255|HAMAP-Rule:MF_03229};
DE AltName: Full=Fat-inducing protein 1 {ECO:0000255|HAMAP-Rule:MF_03229};
GN Name=fitm1l;
GN Synonyms=fit1 {ECO:0000255|HAMAP-Rule:MF_03229},
GN fitm1 {ECO:0000255|HAMAP-Rule:MF_03229}; ORFNames=zgc:112967;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION AS FITM1.
RX PubMed=18160536; DOI=10.1073/pnas.0708579105;
RA Kadereit B., Kumar P., Wang W.-J., Miranda D., Snapp E.L., Severina N.,
RA Torregroza I., Evans T., Silver D.L.;
RT "Evolutionarily conserved gene family important for fat storage.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:94-99(2008).
CC -!- FUNCTION: May play an important role in the formation of lipid droplets
CC (LDs) which are storage organelles at the center of lipid and energy
CC homeostasis (By similarity). May directly bind to diacylglycerol (DAGs)
CC and triacylglycerol (By similarity). {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03229}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
CC -!- SIMILARITY: Belongs to the FIT family. FIT1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03229}.
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DR EMBL; BC090787; AAH90787.1; -; mRNA.
DR RefSeq; NP_001013343.1; NM_001013325.2.
DR AlphaFoldDB; Q5CZN0; -.
DR STRING; 7955.ENSDARP00000073429; -.
DR PaxDb; Q5CZN0; -.
DR GeneID; 503747; -.
DR CTD; 503747; -.
DR ZFIN; ZDB-GENE-050306-28; fitm1l.
DR eggNOG; KOG3750; Eukaryota.
DR InParanoid; Q5CZN0; -.
DR OrthoDB; 1621925at2759; -.
DR PhylomeDB; Q5CZN0; -.
DR Reactome; R-DRE-8964572; Lipid particle organization.
DR PRO; PR:Q5CZN0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0019992; F:diacylglycerol binding; ISS:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03229; FITM1; 1.
DR HAMAP; MF_03230; FITM2; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046402; FIT1.
DR InterPro; IPR046401; FITM1/2.
DR PANTHER; PTHR23129; PTHR23129; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..290
FT /note="Fat storage-inducing transmembrane protein 1"
FT /id="PRO_0000350631"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 290 AA; 32458 MW; E5E1CC56E78AB31D CRC64;
MFLNSILVVI TDLAAGLLGN TSFRRHFHLL LSALLLFGPL LSLWVSHYSV FAKRTHFLYR
VFLRSGWGWT CIFVGSFVFV LSFSVRRSLT LSLRHLSRLA VAGGLWLGFR KLLCLLENAT
GSCYEPLSAA LEMTSGTNGE GQPLLLLREA ETKETCVRSG MLWRGYEVSE DALLLCLCCL
LLAEETAVFG PYLNLGGPSE APLRILFLFC VLLLSLWVFL LLCLLAYFPE FPTQLLGGAL
GCLSWRALYQ GWYRLRPSWY CPGRPGVGLL STQSKQDELL ETQTNAKEID