IFM5_MOUSE
ID IFM5_MOUSE Reviewed; 134 AA.
AC O88728;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Interferon-induced transmembrane protein 5;
DE AltName: Full=Bone-restricted interferon-induced transmembrane protein-like protein;
DE Short=Bril;
DE AltName: Full=Dispanin subfamily A member 1;
DE Short=DSPA1;
DE AltName: Full=Fragilis family member 4;
GN Name=Ifitm5; Synonyms=Bril, Fragilis4;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11106657; DOI=10.1074/jbc.m008354200;
RA Baird J., Ryan K., Hayes I.M., Hampson L., Clark C.M., Wootton A.,
RA Ansell J., Menzel U., Hole N., Graham G.J.;
RT "Differentiating embryonal stem cells are a rich source of haemopoietic
RT gene products and suggest erythroid preconditioning of primitive
RT haemopoietic stem cells.";
RL J. Biol. Chem. 276:9189-9198(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND TOPOLOGY.
RC STRAIN=C57BL/6J; TISSUE=Osteoblast;
RX PubMed=18442316; DOI=10.1359/jbmr.080412;
RA Moffatt P., Gaumond M.H., Salois P., Sellin K., Bessette M.C., Godin E.,
RA Tambasco de Oliveira P., Atkins G.J., Nanci A., Thomas G.;
RT "Bril: a novel bone-specific modulator of mineralization.";
RL J. Bone Miner. Res. 23:1497-1508(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP INDUCTION.
RC STRAIN=129;
RX PubMed=12659663; DOI=10.1186/1471-213x-3-1;
RA Lange U.C., Saitou M., Western P.S., Barton S.C., Surani M.A.;
RT "The fragilis interferon-inducible gene family of transmembrane proteins is
RT associated with germ cell specification in mice.";
RL BMC Dev. Biol. 3:1-1(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP FKBP11.
RX PubMed=20838829; DOI=10.1007/s00774-010-0221-0;
RA Hanagata N., Li X., Morita H., Takemura T., Li J., Minowa T.;
RT "Characterization of the osteoblast-specific transmembrane protein IFITM5
RT and analysis of IFITM5-deficient mice.";
RL J. Bone Miner. Metab. 29:279-290(2011).
RN [7]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [8]
RP FUNCTION, PALMITOYLATION AT CYS-52; CYS-53 AND CYS-86, INTERACTION WITH
RP FKBP11, AND MUTAGENESIS OF CYS-52; CYS-53 AND CYS-86.
RX PubMed=24058703; DOI=10.1371/journal.pone.0075831;
RA Tsukamoto T., Li X., Morita H., Minowa T., Aizawa T., Hanagata N.,
RA Demura M.;
RT "Role of S-palmitoylation on IFITM5 for the interaction with FKBP11 in
RT osteoblast cells.";
RL PLoS ONE 8:E75831-E75831(2013).
RN [9]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-52; CYS-53 AND CYS-86,
RP TOPOLOGY, AND MUTAGENESIS OF SER-42; CYS-52; CYS-53 AND CYS-86.
RX PubMed=24715519; DOI=10.1002/jbmr.2243;
RA Patoine A., Gaumond M.H., Jaiswal P.K., Fassier F., Rauch F., Moffatt P.;
RT "Topological mapping of BRIL reveals a type II orientation and effects of
RT osteogenesis imperfecta mutations on its cellular destination.";
RL J. Bone Miner. Res. 29:2004-2016(2014).
CC -!- FUNCTION: Required for normal bone mineralization.
CC {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:20838829,
CC ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}.
CC -!- SUBUNIT: Interacts with FKBP11. {ECO:0000269|PubMed:20838829,
CC ECO:0000269|PubMed:24058703}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18442316,
CC ECO:0000269|PubMed:24715519}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:18442316}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic bone (at protein level)
CC (PubMed:18442316). Highly expressed in osteoblasts of adults and
CC embryos. Expressed in primitive hemopoietic cells.
CC {ECO:0000269|PubMed:11106657, ECO:0000269|PubMed:18442316}.
CC -!- DEVELOPMENTAL STAGE: In embryos at 16.5 dpf, detected in lumbar and
CC thoracic vertebra, the basisphenoid bone, the mandible, the coronal
CC suture between the frontal and parietal bones, the maxilla, the nasal
CC bone and the palate, as well as in the bone collars of long bones and
CC digital bones in hind limbs, and in the primary ossification center.
CC {ECO:0000269|PubMed:20838829}.
CC -!- INDUCTION: By interferons. {ECO:0000269|PubMed:12659663}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:24058703,
CC ECO:0000269|PubMed:24715519}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality, leading to the birth of only
CC 7% homozygous mutant pups, instead of the expected 25%. Only two out of
CC eight pups were female. Crossing homozygous mice gave rise to about one
CC sixth of the normal litter size, and many newborns died within 48 hours
CC after birth. Homozygous newborns display no striking phenotype other
CC than smaller bones and especially shorter long bones, and this
CC phenotype persists into adulthood. The radius, ulna and tibia are
CC frequently bent in newborns, but this is no longer the case in young
CC adults. {ECO:0000269|PubMed:20838829}.
CC -!- MISCELLANEOUS: Membrane topology is controversial. The N-terminus is
CC cytoplasmic and the C-terminus extracellular according to
CC PubMed:24715519, while both the N-terminus and the C-terminus are
CC extracellular according to PubMed:18442316.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AJ009781; CAA08829.1; -; mRNA.
DR EMBL; EU380257; ABZ85873.1; -; mRNA.
DR EMBL; FJ200451; ACI26732.1; -; mRNA.
DR EMBL; CH466531; EDL17974.1; -; Genomic_DNA.
DR EMBL; BC103790; AAI03791.1; -; mRNA.
DR EMBL; BK001124; DAA01239.1; -; mRNA.
DR CCDS; CCDS21993.1; -.
DR RefSeq; NP_444318.1; NM_053088.2.
DR AlphaFoldDB; O88728; -.
DR STRING; 10090.ENSMUSP00000026562; -.
DR TCDB; 8.A.58.1.4; the dispanin (dispanin) family.
DR PhosphoSitePlus; O88728; -.
DR SwissPalm; O88728; -.
DR PaxDb; O88728; -.
DR PRIDE; O88728; -.
DR ProteomicsDB; 266953; -.
DR Antibodypedia; 41962; 124 antibodies from 20 providers.
DR Ensembl; ENSMUST00000026562; ENSMUSP00000026562; ENSMUSG00000025489.
DR GeneID; 73835; -.
DR KEGG; mmu:73835; -.
DR UCSC; uc009kiy.1; mouse.
DR CTD; 387733; -.
DR MGI; MGI:1934923; Ifitm5.
DR VEuPathDB; HostDB:ENSMUSG00000025489; -.
DR eggNOG; ENOG502RXZM; Eukaryota.
DR GeneTree; ENSGT00950000182857; -.
DR HOGENOM; CLU_124511_2_0_1; -.
DR InParanoid; O88728; -.
DR OMA; HLVISIR; -.
DR OrthoDB; 1555189at2759; -.
DR PhylomeDB; O88728; -.
DR TreeFam; TF334894; -.
DR BioGRID-ORCS; 73835; 0 hits in 72 CRISPR screens.
DR PRO; PR:O88728; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88728; protein.
DR Bgee; ENSMUSG00000025489; Expressed in vault of skull and 66 other tissues.
DR Genevisible; O88728; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:UniProtKB.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:UniProtKB-KW.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Lipoprotein; Membrane;
KW Mineral balance; Palmitate; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..134
FT /note="Interferon-induced transmembrane protein 5"
FT /id="PRO_0000397676"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..134
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:18442316,
FT ECO:0000269|PubMed:24715519"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 52
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:24058703,
FT ECO:0000305|PubMed:24715519"
FT LIPID 53
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:24058703,
FT ECO:0000305|PubMed:24715519"
FT LIPID 86
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:24058703,
FT ECO:0000305|PubMed:24715519"
FT MUTAGEN 42
FT /note="S->L: Abolishes expression at the cell membrane."
FT /evidence="ECO:0000269|PubMed:24715519"
FT MUTAGEN 52
FT /note="C->A: Strongly reduces expression at the cell
FT membrane. Reduces palmitoylation; when associated with A-
FT 53. Abolishes palmitoylation; when associated with A-53 and
FT A-86."
FT /evidence="ECO:0000269|PubMed:24058703,
FT ECO:0000269|PubMed:24715519"
FT MUTAGEN 53
FT /note="C->A: Strongly reduces expression at the cell
FT membrane. Reduces palmitoylation; when associated with A-
FT 52. Abolishes palmitoylation; when associated with A-52 and
FT A-86."
FT /evidence="ECO:0000269|PubMed:24058703,
FT ECO:0000269|PubMed:24715519"
FT MUTAGEN 86
FT /note="C->A: No effect on location at the cell membrane.
FT Abolishes palmitoylation; when associated with A-52 and A-
FT 53."
FT /evidence="ECO:0000269|PubMed:24058703,
FT ECO:0000269|PubMed:24715519"
SQ SEQUENCE 134 AA; 14667 MW; EED20D259EEDD712 CRC64;
MDTSYPREDP RAPSSRKADA AAHTALSMGT PGPTPRDHML WSVFSTMYLN LCCLGFLALV
HSVKARDQKM AGNLEAARQY GSKAKCYNIL AAMWTLVPPL LLLGLVVTGA LHLSKLAKDS
AAFFSTKFDE EDYN
