ID LFG4_MOUSE Reviewed; 238 AA.
AC Q9DA39;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Protein lifeguard 4;
DE AltName: Full=Transmembrane BAX inhibitor motif-containing protein 4;
DE AltName: Full=Z-protein;
GN Name=Tmbim4; Synonyms=Lfg4;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19784873; DOI=10.1007/s10495-009-0402-2;
RA Hu L., Smith T.F., Goldberger G.;
RT "LFG: a candidate apoptosis regulatory gene family.";
RL Apoptosis 14:1255-1265(2009).
CC -!- FUNCTION: Anti-apoptotic protein which can inhibit apoptosis induced by
CC intrinsic and extrinsic apoptotic stimuli. Can modulate both
CC capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated
CC Ca2+ release (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ITPR3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
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DR EMBL; AK006207; BAB24458.1; -; mRNA.
DR CCDS; CCDS24205.1; -.
DR RefSeq; NP_080893.1; NM_026617.3.
DR AlphaFoldDB; Q9DA39; -.
DR SMR; Q9DA39; -.
DR BioGRID; 212733; 1.
DR STRING; 10090.ENSMUSP00000020446; -.
DR PhosphoSitePlus; Q9DA39; -.
DR MaxQB; Q9DA39; -.
DR PaxDb; 10090-ENSMUSP00000020446; -.
DR ProteomicsDB; 290022; -.
DR DNASU; 68212; -.
DR Ensembl; ENSMUST00000020446.11; ENSMUSP00000020446.5; ENSMUSG00000020225.11.
DR GeneID; 68212; -.
DR KEGG; mmu:68212; -.
DR UCSC; uc007hey.1; mouse.
DR AGR; MGI:1915462; -.
DR CTD; 51643; -.
DR MGI; MGI:1915462; Tmbim4.
DR VEuPathDB; HostDB:ENSMUSG00000020225; -.
DR eggNOG; KOG2322; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_058671_0_2_1; -.
DR InParanoid; Q9DA39; -.
DR OMA; FGVMSLY; -.
DR OrthoDB; 944911at2759; -.
DR PhylomeDB; Q9DA39; -.
DR TreeFam; TF321860; -.
DR BioGRID-ORCS; 68212; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Tmbim4; mouse.
DR PRO; PR:Q9DA39; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DA39; Protein.
DR Bgee; ENSMUSG00000020225; Expressed in right kidney and 242 other cell types or tissues.
DR ExpressionAtlas; Q9DA39; baseline and differential.
DR Genevisible; Q9DA39; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR CDD; cd10429; GAAP_like; 1.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR PANTHER; PTHR23291:SF129; GROWTH HORMONE-INDUCIBLE TRANSMEMBRANE PROTEIN-RELATED; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..238
FT /note="Protein lifeguard 4"
FT /id="PRO_0000179093"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..68
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..120
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..175
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 26647 MW; 67F3B6ECA496C9F7 CRC64;
MADTDPGYPR SSIEDDFNYG SCVASASVHI RMAFLRKVYS ILSLQVLLTT VTSALFLYFQ
ALRTFVHESP ALIVVFALGS LGLIFALTLH RHTHPLNLYL LFAFTLSESL AVAAVVTFYD
VYLVLQAFIM TTAVFLGLTA YTLQSKRDFT KFGAGLFAGL WILCLAGFLK LFFYSETMEL
VLASLGALLF CGFIIYDTHS LMHRLSPEEY VIAAISLYMD IINLFLHLLK FLEAVNKK
//
