LFG3_MOUSE
ID LFG3_MOUSE Reviewed; 309 AA.
AC Q8BJZ3; Q8CH91; Q99KB6;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein lifeguard 3;
DE AltName: Full=Responsive to centrifugal force and shear stress gene 1 protein;
DE Short=Protein RECS1;
DE AltName: Full=Transmembrane BAX inhibitor motif-containing protein 1;
GN Name=Tmbim1; Synonyms=Lfg3, Recs1;
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] (ISOFORM 1).
RA Zhao H., Kimura S., Nojima H.;
RT "Mus musculus RECS1 (responsive to centrifugal force and shear stress gene
RT 1).";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16636500; DOI=10.1253/circj.70.615;
RA Zhao H., Ito A., Sakai N., Matsuzawa Y., Yamashita S., Nojima H.;
RT "RECS1 is a negative regulator of matrix metalloproteinase-9 production and
RT aged RECS1 knockout mice are prone to aortic dilation.";
RL Circ. J. 70:615-624(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16607040; DOI=10.1266/ggs.81.41;
RA Zhao H., Ito A., Kimura S.H., Yabuta N., Sakai N., Ikawa M., Okabe M.,
RA Matsuzawa Y., Yamashita S., Nojima H.;
RT "RECS1 deficiency in mice induces susceptibility to cystic medial
RT degeneration.";
RL Genes Genet. Syst. 81:41-50(2006).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Negatively regulates aortic matrix metalloproteinase-9 (MMP9)
CC production and may play a protective role in vascular remodeling.
CC {ECO:0000269|PubMed:16607040, ECO:0000269|PubMed:16636500}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Lysosome membrane {ECO:0000250}. Endosome
CC membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BJZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJZ3-2; Sequence=VSP_008995, VSP_008996;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues except spleen, thymus and
CC testis. {ECO:0000269|PubMed:16607040}.
CC -!- DISRUPTION PHENOTYPE: Mice (older than 14 months) are prone to aortic
CC dilation as well as cystic medial degeneration (CMD).
CC {ECO:0000269|PubMed:16607040, ECO:0000269|PubMed:16636500}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to non-canonical splice donor and
CC acceptor sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
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DR EMBL; AB097685; BAC43762.1; -; mRNA.
DR EMBL; AK077689; BAC36957.1; -; mRNA.
DR EMBL; BC004752; AAH04752.1; -; mRNA.
DR CCDS; CCDS15044.1; -. [Q8BJZ3-1]
DR RefSeq; NP_081430.3; NM_027154.5.
DR AlphaFoldDB; Q8BJZ3; -.
DR SMR; Q8BJZ3; -.
DR STRING; 10090.ENSMUSP00000016309; -.
DR iPTMnet; Q8BJZ3; -.
DR PhosphoSitePlus; Q8BJZ3; -.
DR jPOST; Q8BJZ3; -.
DR MaxQB; Q8BJZ3; -.
DR PaxDb; Q8BJZ3; -.
DR PRIDE; Q8BJZ3; -.
DR ProteomicsDB; 291942; -. [Q8BJZ3-1]
DR ProteomicsDB; 291943; -. [Q8BJZ3-2]
DR GeneID; 69660; -.
DR KEGG; mmu:69660; -.
DR CTD; 64114; -.
DR MGI; MGI:1916910; Tmbim1.
DR eggNOG; KOG2322; Eukaryota.
DR InParanoid; Q8BJZ3; -.
DR PhylomeDB; Q8BJZ3; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 69660; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8BJZ3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BJZ3; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005123; F:death receptor binding; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:1902045; P:negative regulation of Fas signaling pathway; ISS:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:2000504; P:positive regulation of blood vessel remodeling; IMP:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:UniProtKB.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Protein lifeguard 3"
FT /id="PRO_0000179091"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969X1"
FT VAR_SEQ 118..161
FT /note="FTFVEPVGKYVRNNVAVYYVSYAVFLVTYLTLACCQGPRRRFPW -> STWS
FT MQLWGPSVSPCSWLMTHSWSWGTGSTPSARRTTSQAPYRSTQI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008995"
FT VAR_SEQ 162..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008996"
FT CONFLICT 162
FT /note="D -> N (in Ref. 1; BAC43762)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> T (in Ref. 1; BAC43762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34393 MW; 3C33B9879E944B2F CRC64;
MSNPSAPPPY EDHNPLYPGS PPPGGYGQPS VLPGGYPAYP AYPQPGYGHP AGYPQPVPPV
HPMPMNYGHD YNEEERAGSD SFRPGEWDDR KVRHSFIQKV YCIISVQLLI TVAIIAIFTF
VEPVGKYVRN NVAVYYVSYA VFLVTYLTLA CCQGPRRRFP WDIILLTIFT LALGFVTGTI
SSMYENKAVI IAMIITAVVS ISVTIFCFQT KVDFTSCTGL FCVLGIVLMV TGIVTSIVLI
FKYIYWLHMV YAALGAICFT LFLAYDTQLV LGNRKHTISP EDYITGALQI YTDIVYIFTF
VLQLVGSRD
