LFG3_HUMAN
ID LFG3_HUMAN Reviewed; 311 AA.
AC Q969X1; B3KQY6; Q8N1R3; Q8TAM3; Q96K13;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein lifeguard 3;
DE AltName: Full=Protein RECS1 homolog;
DE AltName: Full=Transmembrane BAX inhibitor motif-containing protein 1;
GN Name=TMBIM1; Synonyms=LFG3, RECS1; ORFNames=PP1201, PSEC0158;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-21.
RC TISSUE=Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-21.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-21.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Pancreas;
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 [6]
RP SUBCELLULAR LOCATION.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Negatively regulates aortic matrix metalloproteinase-9 (MMP9)
CC production and may play a protective role in vascular remodeling.
CC -!- INTERACTION:
CC Q969X1; Q8NCR0: B3GALNT2; NbExp=3; IntAct=EBI-2820569, EBI-12934759;
CC Q969X1; Q13323: BIK; NbExp=3; IntAct=EBI-2820569, EBI-700794;
CC Q969X1; P20138: CD33; NbExp=3; IntAct=EBI-2820569, EBI-3906571;
CC Q969X1; Q6P531: GGT6; NbExp=3; IntAct=EBI-2820569, EBI-2868927;
CC Q969X1; Q9HC23: PROK2; NbExp=3; IntAct=EBI-2820569, EBI-13045372;
CC Q969X1; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-2820569, EBI-12375429;
CC Q969X1; Q14973: SLC10A1; NbExp=3; IntAct=EBI-2820569, EBI-3923031;
CC Q969X1; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-2820569, EBI-10315004;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Lysosome membrane {ECO:0000269|PubMed:16607040}.
CC Endosome membrane {ECO:0000269|PubMed:16607040}.
CC -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26693.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB55346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11636.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK027755; BAB55346.1; ALT_INIT; mRNA.
DR EMBL; AK090618; BAG52198.1; -; mRNA.
DR EMBL; AK095270; BAC04516.1; ALT_SEQ; mRNA.
DR EMBL; AF193045; AAG22473.1; -; mRNA.
DR EMBL; AK075465; BAC11636.1; ALT_INIT; mRNA.
DR EMBL; CH471063; EAW70607.1; -; Genomic_DNA.
DR EMBL; BC007980; AAH07980.1; -; mRNA.
DR EMBL; BC013428; AAH13428.1; -; mRNA.
DR EMBL; BC026348; AAH26348.1; -; mRNA.
DR EMBL; BC026693; AAH26693.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2412.1; -.
DR RefSeq; NP_001308356.1; NM_001321427.1.
DR RefSeq; NP_001308357.1; NM_001321428.1.
DR RefSeq; NP_001308358.1; NM_001321429.1.
DR RefSeq; NP_001308359.1; NM_001321430.1.
DR RefSeq; NP_001308361.1; NM_001321432.1.
DR RefSeq; NP_001308362.1; NM_001321433.1.
DR RefSeq; NP_001308364.1; NM_001321435.1.
DR RefSeq; NP_001308365.1; NM_001321436.1.
DR RefSeq; NP_071435.2; NM_022152.5.
DR RefSeq; XP_011509929.1; XM_011511627.1.
DR AlphaFoldDB; Q969X1; -.
DR SMR; Q969X1; -.
DR BioGRID; 122070; 21.
DR IntAct; Q969X1; 18.
DR MINT; Q969X1; -.
DR STRING; 9606.ENSP00000409738; -.
DR TCDB; 1.A.14.3.10; the calcium transporter a (cata) (formerly the testis-enhanced gene transfer (tegt) family.
DR iPTMnet; Q969X1; -.
DR PhosphoSitePlus; Q969X1; -.
DR SwissPalm; Q969X1; -.
DR BioMuta; TMBIM1; -.
DR DMDM; 93117549; -.
DR EPD; Q969X1; -.
DR jPOST; Q969X1; -.
DR MassIVE; Q969X1; -.
DR MaxQB; Q969X1; -.
DR PaxDb; Q969X1; -.
DR PeptideAtlas; Q969X1; -.
DR PRIDE; Q969X1; -.
DR ProteomicsDB; 75867; -.
DR Antibodypedia; 2868; 196 antibodies from 27 providers.
DR DNASU; 64114; -.
DR Ensembl; ENST00000258412.8; ENSP00000258412.3; ENSG00000135926.15.
DR Ensembl; ENST00000396809.6; ENSP00000380025.2; ENSG00000135926.15.
DR Ensembl; ENST00000444881.5; ENSP00000409738.1; ENSG00000135926.15.
DR GeneID; 64114; -.
DR KEGG; hsa:64114; -.
DR MANE-Select; ENST00000258412.8; ENSP00000258412.3; NM_022152.6; NP_071435.2.
DR UCSC; uc002vho.2; human.
DR CTD; 64114; -.
DR DisGeNET; 64114; -.
DR GeneCards; TMBIM1; -.
DR HGNC; HGNC:23410; TMBIM1.
DR HPA; ENSG00000135926; Low tissue specificity.
DR MIM; 610364; gene.
DR neXtProt; NX_Q969X1; -.
DR OpenTargets; ENSG00000135926; -.
DR PharmGKB; PA142670804; -.
DR VEuPathDB; HostDB:ENSG00000135926; -.
DR eggNOG; KOG2322; Eukaryota.
DR GeneTree; ENSGT01050000244890; -.
DR HOGENOM; CLU_058671_3_0_1; -.
DR InParanoid; Q969X1; -.
DR OMA; IYWLHML; -.
DR OrthoDB; 1290306at2759; -.
DR PhylomeDB; Q969X1; -.
DR TreeFam; TF319996; -.
DR PathwayCommons; Q969X1; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q969X1; -.
DR BioGRID-ORCS; 64114; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; TMBIM1; human.
DR GenomeRNAi; 64114; -.
DR Pharos; Q969X1; Tbio.
DR PRO; PR:Q969X1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q969X1; protein.
DR Bgee; ENSG00000135926; Expressed in lower esophagus mucosa and 199 other tissues.
DR ExpressionAtlas; Q969X1; baseline and differential.
DR Genevisible; Q969X1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0005123; F:death receptor binding; IDA: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; ISS:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:1902045; P:negative regulation of Fas signaling pathway; IMP:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:2000504; P:positive regulation of blood vessel remodeling; 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 Endosome; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Protein lifeguard 3"
FT /id="PRO_0000179090"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..72
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 50..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJZ3"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 21
FT /note="P -> L (in dbSNP:rs2292553)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15498874, ECO:0000269|PubMed:16303743"
FT /id="VAR_017382"
FT CONFLICT 119
FT /note="I -> T (in Ref. 1; BAC04516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34607 MW; 12B5741A60C1487F CRC64;
MSNPSAPPPY EDRNPLYPGP PPPGGYGQPS VLPGGYPAYP GYPQPGYGHP AGYPQPMPPT
HPMPMNYGPG HGYDGEERAV SDSFGPGEWD DRKVRHTFIR KVYSIISVQL LITVAIIAIF
TFVEPVSAFV RRNVAVYYVS YAVFVVTYLI LACCQGPRRR FPWNIILLTL FTFAMGFMTG
TISSMYQTKA VIIAMIITAV VSISVTIFCF QTKVDFTSCT GLFCVLGIVL LVTGIVTSIV
LYFQYVYWLH MLYAALGAIC FTLFLAYDTQ LVLGNRKHTI SPEDYITGAL QIYTDIIYIF
TFVLQLMGDR N
