TM41B_HUMAN
ID TM41B_HUMAN Reviewed; 291 AA.
AC Q5BJD5; D3DQU9; E9PP29; Q15055; Q4G0P0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transmembrane protein 41B {ECO:0000305};
DE AltName: Full=Protein stasimon {ECO:0000303|PubMed:30352685};
GN Name=TMEM41B {ECO:0000303|PubMed:30352685, ECO:0000312|HGNC:HGNC:28948};
GN Synonyms=KIAA0033 {ECO:0000303|PubMed:7584026};
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] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH COPA; COPB1; VDAC1 AND ERLIN2.
RX PubMed=30352685; DOI=10.1016/j.bbrc.2018.10.073;
RA Van Alstyne M., Lotti F., Dal Mas A., Area-Gomez E., Pellizzoni L.;
RT "Stasimon/Tmem41b localizes to mitochondria-associated ER membranes and is
RT essential for mouse embryonic development.";
RL Biochem. Biophys. Res. Commun. 506:463-470(2018).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30126924; DOI=10.15252/embr.201845889;
RA Moretti F., Bergman P., Dodgson S., Marcellin D., Claerr I., Goodwin J.M.,
RA DeJesus R., Kang Z., Antczak C., Begue D., Bonenfant D., Graff A.,
RA Genoud C., Reece-Hoyes J.S., Russ C., Yang Z., Hoffman G.R., Mueller M.,
RA Murphy L.O., Xavier R.J., Nyfeler B.;
RT "TMEM41B is a novel regulator of autophagy and lipid mobilization.";
RL EMBO Rep. 19:0-0(2018).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VMP1, AND REGION VTT
RP DOMAIN.
RX PubMed=30093494; DOI=10.1083/jcb.201804132;
RA Morita K., Hama Y., Izume T., Tamura N., Ueno T., Yamashita Y.,
RA Sakamaki Y., Mimura K., Morishita H., Shihoya W., Nureki O., Mano H.,
RA Mizushima N.;
RT "Genome-wide CRISPR screen identifies TMEM41B as a gene required for
RT autophagosome formation.";
RL J. Cell Biol. 217:3817-3828(2018).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30933966; DOI=10.1371/journal.pbio.2007044;
RA Shoemaker C.J., Huang T.Q., Weir N.R., Polyakov N.J., Schultz S.W.,
RA Denic V.;
RT "CRISPR screening using an expanded toolkit of autophagy reporters
RT identifies TMEM41B as a novel autophagy factor.";
RL PLoS Biol. 17:E2007044-E2007044(2019).
RN [14]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=33382968; DOI=10.1016/j.cell.2020.12.006;
RA Schneider W.M., Luna J.M., Hoffmann H.H., Sanchez-Rivera F.J., Leal A.A.,
RA Ashbrook A.W., Le Pen J., Ricardo-Lax I., Michailidis E., Peace A.,
RA Stenzel A.F., Lowe S.W., MacDonald M.R., Rice C.M., Poirier J.T.;
RT "Genome-Scale Identification of SARS-CoV-2 and Pan-coronavirus Host Factor
RT Networks.";
RL Cell 0:0-0(2020).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), DOMAIN (MICROBIAL INFECTION),
RP CHARACTERIZATION OF VARIANTS LEU-266 AND VAL-266, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ZIKA VIRUS NS4A PROTEIN AND YELLOW FEVER VIRUS NS4B
RP PROTEIN (MICROBIAL INFECTION).
RX PubMed=33338421; DOI=10.1016/j.cell.2020.12.005;
RA Hoffmann H.H., Schneider W.M., Rozen-Gagnon K., Miles L.A., Schuster F.,
RA Razooky B., Jacobson E., Wu X., Yi S., Rudin C.M., MacDonald M.R.,
RA McMullan L.K., Poirier J.T., Rice C.M.;
RT "TMEM41B Is a Pan-flavivirus Host Factor.";
RL Cell 0:0-0(2020).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SURF4.
RX PubMed=34015269; DOI=10.1016/j.cmet.2021.05.006;
RA Huang D., Xu B., Liu L., Wu L., Zhu Y., Ghanbarpour A., Wang Y., Chen F.J.,
RA Lyu J., Hu Y., Kang Y., Zhou W., Wang X., Ding W., Li X., Jiang Z.,
RA Chen J., Zhang X., Zhou H., Li J.Z., Guo C., Zheng W., Zhang X., Li P.,
RA Melia T., Reinisch K., Chen X.W.;
RT "TMEM41B acts as an ER scramblase required for lipoprotein biogenesis and
RT lipid homeostasis.";
RL Cell Metab. 0:0-0(2021).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33929485; DOI=10.1083/jcb.202103105;
RA Li Y.E., Wang Y., Du X., Zhang T., Mak H.Y., Hancock S.E., McEwen H.,
RA Pandzic E., Whan R.M., Aw Y.C., Lukmantara I.E., Yuan Y., Dong X., Don A.,
RA Turner N., Qi S., Yang H.;
RT "TMEM41B and VMP1 are scramblases and regulate the distribution of
RT cholesterol and phosphatidylserine.";
RL J. Cell Biol. 220:0-0(2021).
RN [18]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=34043740; DOI=10.1371/journal.ppat.1009599;
RA Trimarco J.D., Heaton B.E., Chaparian R.R., Burke K.N., Binder R.A.,
RA Gray G.C., Smith C.M., Menachery V.D., Heaton N.S.;
RT "TMEM41B is a host factor required for the replication of diverse
RT coronaviruses including SARS-CoV-2.";
RL PLoS Pathog. 17:e1009599-e1009599(2021).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ATG2A.
RX PubMed=33850023; DOI=10.1073/pnas.2101562118;
RA Ghanbarpour A., Valverde D.P., Melia T.J., Reinisch K.M.;
RT "A model for a partnership of lipid transfer proteins and scramblases in
RT membrane expansion and organelle biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes (PubMed:34015269, PubMed:33929485,
CC PubMed:33850023). Has phospholipid scramblase activity toward
CC cholesterol and phosphatidylserine, as well as phosphatidylethanolamine
CC and phosphatidylcholine (PubMed:34015269, PubMed:33929485,
CC PubMed:33850023). Required for autophagosome formation: participates in
CC early stages of autophagosome biogenesis at the endoplasmic reticulum
CC (ER) membrane by reequilibrating the leaflets of the ER as lipids are
CC extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly
CC (PubMed:30093494, PubMed:30126924, PubMed:30933966, PubMed:34015269,
CC PubMed:33929485, PubMed:34043740, PubMed:33850023). In addition to
CC autophagy, involved in other processes in which phospholipid scramblase
CC activity is required (PubMed:33850023). Required for normal motor
CC neuron development (By similarity). {ECO:0000250|UniProtKB:A1A5V7,
CC ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30126924,
CC ECO:0000269|PubMed:30933966, ECO:0000269|PubMed:33850023,
CC ECO:0000269|PubMed:33929485, ECO:0000269|PubMed:34015269,
CC ECO:0000269|PubMed:34043740}.
CC -!- FUNCTION: (Microbial infection) Critical host factor required for
CC infection by human coronaviruses SARS-CoV-2, HCoV-OC43, HCoV-NL63, and
CC HCoV-229E, as well as all flaviviruses tested such as Zika virus and
CC Yellow fever virus (PubMed:33382968, PubMed:33338421). Required post-
CC entry of the virus to facilitate the ER membrane remodeling necessary
CC to form replication organelles (PubMed:33382968).
CC {ECO:0000269|PubMed:33338421, ECO:0000269|PubMed:33382968,
CC ECO:0000269|PubMed:34043740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:33929485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:33929485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:33850023,
CC ECO:0000269|PubMed:33929485, ECO:0000269|PubMed:34015269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:33850023,
CC ECO:0000269|PubMed:33929485};
CC -!- SUBUNIT: Interacts with VMP1 (PubMed:30093494). Interacts with COPA,
CC COPB1, VDAC1 and ERLIN2 (PubMed:30352685). Interacts with ATG2A
CC (PubMed:33850023). Interacts with SURF4 (PubMed:34015269).
CC {ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30352685,
CC ECO:0000269|PubMed:33850023, ECO:0000269|PubMed:34015269}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Zika virus NS4A protein
CC and Yellow fever virus NS4B protein. {ECO:0000269|PubMed:33338421}.
CC -!- INTERACTION:
CC Q5BJD5; A0A142I5B9; Xeno; NbExp=3; IntAct=EBI-1055840, EBI-20625235;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30126924,
CC ECO:0000269|PubMed:30352685, ECO:0000269|PubMed:30933966,
CC ECO:0000269|PubMed:33338421, ECO:0000269|PubMed:34015269,
CC ECO:0000269|PubMed:34043740}; Multi-pass membrane protein
CC {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:34015269}.
CC Note=Localized to specific membrane structures termed mitochondria-
CC associated membranes (MAMs) which connect the endoplasmic reticulum
CC (ER) and the mitochondria. {ECO:0000269|PubMed:30352685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33338421}.
CC Note=(Microbial infection) Upon infection with infection with
CC flaviviruses, diffuse reticular-like pattern to a large cytosolic
CC aggregate that colocalizes with viral non-structural proteins, NS4A
CC (ZIKV) and NS4B (YFV). {ECO:0000269|PubMed:33338421}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5BJD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BJD5-2; Sequence=VSP_026316, VSP_026317;
CC Name=3;
CC IsoId=Q5BJD5-3; Sequence=VSP_045268, VSP_045269;
CC -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As
CC there is no evidence that this domain associates with SNARE proteins,
CC it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
CC {ECO:0000305|PubMed:30093494}.
CC -!- DOMAIN: (Microbial infection) VTT domain is required for flavivirus
CC infection. {ECO:0000269|PubMed:33338421}.
CC -!- SIMILARITY: Belongs to the TMEM41 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05062.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D26067; BAA05062.1; ALT_INIT; mRNA.
DR EMBL; DA149513; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC055845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68594.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68597.1; -; Genomic_DNA.
DR EMBL; BC035034; AAH35034.1; -; mRNA.
DR EMBL; BC044597; AAH44597.1; -; mRNA.
DR EMBL; BC091524; AAH91524.1; -; mRNA.
DR CCDS; CCDS31424.1; -. [Q5BJD5-1]
DR CCDS; CCDS53600.1; -. [Q5BJD5-3]
DR RefSeq; NP_001158502.1; NM_001165030.2. [Q5BJD5-3]
DR RefSeq; NP_055827.1; NM_015012.3. [Q5BJD5-1]
DR AlphaFoldDB; Q5BJD5; -.
DR BioGRID; 136224; 165.
DR IntAct; Q5BJD5; 6.
DR STRING; 9606.ENSP00000433126; -.
DR TCDB; 9.B.27.1.8; the death effector domain a (deda) family.
DR GlyGen; Q5BJD5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5BJD5; -.
DR PhosphoSitePlus; Q5BJD5; -.
DR SwissPalm; Q5BJD5; -.
DR BioMuta; TMEM41B; -.
DR DMDM; 74741383; -.
DR EPD; Q5BJD5; -.
DR jPOST; Q5BJD5; -.
DR MassIVE; Q5BJD5; -.
DR MaxQB; Q5BJD5; -.
DR PaxDb; Q5BJD5; -.
DR PeptideAtlas; Q5BJD5; -.
DR PRIDE; Q5BJD5; -.
DR ProteomicsDB; 22598; -.
DR ProteomicsDB; 62674; -. [Q5BJD5-1]
DR ProteomicsDB; 62675; -. [Q5BJD5-2]
DR Antibodypedia; 11559; 15 antibodies from 10 providers.
DR DNASU; 440026; -.
DR Ensembl; ENST00000299596.8; ENSP00000299596.4; ENSG00000166471.11. [Q5BJD5-1]
DR Ensembl; ENST00000524543.5; ENSP00000431934.1; ENSG00000166471.11. [Q5BJD5-2]
DR Ensembl; ENST00000528080.6; ENSP00000433126.1; ENSG00000166471.11. [Q5BJD5-1]
DR Ensembl; ENST00000533723.1; ENSP00000436480.1; ENSG00000166471.11. [Q5BJD5-3]
DR Ensembl; ENST00000611268.4; ENSP00000480141.1; ENSG00000166471.11. [Q5BJD5-1]
DR GeneID; 440026; -.
DR KEGG; hsa:440026; -.
DR MANE-Select; ENST00000528080.6; ENSP00000433126.1; NM_015012.4; NP_055827.1.
DR UCSC; uc001mhm.5; human. [Q5BJD5-1]
DR CTD; 440026; -.
DR DisGeNET; 440026; -.
DR GeneCards; TMEM41B; -.
DR HGNC; HGNC:28948; TMEM41B.
DR HPA; ENSG00000166471; Low tissue specificity.
DR neXtProt; NX_Q5BJD5; -.
DR OpenTargets; ENSG00000166471; -.
DR PharmGKB; PA134898265; -.
DR VEuPathDB; HostDB:ENSG00000166471; -.
DR eggNOG; KOG3140; Eukaryota.
DR GeneTree; ENSGT00940000156956; -.
DR HOGENOM; CLU_038944_0_1_1; -.
DR InParanoid; Q5BJD5; -.
DR OMA; CIKIPRD; -.
DR OrthoDB; 1222755at2759; -.
DR PhylomeDB; Q5BJD5; -.
DR TreeFam; TF314301; -.
DR PathwayCommons; Q5BJD5; -.
DR SignaLink; Q5BJD5; -.
DR BioGRID-ORCS; 440026; 132 hits in 1091 CRISPR screens.
DR ChiTaRS; TMEM41B; human.
DR GenomeRNAi; 440026; -.
DR Pharos; Q5BJD5; Tbio.
DR PRO; PR:Q5BJD5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q5BJD5; protein.
DR Bgee; ENSG00000166471; Expressed in middle temporal gyrus and 207 other tissues.
DR ExpressionAtlas; Q5BJD5; baseline and differential.
DR Genevisible; Q5BJD5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0032365; P:intracellular lipid transport; IDA:UniProtKB.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR InterPro; IPR032816; SNARE_assoc.
DR InterPro; IPR045014; TM41A/B.
DR PANTHER; PTHR43220; PTHR43220; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Endoplasmic reticulum;
KW Host-virus interaction; Lipid transport; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..291
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291937"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..251
FT /note="VTT domain; required for its function in autophagy"
FT /evidence="ECO:0000305|PubMed:30093494"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 123..127
FT /note="FLQTF -> LYPFN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045268"
FT VAR_SEQ 124..192
FT /note="LQTFAIPGSIFLSILSGFLYPFPLALFLVCLCSGLGASFCYMLSYLVGRPVV
FT YKYLTEKAVKWSQQVER -> YQLANICYSRLYISQYTLRVSLSLSTSLISCLFVFWTW
FT CLFLLYAFLFSWETSCIQIPNRESSKMVTAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026316"
FT VAR_SEQ 128..291
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045269"
FT VAR_SEQ 193..291
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026317"
FT VARIANT 266
FT /note="I -> L (reduced infection with flaviviruses such as
FT Yellow fever virus, Zika virus and Dengue virus; no effect
FT on mobilization of neutral lipids from lipid droplets)"
FT /evidence="ECO:0000269|PubMed:33338421"
FT /id="VAR_084309"
FT VARIANT 266
FT /note="I -> V (reduced infection with Yellow fever virus,
FT Zika virus and Dengue virus; no effect on mobilization of
FT neutral lipids from lipid droplets)"
FT /evidence="ECO:0000269|PubMed:33338421"
FT /id="VAR_084310"
SQ SEQUENCE 291 AA; 32513 MW; D782FBAF1698CD85 CRC64;
MAKGRVAERS QLGAHHTTPV GDGAAGTRGL AAPGSRDHQK EKSWVEAGSA RMSLLILVSI
FLSAAFVMFL VYKNFPQLSE EERVNMKVPR DMDDAKALGK VLSKYKDTFY VQVLVAYFAT
YIFLQTFAIP GSIFLSILSG FLYPFPLALF LVCLCSGLGA SFCYMLSYLV GRPVVYKYLT
EKAVKWSQQV ERHREHLINY IIFLRITPFL PNWFINITSP VINVPLKVFF IGTFLGVAPP
SFVAIKAGTT LYQLTTAGEA VSWNSIFILM ILAVLSILPA IFQKKLKQKF E
