TM41B_MOUSE
ID TM41B_MOUSE Reviewed; 291 AA.
AC Q8K1A5; Q3TKT0; Q3TLK6; Q8C1X2; Q8CBS5; Q8CBU5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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|MGI:MGI:1289225};
GN Synonyms=D7Ertd743e {ECO:0000312|MGI:MGI:1289225},
GN Kiaa0033 {ECO:0000303|PubMed:15368895};
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] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Blastocyst, Bone marrow, Cerebellum, Colon, Diencephalon, Egg, Head,
RC Hypothalamus, Mammary gland, Spleen, and Urinary bladder;
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 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Salivary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=23063131; DOI=10.1016/j.cell.2012.09.012;
RA Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W.,
RA Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.;
RT "An SMN-dependent U12 splicing event essential for motor circuit
RT function.";
RL Cell 151:440-454(2012).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Phospholipid scramblase involved in lipid homeostasis and
CC membrane dynamics processes. Has phospholipid scramblase activity
CC toward cholesterol and phosphatidylserine, as well as
CC phosphatidylethanolamine and phosphatidylcholine. Required for
CC autophagosome formation: participates in early stages of autophagosome
CC biogenesis at the endoplasmic reticulum (ER) membrane by
CC reequilibrating the leaflets of the ER as lipids are extracted by ATG2
CC (ATG2A or ATG2B) to mediate autophagosome assembly. In addition to
CC autophagy, involved in other processes in which phospholipid scramblase
CC activity is required (By similarity). Required for normal motor neuron
CC development (By similarity). {ECO:0000250|UniProtKB:A1A5V7,
CC ECO:0000250|UniProtKB:Q5BJD5}.
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:0000250|UniProtKB:Q5BJD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:Q5BJD5};
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:0000250|UniProtKB:Q5BJD5};
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:0000250|UniProtKB:Q5BJD5};
CC -!- SUBUNIT: Interacts with VMP1. Interacts with COPA, COPB1, VDAC1 and
CC ERLIN2. Interacts with ATG2A. Interacts with SURF4.
CC {ECO:0000250|UniProtKB:Q5BJD5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30352685}; Multi-pass membrane protein
CC {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5BJD5}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K1A5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1A5-2; Sequence=VSP_026319;
CC Name=3;
CC IsoId=Q8K1A5-3; Sequence=VSP_026318;
CC -!- TISSUE SPECIFICITY: Expressed in brain, spinal cord, kidney and first
CC lumbar dorsal root ganglia during postnatal development. Expressed in
CC motor neurons and proprioceptive neurons.
CC {ECO:0000269|PubMed:23063131}.
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:0000250|UniProtKB:Q5BJD5}.
CC -!- DISRUPTION PHENOTYPE: Causes early embryonic lethality
CC (PubMed:30352685). Conditional deletion in the liver leads to decreased
CC number of circulating lipoproteins (PubMed:30352685).
CC {ECO:0000269|PubMed:30352685}.
CC -!- SIMILARITY: Belongs to the TMEM41 family. {ECO:0000305}.
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DR EMBL; AK172876; BAD32154.1; -; mRNA.
DR EMBL; AK029327; BAC26397.1; -; mRNA.
DR EMBL; AK033997; BAC28541.1; -; mRNA.
DR EMBL; AK035266; BAC29008.1; -; mRNA.
DR EMBL; AK035365; BAC29048.1; -; mRNA.
DR EMBL; AK038953; BAC30179.1; -; mRNA.
DR EMBL; AK078357; BAC37235.1; -; mRNA.
DR EMBL; AK090100; BAC41091.1; -; mRNA.
DR EMBL; AK139961; BAE24197.1; -; mRNA.
DR EMBL; AK150353; BAE29490.1; -; mRNA.
DR EMBL; AK153048; BAE31676.1; -; mRNA.
DR EMBL; AK165226; BAE38087.1; -; mRNA.
DR EMBL; AK166427; BAE38770.1; -; mRNA.
DR EMBL; AK166455; BAE38786.1; -; mRNA.
DR EMBL; AK166845; BAE39064.1; -; mRNA.
DR EMBL; BC026515; AAH26515.1; -; mRNA.
DR EMBL; BC027103; AAH27103.1; -; mRNA.
DR CCDS; CCDS21742.1; -. [Q8K1A5-1]
DR RefSeq; NP_705745.3; NM_153525.5. [Q8K1A5-1]
DR AlphaFoldDB; Q8K1A5; -.
DR BioGRID; 231436; 1.
DR STRING; 10090.ENSMUSP00000091641; -.
DR iPTMnet; Q8K1A5; -.
DR PhosphoSitePlus; Q8K1A5; -.
DR SwissPalm; Q8K1A5; -.
DR EPD; Q8K1A5; -.
DR MaxQB; Q8K1A5; -.
DR PaxDb; Q8K1A5; -.
DR PeptideAtlas; Q8K1A5; -.
DR PRIDE; Q8K1A5; -.
DR ProteomicsDB; 260701; -. [Q8K1A5-1]
DR ProteomicsDB; 260702; -. [Q8K1A5-2]
DR ProteomicsDB; 260703; -. [Q8K1A5-3]
DR Antibodypedia; 11559; 15 antibodies from 10 providers.
DR DNASU; 233724; -.
DR Ensembl; ENSMUST00000094097; ENSMUSP00000091641; ENSMUSG00000047554. [Q8K1A5-1]
DR Ensembl; ENSMUST00000118429; ENSMUSP00000112574; ENSMUSG00000047554. [Q8K1A5-1]
DR Ensembl; ENSMUST00000119929; ENSMUSP00000113215; ENSMUSG00000047554. [Q8K1A5-2]
DR GeneID; 233724; -.
DR KEGG; mmu:233724; -.
DR UCSC; uc009jen.1; mouse. [Q8K1A5-1]
DR CTD; 440026; -.
DR MGI; MGI:1289225; Tmem41b.
DR VEuPathDB; HostDB:ENSMUSG00000047554; -.
DR eggNOG; KOG3140; Eukaryota.
DR GeneTree; ENSGT00940000156956; -.
DR HOGENOM; CLU_038944_0_1_1; -.
DR InParanoid; Q8K1A5; -.
DR OMA; CIKIPRD; -.
DR OrthoDB; 1222755at2759; -.
DR PhylomeDB; Q8K1A5; -.
DR TreeFam; TF314301; -.
DR BioGRID-ORCS; 233724; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Tmem41b; mouse.
DR PRO; PR:Q8K1A5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K1A5; protein.
DR Bgee; ENSMUSG00000047554; Expressed in morula and 228 other tissues.
DR ExpressionAtlas; Q8K1A5; baseline and differential.
DR Genevisible; Q8K1A5; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0032365; P:intracellular lipid transport; ISO:MGI.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; ISO:MGI.
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; Endoplasmic reticulum; Lipid transport;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291938"
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..43
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:0000250|UniProtKB:Q5BJD5"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026318"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026319"
FT CONFLICT 34
FT /note="G -> D (in Ref. 2; BAE38770/BAE38786)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="K -> Q (in Ref. 2; BAC41091)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="F -> L (in Ref. 2; BAC29048)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="H -> Y (in Ref. 2; BAE38770/BAE38786)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="S -> P (in Ref. 2; BAC41091)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="S -> N (in Ref. 2; BAE38770/BAE38786)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> I (in Ref. 2; BAE38770/BAE38786)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Q -> K (in Ref. 2; BAE38770/BAE38786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32429 MW; 337B420282D69149 CRC64;
MAKGRVADRS PTEMLHSTPA GDRAVRTQGS AAPGSKDHLN EKPCAEAGSA RTSLLILVSI
FSCAAFVMFL VYKNFPQLSE EERVNMKVPR DMDDAKALGK VLSKYKDTFY VQVLVAYFAT
YIFLQTFAIP GSIFLSILSG FLYPFPLALF LVCLCSGLGA SFCYMLSYLV GRPVVYKYLT
EKAVKWSQQV ERHREHLINY IIFLRITPFL PNWFINITSP VINVPLKVFF IGTFLGVAPP
SFVAIKAGTT LHQLTTAGEA VSWSSVFILM VLALLSILPA IFQKQLKQKF E
