TM41B_DANRE
ID TM41B_DANRE Reviewed; 282 AA.
AC A1A5V7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Transmembrane protein 41B {ECO:0000305};
DE AltName: Full=Protein stasimon {ECO:0000303|PubMed:23063131};
GN Name=tmem41b {ECO:0000250|UniProtKB:Q5BJD5};
GN ORFNames=zgc:158275 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
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 (PubMed:23063131). {ECO:0000250|UniProtKB:Q5BJD5,
CC ECO:0000269|PubMed:23063131}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5BJD5}; 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:0000250|UniProtKB:Q5BJD5}.
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: Morpholino knockdown of the protein causes severe
CC defects in motor neuron axonal outgrowth.
CC {ECO:0000269|PubMed:23063131}.
CC -!- SIMILARITY: Belongs to the TMEM41 family. {ECO:0000305}.
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DR EMBL; BC128830; AAI28831.1; -; mRNA.
DR RefSeq; NP_001073456.1; NM_001079987.1.
DR RefSeq; XP_009301841.1; XM_009303566.2.
DR AlphaFoldDB; A1A5V7; -.
DR STRING; 7955.ENSDARP00000102085; -.
DR PaxDb; A1A5V7; -.
DR Ensembl; ENSDART00000098277; ENSDARP00000089049; ENSDARG00000080006.
DR Ensembl; ENSDART00000110614; ENSDARP00000102085; ENSDARG00000080006.
DR Ensembl; ENSDART00000171493; ENSDARP00000134440; ENSDARG00000080006.
DR GeneID; 561208; -.
DR KEGG; dre:561208; -.
DR CTD; 440026; -.
DR ZFIN; ZDB-GENE-061215-138; tmem41b.
DR eggNOG; KOG3140; Eukaryota.
DR GeneTree; ENSGT00940000156956; -.
DR InParanoid; A1A5V7; -.
DR OMA; CIKIPRD; -.
DR OrthoDB; 1222755at2759; -.
DR PhylomeDB; A1A5V7; -.
DR TreeFam; TF314301; -.
DR PRO; PR:A1A5V7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000080006; Expressed in early embryo and 24 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR InterPro; IPR032816; SNARE_assoc.
DR InterPro; IPR045014; TM41A/B.
DR PANTHER; PTHR43220; PTHR43220; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Endoplasmic reticulum; Lipid transport; Membrane; Neurogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..282
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291942"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..242
FT /note="VTT domain; required for its function in autophagy"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
SQ SEQUENCE 282 AA; 31494 MW; CBA3564517A323FB CRC64;
MAKKRAGNRE TESSPLVEQE PRPSKETPVP KGAQSPGGAS ARMSILLLVV IFACSACVMY
LVFRNFPQLS EDEREKIKIP KDMEDAKALG TVLSKYKDTY YTQVLLAYFA TYIFLQTFAI
PGSIFLSILS GYLYPFPLAL FLVCLCSGLG ASFCYMLSYL VGRPMVYKYL TERAQKWSQQ
VDKHREHLIN YIIFLRITPF LPNWFINITS PVINVPLGVF FLGTFLGVAP PSFVAINAGT
TLYKLTTAGE AVSWNSLLVL GVLAVVSILP VCFQKKLQQK LE
