TM41B_XENLA
ID TM41B_XENLA Reviewed; 278 AA.
AC Q5U4K5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Transmembrane protein 41B {ECO:0000305};
GN Name=tmem41b {ECO:0000250|UniProtKB:Q5BJD5};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SIMILARITY: Belongs to the TMEM41 family. {ECO:0000305}.
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DR EMBL; BC085059; AAH85059.1; -; mRNA.
DR RefSeq; NP_001088592.1; NM_001095123.2.
DR AlphaFoldDB; Q5U4K5; -.
DR DNASU; 495477; -.
DR GeneID; 495477; -.
DR KEGG; xla:495477; -.
DR CTD; 495477; -.
DR Xenbase; XB-GENE-17334906; tmem41b.L.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495477; Expressed in oocyte and 19 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: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 2: Evidence at transcript level;
KW Autophagy; Endoplasmic reticulum; Lipid transport; Membrane; Neurogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..278
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291943"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..238
FT /note="VTT domain; required for its function in autophagy"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 31212 MW; D958B82A198C326E CRC64;
MQVHERSHTG GHTFQCNHGN EKKAPAAGKV HSEGGSARMS LLILVSIFLC AASVMFLVYK
YFPQLSEEEL EKIKVPRDMD DAKALGKVLS KYKDTFYVEV LVAYFTTYIF LQTFAIPGSI
FLSILSGFLY PFPLALFLVC LCSGLGASFC YLLSYLVGRP VVYKYLSDKA IKWSQQVERH
RDHLINYIIF LRITPFLPNW FINITSPVIN VPLKVFFLGT FIGVAPPSFV AIKAGTTLYQ
LTTAGEAVSW NSVIILMVLA VLSILPAIFQ KKLKQKFE
