GenomeNet

Database: UniProt
Entry: TM41B_XENTR
LinkDB: TM41B_XENTR
Original site: TM41B_XENTR 
ID   TM41B_XENTR             Reviewed;         278 AA.
AC   A4II98;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Transmembrane protein 41B {ECO:0000305};
GN   Name=tmem41b {ECO:0000250|UniProtKB:Q5BJD5};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC135922; AAI35923.1; -; mRNA.
DR   AlphaFoldDB; A4II98; -.
DR   STRING; 8364.ENSXETP00000020961; -.
DR   InParanoid; A4II98; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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; IPR045014; TM41A/B.
DR   InterPro; IPR032816; VTT_dom.
DR   PANTHER; PTHR43220; -; 1.
DR   PANTHER; PTHR43220:SF18; TRANSMEMBRANE PROTEIN 41B; 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_0000291944"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..154
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;  31186 MW;  B1360152F757D333 CRC64;
     MQVHERSHTG GHTCQCNHGS EKKAPATGKV HSEGGSARMS LLILVSIFLC AASIMFLVYK
     HFPQLSEEER EKIKVPRDMD DAKALGKVLS KYKDTFYVEV LVAYFTTYIF LQTFAIPGSI
     FLSILSGFLY PFPLALFLVC LCSGLGASFS YLLSYLVGRP VVYKYLSDKA IKWSQQVERH
     RDHLINYIIF LRITPFLPNW FINITSPVIN VPLKVFFLGT FIGVAPPSFV AIKAGTTLYQ
     LTTAGEAVSW NSVIILMVLA VLSILPAIFQ KKLKKKFE
//
DBGET integrated database retrieval system