ID   TM41B_RAT               Reviewed;         291 AA.
AC   Q5FVN2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Transmembrane protein 41B {ECO:0000305};
GN   Name=Tmem41b {ECO:0000312|RGD:1310870};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
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: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; BC089866; AAH89866.1; -; mRNA.
DR   RefSeq; NP_001012358.1; NM_001012358.1.
DR   AlphaFoldDB; Q5FVN2; -.
DR   STRING; 10116.ENSRNOP00000016224; -.
DR   PaxDb; Q5FVN2; -.
DR   Ensembl; ENSRNOT00000016224; ENSRNOP00000016224; ENSRNOG00000010752.
DR   GeneID; 361626; -.
DR   KEGG; rno:361626; -.
DR   UCSC; RGD:1310870; rat.
DR   CTD; 440026; -.
DR   RGD; 1310870; Tmem41b.
DR   eggNOG; KOG3140; Eukaryota.
DR   GeneTree; ENSGT00940000156956; -.
DR   HOGENOM; CLU_038944_0_1_1; -.
DR   InParanoid; Q5FVN2; -.
DR   OMA; CIKIPRD; -.
DR   OrthoDB; 1222755at2759; -.
DR   PhylomeDB; Q5FVN2; -.
DR   TreeFam; TF314301; -.
DR   PRO; PR:Q5FVN2; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000010752; Expressed in duodenum and 19 other tissues.
DR   Genevisible; Q5FVN2; RN.
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:0032365; P:intracellular lipid transport; ISO:RGD.
DR   GO; GO:0044830; P:modulation by host of viral RNA genome replication; ISO:RGD.
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   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..291
FT                   /note="Transmembrane protein 41B"
FT                   /id="PRO_0000291940"
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..38
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"
SQ   SEQUENCE   291 AA;  32511 MW;  595F9E5F5E4A4C84 CRC64;
     MAKGRVAERS QTEMLHSTPA GDRAVGTQGS AAPGNKDHLK EKPCVEAGSA RTSLLILVSI
     FSCAAFVMFL VYKNFPQLSE EERVNMKVPR DMDDAKALGK VLSKYKDTFY VQVLVAYFAT
     YIFLQTFAIP GSIFLSILSG FLYPFPLALF LVCLCSGLGA SFCYMLSYLV GRPVVYKYLT
     EKAVKWSQQV ERHREHLINY IIFLRITPFL PNWFINITSP VINVPLKVFF IGTFLGVAPP
     SFVAIKAGTT LYQLTTAGEA VSWNSVFILM ILALLSILPA IFQKKLKQKF E