TM41B_PONAB
ID TM41B_PONAB Reviewed; 291 AA.
AC Q5RBZ8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Transmembrane protein 41B {ECO:0000305};
GN Name=TMEM41B {ECO:0000250|UniProtKB:Q5BJD5};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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 -!- 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; CR858484; CAH90712.1; -; mRNA.
DR RefSeq; NP_001125395.1; NM_001131923.1.
DR AlphaFoldDB; Q5RBZ8; -.
DR STRING; 9601.ENSPPYP00000022362; -.
DR GeneID; 100172300; -.
DR KEGG; pon:100172300; -.
DR CTD; 440026; -.
DR eggNOG; KOG3140; Eukaryota.
DR InParanoid; Q5RBZ8; -.
DR OrthoDB; 1222755at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..291
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291939"
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"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
SQ SEQUENCE 291 AA; 32449 MW; 28F618BFAFC095BE CRC64;
MAKGRVAERS QMGADHTTPV GDGAAGTRGP AAPGSRDYQK EKSWAEAGSA RMSLLILVSI
FLSAAFVMFL VYKNFPQLSE EERVNMKVPR DMDDAKALGK VLSKYKDTFY VQVLVAYFAT
YIFLQTFAIP GSIFLSILSG FLYPFPLALF LVCLCSGLGA SFCYMLSYLV GRPVVYKYLT
EKAVKWSQQV ERHREHLINY IIFLRITPFL PNWFINITSP VINVPLKVFF IGTFLGVAPP
SFVAIKAGTT LHQPTTAGEA VSWNSIFILM ILAVLSILPA IFQKKLKQKF E
