TM41B_CHICK
ID TM41B_CHICK Reviewed; 269 AA.
AC Q5ZIL6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Transmembrane protein 41B {ECO:0000305};
GN Name=TMEM41B {ECO:0000250|UniProtKB:Q5BJD5};
GN ORFNames=RCJMB04_25c20 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720768; CAG32427.1; -; mRNA.
DR RefSeq; NP_001008469.1; NM_001008469.1.
DR AlphaFoldDB; Q5ZIL6; -.
DR STRING; 9031.ENSGALP00000009322; -.
DR PaxDb; Q5ZIL6; -.
DR Ensembl; ENSGALT00000009336; ENSGALP00000009322; ENSGALG00000005815.
DR GeneID; 423047; -.
DR KEGG; gga:423047; -.
DR CTD; 440026; -.
DR VEuPathDB; HostDB:geneid_423047; -.
DR eggNOG; KOG3140; Eukaryota.
DR GeneTree; ENSGT00940000156956; -.
DR HOGENOM; CLU_038944_0_1_1; -.
DR InParanoid; Q5ZIL6; -.
DR OMA; CIKIPRD; -.
DR OrthoDB; 1222755at2759; -.
DR PhylomeDB; Q5ZIL6; -.
DR TreeFam; TF314301; -.
DR PRO; PR:Q5ZIL6; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000005815; Expressed in spermatocyte and 13 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..269
FT /note="Transmembrane protein 41B"
FT /id="PRO_0000291941"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 118..229
FT /note="VTT domain; required for its function in autophagy"
FT /evidence="ECO:0000250|UniProtKB:Q5BJD5"
SQ SEQUENCE 269 AA; 30269 MW; 3890DD99F3628E4F CRC64;
MAQRRAAAES ARHQRLLEGK AQAEGGSART SLLILVSIFT IAAFLMFLVY KNFPQLSEEE
GKCIKIPRDM DDAKALGKVL SKYKDTFYVQ VLVAYFATYV FLQTFAIPGS IFLSILSGFL
YPFPLALFLV CLCSGLGASF CYMLSYLVGR PVVYKYLTEK AVKWSEQVER HREHLINYII
FLRITPFLPN WFINITSPVI NVPLKVFFIG TFLGVAPPSF VAIKAGTTLY QLTTAGEAVS
WNSLFVLMIL AILSILPALF QKKLKQKFE
