ID G5DYF2_9PIPI Unreviewed; 134 AA.
AC G5DYF2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
DE Flags: Fragment;
OS Hymenochirus curtipes (western dwarf clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Pipinae; Hymenochirus.
OX NCBI_TaxID=8362 {ECO:0000313|EMBL:AEQ17498.1};
RN [1] {ECO:0000313|EMBL:AEQ17498.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:AEQ17498.1};
RA Chain F.J.J., Evans B.J., Dushoff J.;
RT "The odds of duplicate gene persistence after polyploidization.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC from the endoplasmic reticulum to the Golgi.
CC {ECO:0000256|RuleBase:RU367026}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367026}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
CC {ECO:0000256|ARBA:ARBA00007956, ECO:0000256|RuleBase:RU367026}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367026}.
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DR EMBL; JP286166; AEQ17498.1; -; mRNA.
DR AlphaFoldDB; G5DYF2; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.110; -; 1.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR InterPro; IPR041672; Bap31/Bap29_C.
DR PANTHER; PTHR12701:SF15; B-CELL RECEPTOR-ASSOCIATED PROTEIN 31; 1.
DR PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR Pfam; PF05529; Bap31; 1.
DR Pfam; PF18035; Bap31_Bap29_C; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367026};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU367026};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367026}; Receptor {ECO:0000313|EMBL:AEQ17498.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367026};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367026};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367026}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT DOMAIN 1..42
FT /note="BAP29/BAP31 transmembrane"
FT /evidence="ECO:0000259|Pfam:PF05529"
FT DOMAIN 79..134
FT /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF18035"
FT COILED 67..129
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEQ17498.1"
FT NON_TER 134
FT /evidence="ECO:0000313|EMBL:AEQ17498.1"
SQ SEQUENCE 134 AA; 15731 MW; 0245A53C1CBCE03D CRC64;
MSLQWTAVAT FLYAEVFLVL LLCIPFISPT RWQKIFKSRL VQLHIHMKLF RSQRNLYLGV
EVSDLPETNA EEENKKLKEE MRKIKEELES TKKNLHKSES EVLAIKKQCE GLTKEYDRLL
AEHSKLQAQM DGPK
//
