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Database: UniProt
Entry: A0A0M9A8J6_9HYME
LinkDB: A0A0M9A8J6_9HYME
Original site: A0A0M9A8J6_9HYME 
ID   A0A0M9A8J6_9HYME        Unreviewed;       234 AA.
AC   A0A0M9A8J6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN   ORFNames=WN51_02682 {ECO:0000313|EMBL:KOX79417.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX79417.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX79417.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX79417.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX79417.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) 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}.
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DR   EMBL; KQ435711; KOX79417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9A8J6; -.
DR   STRING; 166423.A0A0M9A8J6; -.
DR   OrthoDB; 2882163at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
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; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR   PANTHER; PTHR12701:SF18; ENDOPLASMIC RETICULUM TRANSMEMBRANE PROTEIN; 1.
DR   Pfam; PF05529; Bap31; 1.
DR   Pfam; PF18035; Bap31_Bap29_C; 1.
PE   3: Inferred from homology;
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:KOX79417.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        48..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   DOMAIN          1..133
FT                   /note="BAP29/BAP31 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF05529"
FT   DOMAIN          185..234
FT                   /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF18035"
FT   COILED          165..220
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   234 AA;  27116 MW;  F78953B06ECC710A CRC64;
     MSLQWTLIAG FLYFEIVVVL LLVLPIISPT RWQKLFRSQF LKSLIYKASI YFVFLLGILV
     LFLLDSIREM RKYSTVHETK ELYLNTEMQG SMRLFRAQRN FYISGFALFL SLVIRRLVIL
     ISGQATLLAK SEAVMRQAES ATTTAKRLLL QQKINTKETA ENDTNEAHDK VLSEWKNQIK
     ELQTKNEELE NQLAKEKEDK GAIKSQAESL AKEYDRLNDE HSKCLQSVND KKSD
//
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