ID A0A0L7QNT4_9HYME Unreviewed; 275 AA.
AC A0A0L7QNT4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|ARBA:ARBA00020280};
DE AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|ARBA:ARBA00031071};
GN ORFNames=WH47_08674 {ECO:0000313|EMBL:KOC60302.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC60302.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC60302.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC60302.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC calcium to the ER membrane and thereby regulate the retention of ER
CC resident proteins. May be involved in the recycling of the
CC translocation apparatus after completion of the translocation process
CC or may function as a membrane-bound chaperone facilitating folding of
CC translocated proteins. {ECO:0000256|ARBA:ARBA00025620}.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma. Interacts with palmitoylated calnexin (CALX), the interaction is
CC required for efficient folding of glycosylated proteins.
CC {ECO:0000256|ARBA:ARBA00025854}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family.
CC {ECO:0000256|ARBA:ARBA00006776}.
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DR EMBL; KQ414843; KOC60302.1; -; Genomic_DNA.
DR RefSeq; XP_017795442.1; XM_017939953.1.
DR AlphaFoldDB; A0A0L7QNT4; -.
DR STRING; 597456.A0A0L7QNT4; -.
DR EnsemblMetazoa; XM_017939953.1; XP_017795442.1; LOC108576890.
DR GeneID; 108576890; -.
DR OrthoDB; 5403315at2759; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR005595; TRAP_alpha.
DR PANTHER; PTHR12924:SF0; TRANSLOCON-ASSOCIATED PROTEIN SUBUNIT ALPHA; 1.
DR PANTHER; PTHR12924; TRANSLOCON-ASSOCIATED PROTEIN, ALPHA SUBUNIT; 1.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..275
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005574765"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 218..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30759 MW; 85612FE46D42DB81 CRC64;
MKKFSILLLL FVSTITFTMN RAYAQEDENI DDIVDIEGED NSIITDEEPE DETTNASSDA
DTTILFTKPV YNGLSTLELP AGNLVELLVG FTNKGESDFV LESLDASFRY AMDFNFYIQN
FSTVTYNKIV KSKHEATLAY SFIPSENFAG RPFGFNINLN YKDANGVGFS EAVYNETVQI
IELDDGLDGE TIFLYVFLAA CVILTLVGGQ QLLSSLGRKS RSSNTRKAPV EMGTANPNNV
DYDWLPKETL NRINKSPKTP RQSPRQRKVK KTSDD
//