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Database: UniProt
Entry: A0A0N4VMV5_ENTVE
LinkDB: A0A0N4VMV5_ENTVE
Original site: A0A0N4VMV5_ENTVE 
ID   A0A0N4VMV5_ENTVE        Unreviewed;       275 AA.
AC   A0A0N4VMV5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=EVEC_LOCUS11501 {ECO:0000313|EMBL:VDD96750.1};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001228701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0001228701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDD96750.1, ECO:0000313|Proteomes:UP000274131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (OCT-2018) 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; UXUI01012182; VDD96750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4VMV5; -.
DR   STRING; 51028.A0A0N4VMV5; -.
DR   WBParaSite; EVEC_0001228701-mRNA-1; EVEC_0001228701-mRNA-1; EVEC_0001228701.
DR   Proteomes; UP000038041; Unplaced.
DR   Proteomes; UP000274131; 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:UP000274131};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..275
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033232449"
FT   TRANSMEM        195..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  31241 MW;  A4CC7EB8C7C8D661 CRC64;
     MLSSRLLLTL ITIGLVLPFA QIVRAADEAD GEVEDEKEDT EDSQPAAVDE KAAEEETVPV
     IGPSPDAHVF FLFTQPENSK DLPGGKLVRF LAGFQNWGEK DFIVNYCETS FRYPQDYSYY
     VQNFTALHYN RLVAPKQEGS FDYAFFPPEQ FMGRPLGLVV ELHYEDSDGT KFISTLFNET
     LTIVEDDSNF NTETGFLYVL LAAAVVLVLF AGQQFLSKLT RRHGMTKSRQ NPPIEMGTKN
     EDVDYEWIPR TVMNHKNTRS PKQGSPKHRK PRNEN
//
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