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Database: UniProt
Entry: A0A183I4G9_9BILA
LinkDB: A0A183I4G9_9BILA
Original site: A0A183I4G9_9BILA 
ID   A0A183I4G9_9BILA        Unreviewed;       210 AA.
AC   A0A183I4G9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=OFLC_LOCUS14631 {ECO:0000313|EMBL:VDP17958.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0001464201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0001464201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP17958.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-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; UZAJ01041020; VDP17958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183I4G9; -.
DR   STRING; 387005.A0A183I4G9; -.
DR   WBParaSite; OFLC_0001464201-mRNA-1; OFLC_0001464201-mRNA-1; OFLC_0001464201.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; 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   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        136..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   210 AA;  24167 MW;  FE740CFDDEB9E2EA CRC64;
     MMRPSPDVHV AFIFIQPENP EGLPGGKLVQ FLMGFQNRGE KDFTVHFCET SFRYPQDFSY
     HIQNFSRVHY NRVVAAKQEA TFNYAFYPSD QFAGRPLGLV VELQYQDNDG NAYKNTVFNE
     TITIVEDESN FNTETGFLYV IFAAVVVLIL LAGQHFLSKL TRKHGMSKNR QTQPIEIGTS
     NKNEVDFEWI PREVLNHNKS PKPGSPRQRK
//
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