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Database: UniProt
Entry: A0A0C2GD85_9BILA
LinkDB: A0A0C2GD85_9BILA
Original site: A0A0C2GD85_9BILA 
ID   A0A0C2GD85_9BILA        Unreviewed;       265 AA.
AC   A0A0C2GD85;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=ANCDUO_12986 {ECO:0000313|EMBL:KIH56829.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH56829.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH56829.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH56829.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) 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; KN735215; KIH56829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2GD85; -.
DR   Proteomes; UP000054047; 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:UP000054047};
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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..265
FT                   /note="Translocon-associated protein subunit alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002149112"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          241..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  30035 MW;  E12771468843E9DD CRC64;
     MLSRRLLTAL LGTLVISAAF VYADDAVDGE VTEDQDVAKT EDDDLTVTSS SDAVVSFIFT
     QPADANTVKE LYGGKVVKFL IGFQNRGEKD FLIKHSETSF RYPMDFNYYL QNFTLGQYNR
     RVSPKEEVTL DYAFFAHESF AGRPLGLVVN LHYEDSEGHY ITNVFNETVT ILEDDSGFNT
     ETGFMYLVFA GLIVLLLLIG QHFLNKFTRK AGMQKKRQPV VEQGTNNSEV DFEWIPREIL
     KQNEKKSPKP GSPRNNNNLK TKKTN
//
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