ID G3N5I3_GASAC Unreviewed; 286 AA.
AC G3N5I3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|ARBA:ARBA00020280, ECO:0000256|RuleBase:RU368074};
DE Short=TRAP-alpha {ECO:0000256|RuleBase:RU368074};
DE AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|ARBA:ARBA00031071, ECO:0000256|RuleBase:RU368074};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000556.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000000556.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000000556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 ECO:0000256|RuleBase:RU368074}.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma. {ECO:0000256|RuleBase:RU368074}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU368074}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115,
CC ECO:0000256|RuleBase:RU368074}.
CC -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC being highly negatively charged, and the cytoplasmic C-terminus
CC positively charged. {ECO:0000256|RuleBase:RU368074}.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family.
CC {ECO:0000256|ARBA:ARBA00006776, ECO:0000256|RuleBase:RU368074}.
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DR AlphaFoldDB; G3N5I3; -.
DR Ensembl; ENSGACT00000000556.1; ENSGACP00000000556.1; ENSGACG00000000425.1.
DR GeneTree; ENSGT00400000022103; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000000425; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR005595; TRAP_alpha.
DR PANTHER; PTHR12924:SF1; SIGNAL SEQUENCE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR12924; TRANSLOCON-ASSOCIATED PROTEIN, ALPHA SUBUNIT; 1.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU368074};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368074};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368074};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Signal {ECO:0000256|RuleBase:RU368074, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368074};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368074}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..286
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003448155"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368074"
FT REGION 27..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 31974 MW; 26E0ADE3C673E2FC CRC64;
MFNFGPNVLL LLLVAFPCGL VSFGQVSADS DSDEDIADDP EAAVDEEEDE EEMLVEEDQM
QPSDRDEEDS DEAADKLLSS HPEADTTIIF MTGEEFPANE IVRFLVGFTN KGSQDFTVQS
LEASFRYPQD YQFYIQNFTA LPLSTVVQPQ AQASFEYSFI PAQPMAGRPF GLVILLNYLD
TEGNVFQTAI YNQTVNIIEL EEGLDGETMF LYIFLAGLVS LMLFGIYQVL ETRTKKRIPV
KIERGTGGMN DVDISWIPQE NLNIMNKASP KASPRKRTKR AAGTDQ
//