ID A0A0B0PG13_GOSAR Unreviewed; 216 AA.
AC A0A0B0PG13;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Translocon-associated protein subunit alpha {ECO:0000256|RuleBase:RU368074};
DE Short=TRAP-alpha {ECO:0000256|RuleBase:RU368074};
DE AltName: Full=Signal sequence receptor subunit alpha {ECO:0000256|RuleBase:RU368074};
GN ORFNames=F383_08870 {ECO:0000313|EMBL:KHG23862.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG23862.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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|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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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|RuleBase:RU368074}.
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DR EMBL; KN426578; KHG23862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0PG13; -.
DR Proteomes; UP000032142; 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 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:UP000032142};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368074};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..216
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002078578"
FT TRANSMEM 150..168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368074"
SQ SEQUENCE 216 AA; 23513 MW; 4EB2BBDA492B5AD5 CRC64;
MAMKNFSVFF FALLFLASPF LQVARCQSEA EADVAEAVEG GDLGIVGEDV QDFGESPVNV
IAIKASVHLP FDHRMLVQNL TAAAFNNATV PPSVQATFPY VFAVSKFLQP GTFDLVGSII
YDIDQQPYQS TFYNGTIEVV EAGGFLSVES VFLVTLGIAL LVLLGLWLHG QFQRITKKTK
RAPKVEVGTR APDASLDEWL QGTAYTQSAS KSKKKK
//