ID G7MQI4_MACMU Unreviewed; 298 AA.
AC G7MQI4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
GN ORFNames=EGK_14445 {ECO:0000313|EMBL:EHH17932.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH17932.1};
RN [1] {ECO:0000313|EMBL:EHH17932.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH17932.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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. 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, 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|ARBA:ARBA00006776, ECO:0000256|RuleBase:RU368074}.
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DR EMBL; CM001256; EHH17932.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MQI4; -.
DR Proteomes; UP000013456; Chromosome 4.
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 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..298
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003500115"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368074"
FT REGION 33..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 33760 MW; 89BA4F666B1A76A2 CRC64;
MRLLPRLLLL LLLVFPATVL FRGGPRGSLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK
VEMGTSSQND VDMSWIPQET LNQIISFLPD KASPRRLPRK RAQKRSVGSD ERRRRETH
//
