ID G5E7N7_MELGA Unreviewed; 301 AA.
AC G5E7N7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 49.
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 Name=SSR1 {ECO:0000313|Ensembl:ENSMGAP00000019074.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000019074.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000019074.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000019074.2}
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. 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 RefSeq; XP_010706686.1; XM_010708384.2.
DR AlphaFoldDB; G5E7N7; -.
DR Ensembl; ENSMGAT00000020232.2; ENSMGAP00000019074.2; ENSMGAG00000003888.3.
DR GeneID; 100540889; -.
DR CTD; 6745; -.
DR GeneTree; ENSGT00400000022103; -.
DR InParanoid; G5E7N7; -.
DR TreeFam; TF321074; -.
DR Proteomes; UP000001645; Chromosome 3.
DR Bgee; ENSMGAG00000003888; Expressed in pancreas and 17 other cell types or tissues.
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:UP000001645};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..301
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032763244"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368074"
FT REGION 36..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 33711 MW; 96256280E1866328 CRC64;
MRSAPRLLLL ALLVFPATLL LRDSGAVGSG LLAAAQDATE DEEAVEDTVV EDEDDEAEVE
EDEPTDLTEE KEEEDLSGEP KASPSADTTI LFVKGEDFPA NNIVKFLVGF TNKGTEDFIV
ESLDASFRYP QDYQFYIQNF TALPLNTVVP PQRQATFEYS FIPAEPMGGR PFGLVINLNY
RDANGNMFQD AVFNQTVTII EKEDGLDGET IFMYMFLAGL GLLVIVGLHQ LLESRKRKRP
VQKVEMGTSN QNDVDMSWIP QETLNQIMQS RRDKASPRRL PRKRAQKRSV GSDEKTHPTR
S
//