ID K7ATD7_PANTR Unreviewed; 286 AA.
AC K7ATD7; A0A2J8MTT4; H2QS94;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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|EMBL:JAA21206.1,
GN ECO:0000313|Ensembl:ENSPTRP00000030217.5,
GN ECO:0000313|VGNC:VGNC:12704};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA21206.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030217.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA21206.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA05253.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA41591.1}, Skin {ECO:0000313|EMBL:JAA32582.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA21206.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000030217.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AACZ04065940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04065941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01006085; JAA05253.1; -; mRNA.
DR EMBL; GABC01006084; JAA05254.1; -; mRNA.
DR EMBL; GABF01000940; JAA21205.1; -; mRNA.
DR EMBL; GABF01000939; JAA21206.1; -; mRNA.
DR EMBL; GABD01000518; JAA32582.1; -; mRNA.
DR EMBL; GABE01003148; JAA41591.1; -; mRNA.
DR RefSeq; XP_003311142.1; XM_003311094.4.
DR Ensembl; ENSPTRT00000032707.5; ENSPTRP00000030217.5; ENSPTRG00000017698.6.
DR GeneID; 100614603; -.
DR KEGG; ptr:100614603; -.
DR CTD; 6745; -.
DR VGNC; VGNC:12704; SSR1.
DR eggNOG; KOG1631; Eukaryota.
DR GeneTree; ENSGT00400000022103; -.
DR OMA; FNFHIQN; -.
DR OrthoDB; 5403315at2759; -.
DR TreeFam; TF321074; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017698; Expressed in fibroblast and 21 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 2: Evidence at transcript level;
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 Receptor {ECO:0000313|EMBL:JAA21206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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..286
FT /note="Translocon-associated protein subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015095803"
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 261..286
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"
SQ SEQUENCE 286 AA; 32209 MW; 2C63193C1C3EBEBA 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 LNQINKASPR RLPRKRAQKR SVGSDE
//
