TRAM1_PONAB
ID TRAM1_PONAB Reviewed; 374 AA.
AC Q5R7Z3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Translocating chain-associated membrane protein 1 {ECO:0000250|UniProtKB:Q15629};
DE Short=Protein TRAM1 {ECO:0000250|UniProtKB:Q15629};
GN Name=TRAM1; Synonyms=TRAM {ECO:0000250|UniProtKB:Q15629};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the translocation of nascent protein chains into
CC or through the endoplasmic reticulum (ER) membrane by facilitating the
CC proper chain positioning at the SEC61 channel. Regulates the exposure
CC of nascent secretory protein chain to the cytosol during translocation
CC into the ER. May affect the phospholipid bilayer in the vicinity of the
CC lateral gate of the SEC61 channel, thereby facilitating ER protein
CC transport. Intimately associates with transmembrane (TM) domain of
CC nascent membrane proteins during the entire integration process into
CC the ER membrane. Associates with the second TM domain of G-protein-
CC coupled receptor opsin/OPSD nascent chain in the ER membrane, which may
CC facilitate its integration into the membrane. Under conditions of ER
CC stress, participates in the disposal of misfolded ER membrane proteins
CC during the unfolded protein response (UPR), an integrated stress
CC response (ISR) pathway, by selectively retrotranslocating misfolded ER-
CC membrane proteins from the ER into the cytosol where they are
CC ubiquitinated and degraded by the proteasome.
CC {ECO:0000250|UniProtKB:Q15629}.
CC -!- SUBUNIT: Interacts with SEC61B. May interact with Derlin-1/DERL1.
CC {ECO:0000250|UniProtKB:Q15629}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15629}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q15629}.
CC -!- SIMILARITY: Belongs to the TRAM family. {ECO:0000305}.
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DR EMBL; CR859964; CAH92117.1; -; mRNA.
DR RefSeq; NP_001126237.1; NM_001132765.1.
DR AlphaFoldDB; Q5R7Z3; -.
DR STRING; 9601.ENSPPYP00000020934; -.
DR GeneID; 100173207; -.
DR KEGG; pon:100173207; -.
DR CTD; 23471; -.
DR eggNOG; KOG1608; Eukaryota.
DR InParanoid; Q5R7Z3; -.
DR OrthoDB; 831082at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:InterPro.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR InterPro; IPR016447; Translocation_assoc_membrane.
DR PANTHER; PTHR12371; PTHR12371; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005449; Translocation_assoc_membrane; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..374
FT /note="Translocating chain-associated membrane protein 1"
FT /id="PRO_0000240444"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..76
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..297
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT DOMAIN 117..326
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 334..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15629"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 374 AA; 43054 MW; 298E410940733DB3 CRC64;
MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP
ATEEQATESA SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY MLDKINRRMH FSKTKHSKFN
ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF
PELYFQKTKR EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
FSNEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
LASICITQAF MVWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT ENGVNGTLTS
NVADSPRNKK EKSS
