TRAM1_RAT
ID TRAM1_RAT Reviewed; 374 AA.
AC Q5XI41;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translocating chain-associated membrane protein 1 {ECO:0000250|UniProtKB:Q15629};
DE Short=Protein TRAM1 {ECO:0000250|UniProtKB:Q15629};
GN Name=Tram1 {ECO:0000312|RGD:1359100};
GN Synonyms=Tram {ECO:0000250|UniProtKB:Q15629};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC083851; AAH83851.1; -; mRNA.
DR RefSeq; NP_001007702.1; NM_001007701.1.
DR AlphaFoldDB; Q5XI41; -.
DR STRING; 10116.ENSRNOP00000045166; -.
DR GlyGen; Q5XI41; 1 site.
DR iPTMnet; Q5XI41; -.
DR PhosphoSitePlus; Q5XI41; -.
DR jPOST; Q5XI41; -.
DR PaxDb; Q5XI41; -.
DR PRIDE; Q5XI41; -.
DR GeneID; 312903; -.
DR KEGG; rno:312903; -.
DR UCSC; RGD:1359100; rat.
DR CTD; 23471; -.
DR RGD; 1359100; Tram1.
DR VEuPathDB; HostDB:ENSRNOG00000007892; -.
DR eggNOG; KOG1608; Eukaryota.
DR HOGENOM; CLU_062830_0_0_1; -.
DR InParanoid; Q5XI41; -.
DR OMA; YFHHGIK; -.
DR OrthoDB; 831082at2759; -.
DR PRO; PR:Q5XI41; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007892; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q5XI41; baseline and differential.
DR Genevisible; Q5XI41; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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 1: Evidence at protein 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_0000240445"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..81
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..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 333..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:0007744|PubMed:22673903"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 374 AA; 43030 MW; 14889B19E79BDBA7 CRC64;
MAIRKKSNKN PPVLSHEFVL QNHADIVSCL AMLFLLGLMF EITAKGAIIF VALQYNVTRP
ATEEQAAESA SLYYYGIKDL ATVFFYMLVA IIVHAIIQEY VLDKINRRMH FSKTKHSKFN
ESGQLSAFYL FACVWGTFIL VSENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF
PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
FSDEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
LASICITQAF MMWKFINFQL RRWREHSAFQ APPVKRKPAV TKGRSSRKGT ENGVNGTVTS
NGADSPRSRK EKSS
