TRAM1_CANLF
ID TRAM1_CANLF Reviewed; 374 AA.
AC Q01685;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
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:0000303|PubMed:1315422};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-27 AND 165-185, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=1315422; DOI=10.1038/357047a0;
RA Goerlich D., Hartmann E., Prehn S., Rapoport T.A.;
RT "A protein of the endoplasmic reticulum involved early in polypeptide
RT translocation.";
RL Nature 357:47-52(1992).
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 (PubMed:1315422).
CC Regulates the exposure of nascent secretory protein chain to the
CC cytosol during translocation into the ER. May affect the phospholipid
CC bilayer in the vicinity of the lateral gate of the SEC61 channel,
CC thereby facilitating ER protein transport. Intimately associates with
CC transmembrane (TM) domain of nascent membrane proteins during the
CC entire integration process into the ER membrane. Associates with the
CC second TM domain of G-protein-coupled receptor opsin/OPSD nascent chain
CC in the ER membrane, which may facilitate its integration into the
CC membrane. Under conditions of ER stress, participates in the disposal
CC of misfolded ER membrane proteins during the unfolded protein response
CC (UPR), an integrated stress response (ISR) pathway, by selectively
CC retrotranslocating misfolded ER-membrane proteins from the ER into the
CC cytosol where they are ubiquitinated and degraded by the proteasome (By
CC similarity). {ECO:0000250|UniProtKB:Q15629,
CC ECO:0000269|PubMed:1315422}.
CC -!- SUBUNIT: Interacts with SEC61B. May interact with Derlin-1/DERL1.
CC {ECO:0000250|UniProtKB:Q15629}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:1315422}; 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; X63678; CAA45217.1; -; mRNA.
DR PIR; S21736; S21736.
DR RefSeq; NP_001003267.1; NM_001003267.1.
DR AlphaFoldDB; Q01685; -.
DR STRING; 9615.ENSCAFP00000052565; -.
DR PaxDb; Q01685; -.
DR Ensembl; ENSCAFT00000082516; ENSCAFP00000052565; ENSCAFG00000007866.
DR Ensembl; ENSCAFT00030016091; ENSCAFP00030014043; ENSCAFG00030008666.
DR Ensembl; ENSCAFT00845046178; ENSCAFP00845036259; ENSCAFG00845026170.
DR GeneID; 403948; -.
DR KEGG; cfa:403948; -.
DR CTD; 23471; -.
DR VEuPathDB; HostDB:ENSCAFG00845026170; -.
DR VGNC; VGNC:54123; TRAM1.
DR eggNOG; KOG1608; Eukaryota.
DR GeneTree; ENSGT00510000046470; -.
DR InParanoid; Q01685; -.
DR OrthoDB; 831082at2759; -.
DR Proteomes; UP000002254; Chromosome 29.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum 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; IDA:WormBase.
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 Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1315422"
FT CHAIN 2..374
FT /note="Translocating chain-associated membrane protein 1"
FT /id="PRO_0000185529"
FT TOPO_DOM 2..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..217
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..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; 43161 MW; 4D97B9B7D48D0593 CRC64;
MAIRKKSTKS PPVLSHEFIL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP
ATEEQATEST SLYYYGIKDL ATVFFYMLVA IIIHAIIQEY VLDKINRRMH FSKTKHSKFN
ESGQLSAFYL FSCIWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI AQLAYWFHAF
PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
FSDEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSAGN FNVLAVRIAV
LASICITQAF MMWKFINFQL RRWREHSTFQ APVVKKKPTV TKGRSSRKGT ENGVNGTVTS
NGADSPRNRK EKSS
