TRAM1_MOUSE
ID TRAM1_MOUSE Reviewed; 374 AA.
AC Q91V04;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
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|MGI:MGI:1919515};
GN Synonyms=Tram {ECO:0000250|UniProtKB:Q15629};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hartmann E.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-56, AND MUTAGENESIS OF
RP ASN-56; ASN-120 AND ASN-355.
RX PubMed=21237175; DOI=10.1016/j.jmb.2011.01.009;
RA Tamborero S., Vilar M., Martinez-Gil L., Johnson A.E., Mingarro I.;
RT "Membrane insertion and topology of the translocating chain-associating
RT membrane protein (TRAM).";
RL J. Mol. Biol. 406:571-582(2011).
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:0000269|PubMed:21237175}; 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; AY029764; AAK38167.1; -; mRNA.
DR EMBL; AK088814; BAC40590.1; -; mRNA.
DR EMBL; BC012401; AAH12401.1; -; mRNA.
DR CCDS; CCDS14822.1; -.
DR RefSeq; NP_082449.1; NM_028173.5.
DR AlphaFoldDB; Q91V04; -.
DR BioGRID; 215264; 5.
DR STRING; 10090.ENSMUSP00000027068; -.
DR GlyGen; Q91V04; 1 site.
DR iPTMnet; Q91V04; -.
DR PhosphoSitePlus; Q91V04; -.
DR EPD; Q91V04; -.
DR jPOST; Q91V04; -.
DR MaxQB; Q91V04; -.
DR PaxDb; Q91V04; -.
DR PRIDE; Q91V04; -.
DR ProteomicsDB; 298208; -.
DR Antibodypedia; 12213; 152 antibodies from 28 providers.
DR DNASU; 72265; -.
DR Ensembl; ENSMUST00000027068; ENSMUSP00000027068; ENSMUSG00000025935.
DR GeneID; 72265; -.
DR KEGG; mmu:72265; -.
DR UCSC; uc007ait.2; mouse.
DR CTD; 23471; -.
DR MGI; MGI:1919515; Tram1.
DR VEuPathDB; HostDB:ENSMUSG00000025935; -.
DR eggNOG; KOG1608; Eukaryota.
DR GeneTree; ENSGT00510000046470; -.
DR HOGENOM; CLU_062830_0_0_1; -.
DR InParanoid; Q91V04; -.
DR OMA; YFHHGIK; -.
DR OrthoDB; 831082at2759; -.
DR PhylomeDB; Q91V04; -.
DR TreeFam; TF314319; -.
DR BioGRID-ORCS; 72265; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tram1; mouse.
DR PRO; PR:Q91V04; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91V04; protein.
DR Bgee; ENSMUSG00000025935; Expressed in parotid gland and 254 other tissues.
DR ExpressionAtlas; Q91V04; baseline and differential.
DR Genevisible; Q91V04; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA: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_0000185531"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..76
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..217
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..297
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:21237175"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21237175"
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:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21237175"
FT MUTAGEN 56
FT /note="N->Q: Abolishes glycosylation."
FT /evidence="ECO:0000269|PubMed:21237175"
FT MUTAGEN 120
FT /note="N->Q: No effect on glycosylation; when associated
FT with Q-355."
FT /evidence="ECO:0000269|PubMed:21237175"
FT MUTAGEN 355
FT /note="N->Q: No effect on glycosylation; when associated
FT with Q-120."
FT /evidence="ECO:0000269|PubMed:21237175"
SQ SEQUENCE 374 AA; 43039 MW; E6C65250F68E4393 CRC64;
MAIRKKSNKN PPLLSHEFLL QNHADIVSCL AMLFLLGLMF EVTAKGAIIF VALQYNVTRP
ATEEQATESA SLYHYGIKDL ATVLFYMLVA IIIHAIIQEY VLDKINRRMH FSKTKHSKFN
ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQTKFFYI SQLAYWLHAF
PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
FSDEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
LASICITQAF MMWKFINFQL RRWREHSAFQ APPVKRKPAV TKGRSSRKGT ENGVNGTVTS
NGADSPRNRK EKSS
