TR1L1_MOUSE
ID TR1L1_MOUSE Reviewed; 363 AA.
AC Q8QZR0; Q8C455; Q8C6X6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Translocating chain-associated membrane protein 1-like 1;
GN Name=Tram1l1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Stimulatory or required for the translocation of secretory
CC proteins across the ER membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAM family. {ECO:0000305}.
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DR EMBL; AK044115; BAC31785.1; -; mRNA.
DR EMBL; AK052946; BAC35215.2; -; mRNA.
DR EMBL; AK083053; BAC38746.1; -; mRNA.
DR EMBL; BC024829; AAH24829.1; -; mRNA.
DR EMBL; BC027120; AAH27120.1; -; mRNA.
DR CCDS; CCDS17819.1; -.
DR RefSeq; NP_666252.1; NM_146140.3.
DR AlphaFoldDB; Q8QZR0; -.
DR STRING; 10090.ENSMUSP00000062635; -.
DR iPTMnet; Q8QZR0; -.
DR PhosphoSitePlus; Q8QZR0; -.
DR MaxQB; Q8QZR0; -.
DR PaxDb; Q8QZR0; -.
DR PeptideAtlas; Q8QZR0; -.
DR PRIDE; Q8QZR0; -.
DR ProteomicsDB; 258837; -.
DR Antibodypedia; 26589; 80 antibodies from 16 providers.
DR DNASU; 229801; -.
DR Ensembl; ENSMUST00000058994; ENSMUSP00000062635; ENSMUSG00000044528.
DR GeneID; 229801; -.
DR KEGG; mmu:229801; -.
DR UCSC; uc008rfr.1; mouse.
DR CTD; 133022; -.
DR MGI; MGI:2443503; Tram1l1.
DR VEuPathDB; HostDB:ENSMUSG00000044528; -.
DR eggNOG; KOG1608; Eukaryota.
DR GeneTree; ENSGT00510000046470; -.
DR HOGENOM; CLU_062830_0_0_1; -.
DR InParanoid; Q8QZR0; -.
DR OMA; SENCLAD; -.
DR OrthoDB; 831082at2759; -.
DR PhylomeDB; Q8QZR0; -.
DR TreeFam; TF314319; -.
DR BioGRID-ORCS; 229801; 1 hit in 58 CRISPR screens.
DR PRO; PR:Q8QZR0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8QZR0; protein.
DR Bgee; ENSMUSG00000044528; Expressed in dorsal pancreas and 167 other tissues.
DR Genevisible; Q8QZR0; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; IBA:GO_Central.
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; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..363
FT /note="Translocating chain-associated membrane protein 1-
FT like 1"
FT /id="PRO_0000313707"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..80
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..159
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..218
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..295
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 116..324
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 338..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 39
FT /note="M -> L (in Ref. 1; BAC38746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40983 MW; FFEC1778C2307EC6 CRC64;
MGLRKKNARN PPVLSHEFMV QNHADMVSCV GMFFVLGLMF EGTSEMSIAF LTLQHGVVVP
AEGLPSGSRT LYHYGVKDLA TVFFYMLVAI IIHATIQEYV LDKLSRRLQL TKGKQNKLNE
AGQLSVFYIV SGIWGMIILA SENCLSDPTL LWKSQPHNMM TFQMKFFYIS QLAYWFHSFP
ELYFQKVRKQ DIPGQLIYIG LHLFHIGGAY LLYLNHLGLL LLMLHYAVEL LSSVCSLLYF
GDERYQKGLS LWPIVFISGR LVTLIVSVVT VGLHLAGTNR NGNALSGNVN VLAAKIAVLS
SSCSIQVYIT WTLTTVWLQR WLEDANLHVC GRKRRSRARK GTENGVENPN RIDSPPKKKE
KAP
