TRAM2_MOUSE
ID TRAM2_MOUSE Reviewed; 370 AA.
AC Q924Z5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translocating chain-associated membrane protein 2;
GN Name=Tram2;
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=C57BL/6J;
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 INTERACTION WITH SERCA2B.
RX PubMed=14749390; DOI=10.1128/mcb.24.4.1758-1768.2004;
RA Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
RT "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and
RT is necessary for collagen type I synthesis.";
RL Mol. Cell. Biol. 24:1758-1768(2004).
CC -!- FUNCTION: Necessary for collagen type I synthesis. May couple the
CC activity of the ER Ca(2+) pump SERCA2B with the activity of the
CC translocon. This coupling may increase the local Ca(2+) concentration
CC at the site of collagen synthesis, and a high Ca(2+) concentration may
CC be necessary for the function of molecular chaperones involved in
CC collagen folding. Required for proper insertion of the first
CC transmembrane helix N-terminus of TM4SF20 into the ER lumen, may act as
CC a ceramide sensor for regulated alternative translocation (RAT).
CC {ECO:0000250|UniProtKB:Q15035}.
CC -!- SUBUNIT: Interacts with COL1A1 (By similarity). Interacts with SERCA2B.
CC {ECO:0000250, ECO:0000269|PubMed:14749390}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAM family. {ECO:0000305}.
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DR EMBL; AY029530; AAK40298.1; -; mRNA.
DR EMBL; AK082751; BAC38601.1; -; mRNA.
DR EMBL; BC018212; AAH18212.1; -; mRNA.
DR CCDS; CCDS14846.1; -.
DR RefSeq; NP_803128.1; NM_177409.3.
DR AlphaFoldDB; Q924Z5; -.
DR BioGRID; 228462; 1.
DR STRING; 10090.ENSMUSP00000047992; -.
DR GlyGen; Q924Z5; 1 site.
DR iPTMnet; Q924Z5; -.
DR PhosphoSitePlus; Q924Z5; -.
DR EPD; Q924Z5; -.
DR jPOST; Q924Z5; -.
DR MaxQB; Q924Z5; -.
DR PaxDb; Q924Z5; -.
DR PeptideAtlas; Q924Z5; -.
DR PRIDE; Q924Z5; -.
DR ProteomicsDB; 258964; -.
DR Antibodypedia; 30914; 174 antibodies from 27 providers.
DR DNASU; 170829; -.
DR Ensembl; ENSMUST00000037998; ENSMUSP00000047992; ENSMUSG00000041779.
DR GeneID; 170829; -.
DR KEGG; mmu:170829; -.
DR UCSC; uc007alg.2; mouse.
DR CTD; 9697; -.
DR MGI; MGI:1924817; Tram2.
DR VEuPathDB; HostDB:ENSMUSG00000041779; -.
DR eggNOG; KOG1608; Eukaryota.
DR GeneTree; ENSGT00510000046470; -.
DR HOGENOM; CLU_062830_0_0_1; -.
DR InParanoid; Q924Z5; -.
DR OMA; CRLCMLL; -.
DR OrthoDB; 831082at2759; -.
DR PhylomeDB; Q924Z5; -.
DR TreeFam; TF314319; -.
DR BioGRID-ORCS; 170829; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tram2; mouse.
DR PRO; PR:Q924Z5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q924Z5; protein.
DR Bgee; ENSMUSG00000041779; Expressed in ascending aorta and 180 other tissues.
DR Genevisible; Q924Z5; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0032964; P:collagen biosynthetic process; ISO:MGI.
DR GO; GO:0045048; P:protein insertion into ER membrane; 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 Glycoprotein; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..370
FT /note="Translocating chain-associated membrane protein 2"
FT /id="PRO_0000185533"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..75
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..159
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..287
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 112..321
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 332..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 43183 MW; F8E768AFB0582548 CRC64;
MAFRRRTKSY PLFSQEFIIH NHADIGFCLV LCVLIGLMFE VTAKTAFLFI LPQYNISVPT
ADSETVHYHY GPKDLVTILF YVVITIIFHA VVQEYILDKI SKRLHLSKVK HSKFNESGQL
LVFHLSAVAW CFYVIVTEGY LTNPRSLWED YPHVYLSFQV KFFYLGQLAY WLHSLPELYF
QKVRKEEVPR QLQYICLYLL HITGAYLLNL SRLGLILLLL QYSTEALFHM ARLFHFADEN
NERLFNAWAA VFGVTRLFIL TLAVLTIGFG LARVENQVFD PEKGNFNTLP CRLGMLLLVC
VAQAWLMWRF IHSQLRHWRE YWKEQSAKRR VSAVPRPPAK LLKREPGYHE NGVVKAENGT
SSRTKKLKSP
