TMED3_MOUSE
ID TMED3_MOUSE Reviewed; 221 AA.
AC Q78IS1; Q9DC62; Q9DCK9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transmembrane emp24 domain-containing protein 3;
DE AltName: Full=p24 family protein gamma-4;
DE Short=p24gamma4;
DE Flags: Precursor;
GN Name=Tmed3;
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=Kidney, and Lung;
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 STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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).
CC -!- FUNCTION: Potential role in vesicular protein trafficking, mainly in
CC the early secretory pathway. Contributes to the coupled localization of
CC TMED2 and TMED10 in the cis-Golgi network (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer in endoplasmic reticulum, endoplasmic reticulum-Golgi
CC intermediate compartment and cis-Golgi network. Interacts (via C-
CC terminus) with COPG1; the interaction involves dimeric TMED3; however,
CC there are conflicting reports on the interaction. Interacts with
CC GORASP1 and GORASP2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I
CC membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane
CC protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q6AY25}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Probably cycles between compartments of the early
CC secretatory pathway. {ECO:0000250|UniProtKB:Q9Y3Q3}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22292.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK002698; BAB22292.1; ALT_FRAME; mRNA.
DR EMBL; AK004545; BAB23361.1; -; mRNA.
DR EMBL; BC023338; AAH23338.1; -; mRNA.
DR CCDS; CCDS23396.1; -.
DR RefSeq; NP_079636.2; NM_025360.2.
DR AlphaFoldDB; Q78IS1; -.
DR SMR; Q78IS1; -.
DR BioGRID; 211221; 2.
DR STRING; 10090.ENSMUSP00000058723; -.
DR PhosphoSitePlus; Q78IS1; -.
DR EPD; Q78IS1; -.
DR MaxQB; Q78IS1; -.
DR PaxDb; Q78IS1; -.
DR PeptideAtlas; Q78IS1; -.
DR PRIDE; Q78IS1; -.
DR ProteomicsDB; 259575; -.
DR Antibodypedia; 27806; 158 antibodies from 20 providers.
DR DNASU; 66111; -.
DR Ensembl; ENSMUST00000058488; ENSMUSP00000058723; ENSMUSG00000032353.
DR GeneID; 66111; -.
DR KEGG; mmu:66111; -.
DR UCSC; uc009qzo.2; mouse.
DR CTD; 23423; -.
DR MGI; MGI:1913361; Tmed3.
DR VEuPathDB; HostDB:ENSMUSG00000032353; -.
DR eggNOG; KOG1693; Eukaryota.
DR GeneTree; ENSGT00940000159833; -.
DR HOGENOM; CLU_066963_6_0_1; -.
DR InParanoid; Q78IS1; -.
DR OMA; GIGQVMM; -.
DR OrthoDB; 1328081at2759; -.
DR PhylomeDB; Q78IS1; -.
DR TreeFam; TF313000; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 66111; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmed3; mouse.
DR PRO; PR:Q78IS1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q78IS1; protein.
DR Bgee; ENSMUSG00000032353; Expressed in prostate gland ventral lobe and 272 other tissues.
DR Genevisible; Q78IS1; MM.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Methylation; Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..221
FT /note="Transmembrane emp24 domain-containing protein 3"
FT /id="PRO_0000010385"
FT TOPO_DOM 28..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..124
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT MOTIF 208..221
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 208..209
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 103
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY25"
FT CONFLICT 18
FT /note="L -> A (in Ref. 1; BAB23361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25465 MW; A1DA79631DAFB8DC CRC64;
MVHEAPHASS FQMLLQLLLL LLLRAEPLRS AELTFELPDN AKQCFHEEVE QGVKFSLDYQ
VITGGHYDVD CYVEDPRGNV IYRETKKQYD SFTYKTEAKG VYRFCFSNEF STFSHKTVYF
DFQVGDEPPI LPDMGNRVTA LTQMESACVT IHEALKTVID SQTHYRLREA QDRARAEDLN
SRVSYWSVGE TIALFVVSFS QVLLLKSFFT EKRPVNRAVH S
