TMED5_MOUSE
ID TMED5_MOUSE Reviewed; 229 AA.
AC Q9CXE7; Q3TDS6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transmembrane emp24 domain-containing protein 5;
DE AltName: Full=p24 family protein gamma-2;
DE Short=p24gamma2;
DE Flags: Precursor;
GN Name=Tmed5;
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, and NOD; TISSUE=Colon, and Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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. Required for the maintenance of the Golgi
CC apparatus; involved in protein exchange between Golgi stacks during
CC assembly. Probably not required for COPI-vesicle-mediated retrograde
CC transport (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TMED9 and TMED10. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane
CC protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=Probably cycles between compartments of the early
CC secretatory pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AK014490; BAB29390.1; -; mRNA.
DR EMBL; AK033463; BAC28301.1; -; mRNA.
DR EMBL; AK170036; BAE41524.1; -; mRNA.
DR CCDS; CCDS19508.1; -.
DR RefSeq; NP_083152.1; NM_028876.2.
DR PDB; 5GU5; X-ray; 2.80 A; A=33-144.
DR PDBsum; 5GU5; -.
DR AlphaFoldDB; Q9CXE7; -.
DR SMR; Q9CXE7; -.
DR BioGRID; 215788; 3.
DR STRING; 10090.ENSMUSP00000002837; -.
DR PhosphoSitePlus; Q9CXE7; -.
DR EPD; Q9CXE7; -.
DR jPOST; Q9CXE7; -.
DR MaxQB; Q9CXE7; -.
DR PaxDb; Q9CXE7; -.
DR PeptideAtlas; Q9CXE7; -.
DR PRIDE; Q9CXE7; -.
DR ProteomicsDB; 259426; -.
DR TopDownProteomics; Q9CXE7; -.
DR Antibodypedia; 33655; 36 antibodies from 17 providers.
DR DNASU; 73130; -.
DR Ensembl; ENSMUST00000002837; ENSMUSP00000002837; ENSMUSG00000063406.
DR GeneID; 73130; -.
DR KEGG; mmu:73130; -.
DR UCSC; uc008ynp.1; mouse.
DR CTD; 50999; -.
DR MGI; MGI:1921586; Tmed5.
DR VEuPathDB; HostDB:ENSMUSG00000063406; -.
DR eggNOG; KOG3287; Eukaryota.
DR GeneTree; ENSGT00940000155468; -.
DR HOGENOM; CLU_066963_0_0_1; -.
DR InParanoid; Q9CXE7; -.
DR OMA; FATGGRM; -.
DR OrthoDB; 1292519at2759; -.
DR PhylomeDB; Q9CXE7; -.
DR TreeFam; TF313000; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 73130; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q9CXE7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXE7; protein.
DR Bgee; ENSMUSG00000063406; Expressed in dorsal pancreas and 245 other tissues.
DR ExpressionAtlas; Q9CXE7; baseline and differential.
DR Genevisible; Q9CXE7; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; 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; IBA:GO_Central.
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:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
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 InterPro; IPR015717; TMED5.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR PANTHER; PTHR22811:SF41; PTHR22811:SF41; 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 3D-structure; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..229
FT /note="Transmembrane emp24 domain-containing protein 5"
FT /id="PRO_0000010390"
FT TOPO_DOM 28..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..126
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 83..96
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5GU5"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:5GU5"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:5GU5"
SQ SEQUENCE 229 AA; 26172 MW; 731E97AC5C1212BC CRC64;
MGGRMWLPFP VLLLSALPAA LLRGAAGFTP SLDSDFTFTL PAGRKECFYQ PMPLKASLEI
EYQVLDGGEL DIDFHLTSPE GRTLVFEQRK SDGVHTIETE DGDYMFCFDN TFSTISEKVI
FFELILDNMG EEVQGQEDWK KYITNTDVLE MKLEDILESI NSIKSRLSKS GHIQTLLRAF
EARDRNIQES NFDRVNFWSV VNLMVMVVVS AIQVYTLKSL FEDKRKSRT
