TMED7_RAT
ID TMED7_RAT Reviewed; 226 AA.
AC D3ZTX0;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Transmembrane emp24 domain-containing protein 7;
DE AltName: Full=p24 family protein gamma-3;
DE Short=p24gamma3;
DE AltName: Full=p27;
DE Flags: Precursor;
GN Name=Tmed7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PROTEIN SEQUENCE OF 37-54, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9472029; DOI=10.1083/jcb.140.4.751;
RA Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P.,
RA Thomas D.Y., Bergeron J.J., Nilsson T.;
RT "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both
RT COP I and II coatomer.";
RL J. Cell Biol. 140:751-765(1998).
CC -!- FUNCTION: Potential role in vesicular protein trafficking, mainly in
CC the early secretory pathway. Appears to play a role in the biosynthesis
CC of secreted cargo including processing and post-translational
CC modifications (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Predominantly monomeric and to lesser extent homodimeric in
CC endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate
CC compartment and trans-Golgi network. Oligomerizes with other members of
CC the EMP24/GP25L family such as TMED2, TMED9 and TMED10. Interacts (via
CC C-terminus) with COPG1; the interaction involves dimeric TMED7 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:9472029}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:9472029}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:9472029}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000269|PubMed:9472029}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:9472029}. Cytoplasmic
CC vesicle, COPI-coated vesicle membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Note=Cycles between compartments of the early
CC secretatory pathway.
CC -!- PTM: N-linked glycosylated in complex form containing terminal sialic
CC acid. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; CH473971; EDM14393.1; -; Genomic_DNA.
DR RefSeq; NP_001099228.1; NM_001105758.1.
DR AlphaFoldDB; D3ZTX0; -.
DR SMR; D3ZTX0; -.
DR IntAct; D3ZTX0; 3.
DR STRING; 10116.ENSRNOP00000004942; -.
DR GlyGen; D3ZTX0; 1 site.
DR jPOST; D3ZTX0; -.
DR PaxDb; D3ZTX0; -.
DR PeptideAtlas; D3ZTX0; -.
DR PRIDE; D3ZTX0; -.
DR Ensembl; ENSRNOT00000004942; ENSRNOP00000004942; ENSRNOG00000003691.
DR GeneID; 252889; -.
DR KEGG; rno:252889; -.
DR UCSC; RGD:727954; rat.
DR CTD; 51014; -.
DR RGD; 727954; Tmed7.
DR eggNOG; KOG1693; Eukaryota.
DR GeneTree; ENSGT00940000158463; -.
DR HOGENOM; CLU_066963_6_0_1; -.
DR InParanoid; D3ZTX0; -.
DR OMA; NAEDCFY; -.
DR OrthoDB; 1292519at2759; -.
DR PhylomeDB; D3ZTX0; -.
DR TreeFam; TF313000; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:D3ZTX0; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Proteomes; UP000234681; Chromosome 18.
DR Bgee; ENSRNOG00000003691; Expressed in duodenum and 20 other tissues.
DR Genevisible; D3ZTX0; RN.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
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:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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 InterPro; IPR015718; TMED7.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR PANTHER; PTHR22811:SF117; PTHR22811:SF117; 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; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..226
FT /note="Transmembrane emp24 domain-containing protein 7"
FT /id="PRO_0000413989"
FT TOPO_DOM 36..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..130
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT MOTIF 213..226
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 213..214
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 226 AA; 25479 MW; 88DF436F6A4A5A6A CRC64;
MPRPRSATCW AAAAGRWSCR LLALLLLLLL PGPSGGSEIT FELPDNAKQC FYEDITQGTK
CTLEFQVITG GHYDVDCRLE DPDGKVLYKE MKKQYDSFTF TASKNGTYKF CFSNEFSTFT
HKTVYFDFQV GEDPPLFPSE NRVSALTQME SACVSIHEAL KSVIDYQTHF RLREAQGRSR
AEDLNTRVAY WSVGEALILL VVSIGQVFLL KSFFSDKRTT TTRVGS