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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
 
 
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