TMED9_RAT
ID TMED9_RAT Reviewed; 235 AA.
AC Q5I0E7;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Transmembrane emp24 domain-containing protein 9;
DE AltName: Full=p24 family protein alpha-2;
DE Short=p24alpha2;
DE Flags: Precursor;
GN Name=Tmed9;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Lung;
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 PROTEIN SEQUENCE OF 38-64, SIGNAL SEQUENCE CLEAVAGE SITE, SUBUNIT, AND
RP 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).
RN [5]
RP INTERACTION WITH STX17.
RX PubMed=21545355; DOI=10.1042/bc20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain
RT the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
CC -!- FUNCTION: Appears to be involved in vesicular protein trafficking,
CC mainly in the early secretory pathway. In COPI vesicle-mediated
CC retrograde transport involved in the coatomer recruitment to membranes
CC of the early secretory pathway. Increases coatomer-dependent activity
CC of ARFGAP2. Thought to play a crucial role in the specific retention of
CC p24 complexes in cis-Golgi membranes; specifically contributes to the
CC coupled localization of TMED2 and TMED10 in the cis-Golgi network. May
CC be involved in organization of intracellular membranes, such as of the
CC ER-Golgi intermediate compartment and the Golgi apparatus. Involved in
CC ER localization of PTPN2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer in endoplasmic reticulum. Predominantly
CC monomeric and to lesser extent homodimeric in endoplasmic reticulum-
CC Golgi intermediate compartment and cis-Golgi network. Probably
CC oligomerizes with other members of the EMP24/GP25L family such as
CC TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-
CC terminus) with COPG1; the interaction involves dimeric TMED9. Interacts
CC with PTPN2 and SPAST (By similarity). Interacts with STX17; the
CC interaction is direct. {ECO:0000250, ECO:0000269|PubMed:21545355,
CC ECO:0000269|PubMed:9472029}.
CC -!- INTERACTION:
CC Q5I0E7; Q9R064: Gorasp2; NbExp=3; IntAct=EBI-920903, EBI-4422912;
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}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type
CC I membrane protein {ECO:0000250}. Note=Cycles between compartments of
CC the early secretatory pathway.
CC -!- PTM: N-linked glycosylated containing high mannose. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; CH474032; EDL93964.1; -; Genomic_DNA.
DR EMBL; BC088422; AAH88422.1; -; mRNA.
DR RefSeq; NP_001009703.1; NM_001009703.1.
DR AlphaFoldDB; Q5I0E7; -.
DR SMR; Q5I0E7; -.
DR BioGRID; 262515; 5.
DR IntAct; Q5I0E7; 5.
DR STRING; 10116.ENSRNOP00000030668; -.
DR GlyGen; Q5I0E7; 1 site.
DR jPOST; Q5I0E7; -.
DR PaxDb; Q5I0E7; -.
DR PRIDE; Q5I0E7; -.
DR Ensembl; ENSRNOT00000109911; ENSRNOP00000083476; ENSRNOG00000021882.
DR GeneID; 361207; -.
DR KEGG; rno:361207; -.
DR UCSC; RGD:1307627; rat.
DR CTD; 54732; -.
DR RGD; 1307627; Tmed9.
DR eggNOG; KOG1690; Eukaryota.
DR GeneTree; ENSGT00940000159747; -.
DR HOGENOM; CLU_066963_2_2_1; -.
DR InParanoid; Q5I0E7; -.
DR OMA; MSHRVRM; -.
DR OrthoDB; 1294924at2759; -.
DR PhylomeDB; Q5I0E7; -.
DR TreeFam; TF314123; -.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q5I0E7; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000021882; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5I0E7; RN.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISO:RGD.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:9472029"
FT CHAIN 38..235
FT /note="Transmembrane emp24 domain-containing protein 9"
FT /id="PRO_0000413988"
FT TOPO_DOM 38..202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..145
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 121..160
FT /note="Required for interaction with STX17"
FT /evidence="ECO:0000250"
FT COILED 154..184
FT /evidence="ECO:0000255"
FT MOTIF 228..235
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 228..229
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KF1"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 27028 MW; 32F0D1DCC9EFBA6E CRC64;
MAAVRGVRVV GTSPGLLLGR GMRAFLLLLC LAARGGALYF HIGETEKKCF IEEIPDETMV
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
