ID   TMED3_RAT               Reviewed;         221 AA.
AC   Q6AY25;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   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 MRNA].
RC   TISSUE=Testis;
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   [2]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GORASP1 AND GORASP2.
RX   PubMed=11739402; DOI=10.1083/jcb.200108102;
RA   Barr F.A., Preisinger C., Kopajtich R., Koerner R.;
RT   "Golgi matrix proteins interact with p24 cargo receptors and aid their
RT   efficient retention in the Golgi apparatus.";
RL   J. Cell Biol. 155:885-891(2001).
RN   [3]
RP   METHYLATION AT ARG-103, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA   Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA   Yates J.R. III, Howell K.E.;
RT   "Organellar proteomics reveals Golgi arginine dimethylation.";
RL   Mol. Biol. Cell 15:2907-2919(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15718469; DOI=10.1126/science.1108061;
RA   Malsam J., Satoh A., Pelletier L., Warren G.;
RT   "Golgin tethers define subpopulations of COPI vesicles.";
RL   Science 307:1095-1098(2005).
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 (By similarity).
CC       Interacts with GORASP1 and GORASP2. {ECO:0000250,
CC       ECO:0000269|PubMed:11739402}.
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:0000269|PubMed:11739402}; 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:0000269|PubMed:15718469}; 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}.
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DR   EMBL; BC079220; AAH79220.1; -; mRNA.
DR   RefSeq; NP_001004249.1; NM_001004249.1.
DR   AlphaFoldDB; Q6AY25; -.
DR   SMR; Q6AY25; -.
DR   STRING; 10116.ENSRNOP00000018603; -.
DR   iPTMnet; Q6AY25; -.
DR   PhosphoSitePlus; Q6AY25; -.
DR   PaxDb; Q6AY25; -.
DR   GeneID; 300888; -.
DR   KEGG; rno:300888; -.
DR   UCSC; RGD:1303327; rat.
DR   CTD; 23423; -.
DR   RGD; 1303327; Tmed3.
DR   VEuPathDB; HostDB:ENSRNOG00000013889; -.
DR   eggNOG; KOG1693; Eukaryota.
DR   HOGENOM; CLU_066963_6_0_1; -.
DR   InParanoid; Q6AY25; -.
DR   OMA; GIGQVMM; -.
DR   OrthoDB; 1328081at2759; -.
DR   PhylomeDB; Q6AY25; -.
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:Q6AY25; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000013889; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6AY25; RN.
DR   GO; GO:0030126; C:COPI vesicle coat; IDA: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; IDA: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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..221
FT                   /note="Transmembrane emp24 domain-containing protein 3"
FT                   /id="PRO_0000010386"
FT   TOPO_DOM        31..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:0000269|PubMed:15047867"
SQ   SEQUENCE   221 AA;  25510 MW;  739E5B785791C443 CRC64;
     MGNEVPRASS FQMLMLLLLL LLLRAERLRG AELTFELPDN AKQCFHEEVE QGVKFSLDYQ
     VITGGHYDVD CYVEDPMGNI IYRETKKQYD SFTYKTEVKG VYRFCFSNEF STFSHKTVYF
     DFQVGDEPPI LPDMGNRVTA LTQMESACVT IHEALKTVID SQTHYRLREA QDRARAEDLN
     SRVSYWSVGE TIALFVVSFS QVLLLKSFFT EKRPINRAVH S