TMED2_CRIGR
ID TMED2_CRIGR Reviewed; 196 AA.
AC P49020;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Transmembrane emp24 domain-containing protein 2;
DE AltName: Full=COPI-coated vesicle membrane protein p24;
DE AltName: Full=p24 family protein beta-1;
DE Short=p24beta1;
DE Flags: Precursor; Fragment;
GN Name=TMED2; Synonyms=RNP24;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7644530; DOI=10.1073/pnas.92.17.8011;
RA Stamnes M.A., Craighead M.W., Hoe M.H., Lampen N., Geromanos S., Tempst P.,
RA Rothman J.E.;
RT "An integral membrane component of coatomer-coated transport vesicles
RT defines a family of proteins involved in budding.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8011-8015(1995).
CC -!- FUNCTION: Involved in vesicular protein trafficking. Mainly functions
CC in the early secretory pathway but also in post-Golgi membranes.
CC Thought to act as cargo receptor at the lumenal side for incorporation
CC of secretory cargo molecules into transport vesicles and to be involved
CC in vesicle coat formation at the cytoplasmic side. In COPII vesicle-
CC mediated anterograde transport involved in the transport of GPI-
CC anchored proteins and proposed to act together with TMED10 as their
CC cargo receptor; the function specifically implies SEC24C and SEC24D of
CC the COPII vesicle coat and lipid raft-like microdomains of the ER.
CC Recognizes GPI anchors structural remodeled in the ER by PGAP1 and
CC MPPE1. In COPI vesicle-mediated retrograde transport inhibits the
CC GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing
CC immature uncoating and allowing cargo selection to take place. Involved
CC in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1,
CC OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma
CC membrane thus contributing to receptor resensitization. Facilitates
CC CASR maturation and stabilization in the early secretory pathway and
CC increases CASR plasma membrane targeting. Proposed to be involved in
CC organization of intracellular membranes such as the maintenance of the
CC Golgi apparatus. May also play a role in the biosynthesis of secreted
CC cargo such as eventual processing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer in the endoplasmic reticulum,
CC endoplasmic reticulum-Golgi intermediate compartment and Golgi.
CC Probably oligomerizes with other members of the EMP24/GP25L family such
CC as TMED7, TMED9 and TMED10. Interacts (via GOLD domain) with TMED10
CC (via GOLD domain). Associates with the COPI vesicle coat (coatomer);
CC TMED10:TMED2 heterotetramers are proposed to be involved in coatomer
CC association. Interacts (via C-terminus) with COPG1; the interaction
CC involves dimeric TMED2. Interacts with SEC23A; indicative for an
CC association of TMED2 with the COPII vesicle coat. Interacts with ARF1
CC and ARFGAP1. Interacts with CD59, SEC24A, SEC24B, SEC24C, SEC24D and
CC ATL1. Interacts with KDELR1; the interaction is decreased by KDEL
CC ligand. Interacts with F2RL1; the interaction occurs at the Golgi
CC apparatus. Interacts with CASR (immaturely glycosylated form); the
CC interaction occurs in the endoplasmic reticulum-Golgi intermediate
CC compartment or cis-Golgi. Interacts with F2RL1; the interaction occurs
CC at the Golgi apparatus. Interacts with GORASP1 and GORASP2. Found in a
CC complex composed at least of SURF4, TMED2 and TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:Q15363, ECO:0000250|UniProtKB:Q63524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=Cycles between compartments of the early
CC secretatory pathway. {ECO:0000250|UniProtKB:Q15363}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; U26264; AAA82925.1; -; mRNA.
DR AlphaFoldDB; P49020; -.
DR SMR; P49020; -.
DR ELM; P49020; -.
DR IntAct; P49020; 1.
DR STRING; 10029.XP_007623150.1; -.
DR eggNOG; KOG1692; Eukaryota.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:UniProtKB.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
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; ISS: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:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 Coiled coil; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL <1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..196
FT /note="Transmembrane emp24 domain-containing protein 2"
FT /id="PRO_0000010380"
FT TOPO_DOM 16..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..107
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 113..152
FT /note="Required for TMED10 and TMED2 cis-Golgi network
FT localization"
FT /evidence="ECO:0000250"
FT COILED 112..162
FT /evidence="ECO:0000255"
FT MOTIF 189..196
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 189..190
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 196 AA; 22189 MW; 63502CF101B77810 CRC64;
DVLVLLAALL ATASGYFVSI DAHAEECFFE RVTSGTKMGL IFEVAEGGFL DIDVEITGPD
NKGIYKGDRE SSGKYTFAAH MDGTYKFCFS NRMSTMTPKI VMFTIDIGEA PKGQDMETEA
HQNKLEEMIN ELAVAMTAVK HEQEYMEVRE RIHRAINDNT NSRVVLWSFF EALVLVAMTL
GQIYYLKRFF EVRRVV
