TMED9_BOVIN
ID TMED9_BOVIN Reviewed; 235 AA.
AC Q3T133; Q5E957;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Interacts with STX17; the interaction is direct
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane
CC protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Cycles between compartments of the early secretatory pathway.
CC {ECO:0000250}.
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; BT021063; AAX09080.1; -; mRNA.
DR EMBL; BC102145; AAI02146.1; -; mRNA.
DR RefSeq; NP_001029984.1; NM_001034812.2.
DR PDB; 4J73; X-ray; 1.44 A; B=229-235.
DR PDBsum; 4J73; -.
DR AlphaFoldDB; Q3T133; -.
DR SMR; Q3T133; -.
DR IntAct; Q3T133; 4.
DR MINT; Q3T133; -.
DR STRING; 9913.ENSBTAP00000001830; -.
DR PaxDb; Q3T133; -.
DR PeptideAtlas; Q3T133; -.
DR PRIDE; Q3T133; -.
DR Ensembl; ENSBTAT00000001830; ENSBTAP00000001830; ENSBTAG00000001394.
DR GeneID; 618580; -.
DR KEGG; bta:618580; -.
DR CTD; 54732; -.
DR VEuPathDB; HostDB:ENSBTAG00000001394; -.
DR eggNOG; KOG1690; Eukaryota.
DR GeneTree; ENSGT00940000159747; -.
DR HOGENOM; CLU_066963_2_2_1; -.
DR InParanoid; Q3T133; -.
DR OMA; MSHRVRM; -.
DR OrthoDB; 1294924at2759; -.
DR TreeFam; TF314123; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000001394; Expressed in saliva-secreting gland and 103 other tissues.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISS:UniProtKB.
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 3D-structure; Acetylation; Coiled coil; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000250"
FT CHAIN 38..235
FT /note="Transmembrane emp24 domain-containing protein 9"
FT /id="PRO_0000042789"
FT TOPO_DOM 38..201
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..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 110
FT /note="F -> I (in Ref. 1; AAX09080)"
FT /evidence="ECO:0000305"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:4J73"
SQ SEQUENCE 235 AA; 27298 MW; 3F38C286A2021C16 CRC64;
MAAERSLWVV GLCPGSRLGR VVRVLLLLLW FAARGGALYF HIGETEKKCF IEEIPDETMV
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
