ID   TMEDA_TAKRU             Reviewed;         213 AA.
AC   Q90515;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Transmembrane emp24 domain-containing protein 10;
DE   AltName: Full=S31III125;
DE   AltName: Full=Transmembrane protein Tmp21;
DE   AltName: Full=p24 family protein delta-1;
DE            Short=p24delta1;
DE   Flags: Precursor;
GN   Name=tmed10; Synonyms=tmp21;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., Rogaev E.I.,
RA   St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated with
RT   familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: Involved in vesicular protein trafficking. Mainly functions
CC       in the early secretory pathway. Thought to act as cargo receptor at the
CC       lumenal side for incorporation of secretory cargo molecules into
CC       transport vesicles and to be involved in vesicle coat formation at the
CC       cytoplasmic side (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Probably oligomerizes with other members of the EMP24/GP25L
CC       family. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum-Golgi
CC       intermediate compartment membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR   EMBL; U40761; AAC59782.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90515; -.
DR   SMR; Q90515; -.
DR   STRING; 31033.ENSTRUP00000027091; -.
DR   eggNOG; KOG1691; Eukaryota.
DR   InParanoid; Q90515; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
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   PANTHER; PTHR22811; PTHR22811; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..213
FT                   /note="Transmembrane emp24 domain-containing protein 10"
FT                   /id="PRO_0000010405"
FT   TOPO_DOM        20..179
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..187
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   MOTIF           205..213
FT                   /note="COPI vesicle coat-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           205..206
FT                   /note="COPII vesicle coat-binding"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   213 AA;  24653 MW;  895DFA3C1484AC84 CRC64;
     MARLTALLFL PVLIESAFSI SFFLPVNTRK CLREEIHKDV LVTGEYEISE QVVTVHTSST
     VVGDGSIFKI TDSSSHTLYS KEDATKGKFA FTTEDYDMFE VCFESKCTGR VPDQLVNLDM
     KHGVEAKNYE EIAKVEKLKP LEVELRRLED LSESIVNDFA YMKKREEEMR DTNESTNTRV
     LYFSIFSMFC LIGLATWQVF YLRRFFKAKK LIE