ID   TMD11_CANLF             Reviewed;         215 AA.
AC   P27869;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Transmembrane emp24 domain-containing protein 11;
DE   AltName: Full=Glycoprotein 25L;
DE            Short=GP25L;
DE   AltName: Full=p24 family protein alpha-1;
DE            Short=p24alpha1;
DE   Flags: Precursor;
GN   Name=TMED11;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=1918067; DOI=10.1016/s0021-9258(18)55036-5;
RA   Wada I., Rindress D., Cameron P.H., Ou W.-J., Doherty J.J. II, Louvard D.,
RA   Bell A.W., Dignard D., Thomas D.Y., Bergeron J.J.M.;
RT   "SSR alpha and associated calnexin are major calcium binding proteins of
RT   the endoplasmic reticulum membrane.";
RL   J. Biol. Chem. 266:19599-19610(1991).
CC   -!- FUNCTION: Part of a complex whose function is to bind Ca(2+) to the ER
CC       membrane and thereby regulate the retention of ER resident proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC       I membrane protein.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR   EMBL; X53592; CAA37662.1; -; mRNA.
DR   PIR; C37273; C37273.
DR   RefSeq; NP_001003286.1; NM_001003286.1.
DR   AlphaFoldDB; P27869; -.
DR   SMR; P27869; -.
DR   ELM; P27869; -.
DR   STRING; 9615.ENSCAFP00000024552; -.
DR   PaxDb; P27869; -.
DR   Ensembl; ENSCAFT00030000959; ENSCAFP00030000831; ENSCAFG00030000584.
DR   Ensembl; ENSCAFT00040006408; ENSCAFP00040005548; ENSCAFG00040003360.
DR   Ensembl; ENSCAFT00845001546; ENSCAFP00845001218; ENSCAFG00845000919.
DR   GeneID; 403969; -.
DR   KEGG; cfa:403969; -.
DR   CTD; 67366; -.
DR   VEuPathDB; HostDB:ENSCAFG00845000919; -.
DR   eggNOG; KOG1690; Eukaryota.
DR   GeneTree; ENSGT00940000160999; -.
DR   HOGENOM; CLU_066963_2_2_1; -.
DR   InParanoid; P27869; -.
DR   OMA; SAAFYFH; -.
DR   OrthoDB; 1294924at2759; -.
DR   TreeFam; TF314123; -.
DR   Proteomes; UP000002254; Chromosome 3.
DR   Bgee; ENSCAFG00000016696; Expressed in pancreas and 25 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:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IPR015719; TMED11.
DR   PANTHER; PTHR22811; PTHR22811; 1.
DR   PANTHER; PTHR22811:SF3; PTHR22811:SF3; 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   Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..17
FT   CHAIN           18..215
FT                   /note="Transmembrane emp24 domain-containing protein 11"
FT                   /id="PRO_0000010378"
FT   TOPO_DOM        18..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..125
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   COILED          129..171
FT                   /evidence="ECO:0000255"
FT   MOTIF           208..215
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   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   215 AA;  24882 MW;  4A0DA7DFD0075815 CRC64;
     MPMLAFALSF YFSLSTAFYF HVGEREEKCI IEDIPSDTLV TGTFKTQQWD FRRQDFLESA
     PGLGMFVTVT TYNDEVLLSK LYGPQGRFYF TSHSPGEHII CLESNSTRLV SFGGSKLRIH
     LEIRVGQHDL DAAIAQAKDK VNEVSFKLEH LIEQIEQIVK EQNYQRDREE NFRMISEDTN
     SNVLWWAFAQ TLIFIAIGIF QMKSLKNFFI AKKLV