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 12-OCT-2022, entry version 117. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; ENSCAFT00000026438; ENSCAFP00000024552; ENSCAFG00000016696. 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 //