TMED2_HUMAN
ID TMED2_HUMAN Reviewed; 201 AA.
AC Q15363;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Transmembrane emp24 domain-containing protein 2;
DE AltName: Full=Membrane protein p24A;
DE AltName: Full=p24;
DE AltName: Full=p24 family protein beta-1;
DE Short=p24beta1;
DE Flags: Precursor;
GN Name=TMED2; Synonyms=RNP24;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8663407; DOI=10.1074/jbc.271.29.17183;
RA Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R., Nastainczyk W.,
RA Schulz I.;
RT "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal
RT membranes, are members of a protein family involved in vesicular
RT trafficking.";
RL J. Biol. Chem. 271:17183-17189(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH COPI AND COPII VESICLE COAT.
RX PubMed=9472029; DOI=10.1083/jcb.140.4.751;
RA Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P.,
RA Thomas D.Y., Bergeron J.J., Nilsson T.;
RT "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both
RT COP I and II coatomer.";
RL J. Cell Biol. 140:751-765(1998).
RN [4]
RP SUBUNIT.
RX PubMed=10359607; DOI=10.1091/mbc.10.6.1939;
RA Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.;
RT "Localization and recycling of gp27 (hp24gamma3): complex formation with
RT other p24 family members.";
RL Mol. Biol. Cell 10:1939-1955(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 194-PHE-PHE-195 AND 198-ARG-ARG-199.
RX PubMed=10761932; DOI=10.1016/s0092-8674(00)80703-5;
RA Goldberg J.;
RT "Decoding of sorting signals by coatomer through a GTPase switch in the
RT COPI coat complex.";
RL Cell 100:671-679(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10852829; DOI=10.1242/jcs.113.13.2507;
RA Emery G., Rojo M., Gruenberg J.;
RT "Coupled transport of p24 family members.";
RL J. Cell Sci. 113:2507-2516(2000).
RN [7]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12237308; DOI=10.1074/jbc.m206989200;
RA Jenne N., Frey K., Brugger B., Wieland F.T.;
RT "Oligomeric state and stoichiometry of p24 proteins in the early secretory
RT pathway.";
RL J. Biol. Chem. 277:46504-46511(2002).
RN [8]
RP INTERACTION WITH COPG1.
RX PubMed=16940185; DOI=10.1128/mcb.01055-06;
RA Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.;
RT "Coatomer, the coat protein of COPI transport vesicles, discriminates
RT endoplasmic reticulum residents from p24 proteins.";
RL Mol. Cell. Biol. 26:8011-8021(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH F2RL1.
RX PubMed=17693410; DOI=10.1074/jbc.m703205200;
RA Luo W., Wang Y., Reiser G.;
RT "p24A, a type I transmembrane protein, controls ARF1-dependent
RT resensitization of protease-activated receptor-2 by influence on receptor
RT trafficking.";
RL J. Biol. Chem. 282:30246-30255(2007).
RN [10]
RP INTERACTION WITH ATL1.
RX PubMed=17321752; DOI=10.1016/j.mcn.2007.01.012;
RA Namekawa M., Muriel M.-P., Janer A., Latouche M., Dauphin A., Debeir T.,
RA Martin E., Duyckaerts C., Prigent A., Depienne C., Sittler A., Brice A.,
RA Ruberg M.;
RT "Mutations in the SPG3A gene encoding the GTPase atlastin interfere with
RT vesicle trafficking in the ER/Golgi interface and Golgi morphogenesis.";
RL Mol. Cell. Neurosci. 35:1-13(2007).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH SURF4 AND TMED10.
RX PubMed=18287528; DOI=10.1091/mbc.e07-10-0989;
RA Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.;
RT "The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate
RT compartment (ERGIC)-53, and p25 are required to maintain the architecture
RT of ERGIC and Golgi.";
RL Mol. Biol. Cell 19:1976-1990(2008).
RN [12]
RP FUNCTION, INTERACTION WITH CASR, AND MUTAGENESIS OF 194-PHE-PHE-195.
RX PubMed=20361938; DOI=10.1016/j.bbrc.2010.03.156;
RA Stepanchick A., Breitwieser G.E.;
RT "The cargo receptor p24A facilitates calcium sensing receptor maturation
RT and stabilization in the early secretory pathway.";
RL Biochem. Biophys. Res. Commun. 395:136-140(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH CD59; SEC24A; SEC24B; SEC24C AND SEC24D.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, AND INTERACTION WITH F2R; P2RY4; P2RY11 AND OPRM1.
RX PubMed=21219331; DOI=10.1111/j.1471-4159.2011.07173.x;
RA Luo W., Wang Y., Reiser G.;
RT "Proteinase-activated receptors, nucleotide P2Y receptors, and mu-opioid
RT receptor-1B are under the control of the type I transmembrane proteins p23
RT and p24A in post-Golgi trafficking.";
RL J. Neurochem. 117:71-81(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 19-114, AND INTERACTION WITH
RP TMED10.
RX PubMed=27569046; DOI=10.1016/j.jmb.2016.08.023;
RA Nagae M., Hirata T., Morita-Matsumoto K., Theiler R., Fujita M.,
RA Kinoshita T., Yamaguchi Y.;
RT "3D structure and interaction of p24beta and p24delta golgi dynamics
RT domains: implication for p24 complex formation and cargo transport.";
RL J. Mol. Biol. 428:4087-4099(2016).
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. {ECO:0000269|PubMed:10761932,
CC ECO:0000269|PubMed:17693410, ECO:0000269|PubMed:20361938,
CC ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.
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 (By similarity). Interacts with CD59, SEC24A, SEC24B,
CC SEC24C, SEC24D and ATL1. Interacts with KDELR1; the interaction is
CC decreased by KDEL ligand (By similarity). Interacts with F2RL1; the
CC interaction occurs at the Golgi apparatus. Interacts with CASR
CC (immaturely glycosylated form); the interaction occurs in the
CC endoplasmic reticulum-Golgi intermediate compartment or cis-Golgi.
CC Interacts with F2RL1; the interaction occurs at the Golgi apparatus.
CC Interacts with GORASP1 and GORASP2 (By similarity). Found in a complex
CC composed at least of SURF4, TMED2 and TMED10.
CC {ECO:0000250|UniProtKB:Q63524, ECO:0000269|PubMed:10359607,
CC ECO:0000269|PubMed:12237308, ECO:0000269|PubMed:16940185,
CC ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:17693410,
CC ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:20361938,
CC ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331,
CC ECO:0000269|PubMed:27569046}.
CC -!- INTERACTION:
CC Q15363; P41180: CASR; NbExp=3; IntAct=EBI-998485, EBI-4400127;
CC Q15363; P13987: CD59; NbExp=4; IntAct=EBI-998485, EBI-297972;
CC Q15363; P55085: F2RL1; NbExp=6; IntAct=EBI-998485, EBI-4303189;
CC Q15363; P49755: TMED10; NbExp=7; IntAct=EBI-998485, EBI-998422;
CC Q15363; O35587: TMED10; Xeno; NbExp=2; IntAct=EBI-998485, EBI-4405327;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000269|PubMed:9472029}; Single-pass
CC type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000269|PubMed:10852829,
CC ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass
CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass
CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000269|PubMed:12237308};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Cycles between
CC compartments of the early secretatory pathway.
CC {ECO:0000269|PubMed:12237308}.
CC -!- MISCELLANEOUS: Ectopic expression of TMED2 alone does not result in its
CC proper cis-Golgi network localization. Coexpression of TMED10 is
CC necessary, and coexpression of TMED3 and/or TMED9 is facilitating
CC localization. Down-regulation of TMED10 expression reduces TMED2
CC protein level.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; X92098; CAA63069.1; -; mRNA.
DR EMBL; BC025957; AAH25957.1; -; mRNA.
DR CCDS; CCDS9250.1; -.
DR RefSeq; NP_001308374.1; NM_001321445.1.
DR RefSeq; NP_006806.1; NM_006815.3.
DR PDB; 5AZW; X-ray; 1.50 A; A/B=19-114.
DR PDBsum; 5AZW; -.
DR AlphaFoldDB; Q15363; -.
DR SMR; Q15363; -.
DR BioGRID; 116158; 113.
DR ELM; Q15363; -.
DR IntAct; Q15363; 62.
DR MINT; Q15363; -.
DR STRING; 9606.ENSP00000262225; -.
DR TCDB; 9.B.188.1.2; the transmembrane emp24 domain-containing protein (tmed) family.
DR iPTMnet; Q15363; -.
DR MetOSite; Q15363; -.
DR PhosphoSitePlus; Q15363; -.
DR BioMuta; TMED2; -.
DR DMDM; 3914237; -.
DR EPD; Q15363; -.
DR jPOST; Q15363; -.
DR MassIVE; Q15363; -.
DR PaxDb; Q15363; -.
DR PeptideAtlas; Q15363; -.
DR PRIDE; Q15363; -.
DR ProteomicsDB; 60540; -.
DR TopDownProteomics; Q15363; -.
DR Antibodypedia; 2983; 156 antibodies from 24 providers.
DR DNASU; 10959; -.
DR Ensembl; ENST00000262225.8; ENSP00000262225.3; ENSG00000086598.11.
DR GeneID; 10959; -.
DR KEGG; hsa:10959; -.
DR MANE-Select; ENST00000262225.8; ENSP00000262225.3; NM_006815.4; NP_006806.1.
DR CTD; 10959; -.
DR DisGeNET; 10959; -.
DR GeneCards; TMED2; -.
DR HGNC; HGNC:16996; TMED2.
DR HPA; ENSG00000086598; Low tissue specificity.
DR MIM; 619642; gene.
DR neXtProt; NX_Q15363; -.
DR OpenTargets; ENSG00000086598; -.
DR PharmGKB; PA142670796; -.
DR VEuPathDB; HostDB:ENSG00000086598; -.
DR eggNOG; KOG1692; Eukaryota.
DR GeneTree; ENSGT00940000155143; -.
DR InParanoid; Q15363; -.
DR OMA; ADSSWHY; -.
DR OrthoDB; 1328081at2759; -.
DR PhylomeDB; Q15363; -.
DR TreeFam; TF313000; -.
DR PathwayCommons; Q15363; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; Q15363; -.
DR BioGRID-ORCS; 10959; 420 hits in 1079 CRISPR screens.
DR ChiTaRS; TMED2; human.
DR GeneWiki; TMED2; -.
DR GenomeRNAi; 10959; -.
DR Pharos; Q15363; Tbio.
DR PRO; PR:Q15363; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15363; protein.
DR Bgee; ENSG00000086598; Expressed in parotid gland and 215 other tissues.
DR ExpressionAtlas; Q15363; baseline and differential.
DR Genevisible; Q15363; HS.
DR GO; GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; ISS:HGNC-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:HGNC-UCL.
DR GO; GO:1905069; P:allantois development; IEA:Ensembl.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0060717; P:chorion development; IEA:Ensembl.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; TAS:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0036499; P:PERK-mediated unfolded protein response; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:2000638; P:regulation of SREBP signaling pathway; IEA:Ensembl.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
DR GO; GO:0035459; P:vesicle cargo loading; TAS:UniProtKB.
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 3D-structure; Coiled coil; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..201
FT /note="Transmembrane emp24 domain-containing protein 2"
FT /id="PRO_0000010381"
FT TOPO_DOM 21..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..112
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..181
FT /note="Interaction with F2RL1"
FT /evidence="ECO:0000269|PubMed:17693410"
FT REGION 118..157
FT /note="Required for TMED10 and TMED2 cis-Golgi network
FT localization"
FT COILED 117..167
FT /evidence="ECO:0000255"
FT MOTIF 194..201
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 194..195
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MUTAGEN 194..195
FT /note="FF->AA: Disrupts association with coatomer; when
FT associated with S-198-199-S."
FT /evidence="ECO:0000269|PubMed:10761932,
FT ECO:0000269|PubMed:20361938"
FT MUTAGEN 194..195
FT /note="FF->AA: Reduced surface and total expression of
FT CASR."
FT /evidence="ECO:0000269|PubMed:10761932,
FT ECO:0000269|PubMed:20361938"
FT MUTAGEN 198..199
FT /note="RR->SS: Disrupts association with coatomer; when
FT associated with A-194-195-A."
FT /evidence="ECO:0000269|PubMed:10761932"
FT MUTAGEN 198..199
FT /note="RR->SS: No inhibition of coatomer-dependent GTP
FT hydrolysis."
FT /evidence="ECO:0000269|PubMed:10761932"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 68..83
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 85..96
FT /evidence="ECO:0007829|PDB:5AZW"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:5AZW"
SQ SEQUENCE 201 AA; 22761 MW; C452370E459DC894 CRC64;
MVTLAELLVL LAALLATVSG YFVSIDAHAE ECFFERVTSG TKMGLIFEVA EGGFLDIDVE
ITGPDNKGIY KGDRESSGKY TFAAHMDGTY KFCFSNRMST MTPKIVMFTI DIGEAPKGQD
METEAHQNKL EEMINELAVA MTAVKHEQEY MEVRERIHRA INDNTNSRVV LWSFFEALVL
VAMTLGQIYY LKRFFEVRRV V
