CNR1_RAT
ID CNR1_RAT Reviewed; 473 AA.
AC P20272;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cannabinoid receptor 1;
DE Short=CB-R;
DE Short=CB1;
DE AltName: Full=Brain-type cannabinoid receptor;
GN Name=Cnr1; Synonyms=Skr6 {ECO:0000303|PubMed:2165569};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=2165569; DOI=10.1038/346561a0;
RA Matsuda L.A., Lolait S.J., Brownstein M.J., Young A.C., Bonner T.I.;
RT "Structure of a cannabinoid receptor and functional expression of the
RT cloned cDNA.";
RL Nature 346:561-564(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8832654; DOI=10.1016/0304-3940(96)12792-0;
RA Ho B.Y., Zhao J.;
RT "Determination of the cannabinoid receptors in mouse x rat hybridoma NG108-
RT 15 cells and rat GH4C1 cells.";
RL Neurosci. Lett. 212:123-126(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-107.
RX PubMed=7876112; DOI=10.1074/jbc.270.8.3726;
RA Shire D., Carillon C., Kaghad M., Calandra B., Rinaldi-Carmona M.,
RA Le Fur G., Caput D., Ferrara P.;
RT "An amino-terminal variant of the central cannabinoid receptor resulting
RT from alternative splicing.";
RL J. Biol. Chem. 270:3726-3731(1995).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10362691; DOI=10.1152/ajpheart.1999.276.6.h2085;
RA Gebremedhin D., Lange A.R., Campbell W.B., Hillard C.J., Harder D.R.;
RT "Cannabinoid CB1 receptor of cat cerebral arterial muscle functions to
RT inhibit L-type Ca2+ channel current.";
RL Am. J. Physiol. 276:H2085-H2093(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10891614; DOI=10.1016/s0306-4522(00)00157-3;
RA Denovan-Wright E.M., Robertson H.A.;
RT "Cannabinoid receptor messenger RNA levels decrease in a subset of neurons
RT of the lateral striatum, cortex and hippocampus of transgenic Huntington's
RT disease mice.";
RL Neuroscience 98:705-713(2000).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=16033894; DOI=10.1523/jneurosci.0442-05.2005;
RA Bodor A.L., Katona I., Nyiri G., Mackie K., Ledent C., Hajos N.,
RA Freund T.F.;
RT "Endocannabinoid signaling in rat somatosensory cortex: laminar differences
RT and involvement of specific interneuron types.";
RL J. Neurosci. 25:6845-6856(2005).
RN [7]
RP INTERACTION WITH CNRIP1.
RC TISSUE=Brain;
RX PubMed=17895407; DOI=10.1124/mol.107.039263;
RA Niehaus J.L., Liu Y., Wallis K.T., Egertova M., Bhartur S.G.,
RA Mukhopadhyay S., Shi S., He H., Selley D.E., Howlett A.C., Elphick M.R.,
RA Lewis D.L.;
RT "CB1 cannabinoid receptor activity is modulated by the cannabinoid receptor
RT interacting protein CRIP 1a.";
RL Mol. Pharmacol. 72:1557-1566(2007).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=18077343; DOI=10.1073/pnas.0706980105;
RA Heimann A.S., Gomes I., Dale C.S., Pagano R.L., Gupta A., de Souza L.L.,
RA Luchessi A.D., Castro L.M., Giorgi R., Rioli V., Ferro E.S., Devi L.A.;
RT "Hemopressin is an inverse agonist of CB1 cannabinoid receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20588-20593(2007).
RN [9]
RP INTERACTION WITH GNAI3 AND GNAO1, AND PALMITOYLATION AT CYS-416.
RX PubMed=21895628; DOI=10.1111/j.1476-5381.2011.01658.x;
RA Oddi S., Dainese E., Sandiford S., Fezza F., Lanuti M., Chiurchiu V.,
RA Totaro A., Catanzaro G., Barcaroli D., De Laurenzi V., Centonze D.,
RA Mukhopadhyay S., Selent J., Howlett A.C., Maccarrone M.;
RT "Effects of palmitoylation of Cys(415) in helix 8 of the CB(1) cannabinoid
RT receptor on membrane localization and signalling.";
RL Br. J. Pharmacol. 165:2635-2651(2012).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23955712; DOI=10.1038/nm.3265;
RA Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J., Tam J.,
RA Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M., Czech M.P.,
RA Kunos G.;
RT "Activation of the Nlrp3 inflammasome in infiltrating macrophages by
RT endocannabinoids mediates beta cell loss in type 2 diabetes.";
RL Nat. Med. 19:1132-1140(2013).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26671069; DOI=10.1371/journal.pone.0145244;
RA Arrabal S., Lucena M.A., Canduela M.J., Ramos-Uriarte A., Rivera P.,
RA Serrano A., Pavon F.J., Decara J., Vargas A., Baixeras E.,
RA Martin-Rufian M., Marquez J., Fernandez-Llebrez P., De Roos B., Grandes P.,
RA Rodriguez de Fonseca F., Suarez J.;
RT "Pharmacological blockade of cannabinoid CB1 receptors in diet-induced
RT obesity regulates mitochondrial dihydrolipoamide dehydrogenase in muscle.";
RL PLoS ONE 10:E0145244-E0145244(2015).
CC -!- FUNCTION: G-protein coupled receptor for cannabinoids, including
CC endocannabinoids (eCBs), such as N-arachidonoylethanolamide (also
CC called anandamide or AEA) and 2-arachidonoylglycerol (2-AG)
CC (PubMed:2165569). Mediates many cannabinoid-induced effects, acting,
CC among others, on food intake, memory loss, gastrointestinal motility,
CC catalepsy, ambulatory activity, anxiety, chronic pain. Signaling
CC typically involves reduction in cyclic AMP. In the hypothalamus, may
CC have a dual effect on mitochondrial respiration depending upon the
CC agonist dose and possibly upon the cell type. Increases respiration at
CC low doses, while decreases respiration at high doses. At high doses,
CC CNR1 signal transduction involves G-protein alpha-i protein activation
CC and subsequent inhibition of mitochondrial soluble adenylate cyclase,
CC decrease in cyclic AMP concentration, inhibition of protein kinase A
CC (PKA)-dependent phosphorylation of specific subunits of the
CC mitochondrial electron transport system, including NDUFS2. In the
CC hypothalamus, inhibits leptin-induced reactive oxygen species (ROS)
CC formation and mediates cannabinoid-induced increase in SREBF1 and FASN
CC gene expression. In response to cannabinoids, drives the release of
CC orexigenic beta-endorphin, but not that of melanocyte-stimulating
CC hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence
CC promoting food intake. In the hippocampus, regulates cellular
CC respiration and energy production in response to cannabinoids. Involved
CC in cannabinoid-dependent depolarization-induced suppression of
CC inhibition (DSI), a process in which depolarization of CA1 postsynaptic
CC pyramidal neurons mobilizes eCBs, which retrogradely activate
CC presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory
CC neurotransmission. Also reduces excitatory synaptic transmission (By
CC similarity). In superior cervical ganglions and cerebral vascular
CC smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a
CC constitutive, as well as agonist-dependent manner (By similarity).
CC Induces leptin production in adipocytes and reduces LRP2-mediated
CC leptin clearance in the kidney, hence participating in hyperleptinemia.
CC In adipose tissue, CNR1 signaling leads to increased expression of
CC SREBF1, ACACA and FASN genes. In the liver, activation by
CC endocannabinoids leads to increased de novo lipogenesis and reduced
CC fatty acid catabolism, associated with increased expression of
CC SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes. May also affect de
CC novo cholesterol synthesis and HDL-cholesteryl ether uptake (By
CC similarity). Peripherally modulates energy metabolism. In high
CC carbohydrate diet-induced obesity, may decrease the expression of
CC mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as
CC well as that of selected glucose/ pyruvate metabolic enzymes, hence
CC affecting energy expenditure through mitochondrial metabolism
CC (PubMed:26671069). In response to cannabinoid anandamide, elicits a
CC pro-inflammatory response in macrophages, which involves NLRP3
CC inflammasome activation and IL1B and IL18 secretion. In macrophages
CC infiltrating pancreatic islets, this process may participate in the
CC progression of type-2 diabetes and associated loss of pancreatic beta-
CC cells (PubMed:23955712). {ECO:0000250|UniProtKB:O02777,
CC ECO:0000250|UniProtKB:P47746, ECO:0000269|PubMed:2165569,
CC ECO:0000269|PubMed:23955712, ECO:0000269|PubMed:26671069}.
CC -!- ACTIVITY REGULATION: Hemopressin, a peptide derived from hemoglobin
CC subunit alpha (HBA1 and/or HBA2), acts as an antagonist peptide:
CC hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and
CC subsequent signaling. {ECO:0000269|PubMed:18077343}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CNRIP1 (PubMed:17895407).
CC Associates with G protein alpha subunits, including G(i) alpha-1/GNAI1,
CC G(i) alpha-3/GNAI3 and G(o)-alpha/GNAO1; palmitoylation is important
CC for interaction with GNAI3 and GNAO1 (PubMed:21895628).
CC {ECO:0000269|PubMed:17895407, ECO:0000269|PubMed:21895628}.
CC -!- INTERACTION:
CC P20272; P30543: Adora2a; NbExp=3; IntAct=EBI-2909800, EBI-2902822;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47746};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21554}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:P47746}. Cell
CC projection, axon {ECO:0000269|PubMed:16033894}. Presynapse
CC {ECO:0000269|PubMed:16033894}. Note=Unexpectedly, in the mitochondria,
CC the C-terminus is located in the mitochondrial intermembrane space, a
CC compartment topologically considered as extracellular. In canonical
CC seven-transmembrane G-protein coupled receptors, the C-terminus is
CC cytosolic (By similarity). In interneurons, found on the membrane of
CC cytoplasmic compartments, some of which could be elements of the
CC endosome-lysosome system and multivesicular bodies (PubMed:16033894).
CC Found on presynaptic axon terminals in some GABAergic neurons in the
CC somatosensory cortex (PubMed:16033894). {ECO:0000250|UniProtKB:P47746,
CC ECO:0000269|PubMed:16033894}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, in the striatum, medial
CC septum, descending arm of the band of Broca, the amygdaloid nucleus,
CC the hippocampus and cortex (at protein level). High levels in the
CC lateral striatum. In rostral brain regions, high expression levels in
CC the dorsal lateral striatum, while in the caudal brain regions, high
CC levels are observed in the ventral lateral striatum (PubMed:2165569,
CC PubMed:10362691, PubMed:10891614, PubMed:16033894). Expressed in
CC monocytes/macrophages (at protein level) (PubMed:23955712). Expressed
CC in striated muscles and in vascular smooth muscles cells (at protein
CC level) (PubMed:10362691, PubMed:26671069).
CC {ECO:0000269|PubMed:10362691, ECO:0000269|PubMed:10891614,
CC ECO:0000269|PubMed:16033894, ECO:0000269|PubMed:2165569,
CC ECO:0000269|PubMed:23955712, ECO:0000269|PubMed:26671069}.
CC -!- PTM: Palmitoylation at Cys-416 is important for recruitment at both
CC plasma membrane and lipid rafts and association with G protein alpha
CC subunits. {ECO:0000269|PubMed:21895628}.
CC -!- MISCELLANEOUS: High-fat diet also increases the hepatic levels of CNR1
CC ligand anandamide, but not that of 2-arachidonoylglycerol.
CC {ECO:0000250|UniProtKB:P47746}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X55812; CAA39332.1; -; mRNA.
DR EMBL; U40395; AAA99067.1; -; mRNA.
DR PIR; A33117; A33117.
DR RefSeq; NP_036916.1; NM_012784.4.
DR RefSeq; XP_006238046.1; XM_006237984.3.
DR RefSeq; XP_017448640.1; XM_017593151.1.
DR AlphaFoldDB; P20272; -.
DR SMR; P20272; -.
DR BioGRID; 247288; 3.
DR IntAct; P20272; 3.
DR MINT; P20272; -.
DR STRING; 10116.ENSRNOP00000010850; -.
DR BindingDB; P20272; -.
DR ChEMBL; CHEMBL3571; -.
DR DrugCentral; P20272; -.
DR GuidetoPHARMACOLOGY; 56; -.
DR GlyGen; P20272; 2 sites.
DR iPTMnet; P20272; -.
DR PhosphoSitePlus; P20272; -.
DR SwissPalm; P20272; -.
DR PaxDb; P20272; -.
DR PRIDE; P20272; -.
DR Ensembl; ENSRNOT00000010850; ENSRNOP00000010850; ENSRNOG00000008223.
DR Ensembl; ENSRNOT00000099728; ENSRNOP00000081243; ENSRNOG00000008223.
DR Ensembl; ENSRNOT00000101534; ENSRNOP00000085179; ENSRNOG00000008223.
DR Ensembl; ENSRNOT00000117169; ENSRNOP00000079932; ENSRNOG00000008223.
DR GeneID; 25248; -.
DR KEGG; rno:25248; -.
DR UCSC; RGD:2369; rat.
DR CTD; 1268; -.
DR RGD; 2369; Cnr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_7_0_1; -.
DR InParanoid; P20272; -.
DR OMA; CMMWAIS; -.
DR OrthoDB; 822074at2759; -.
DR PhylomeDB; P20272; -.
DR TreeFam; TF330052; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P20272; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008223; Expressed in Ammon's horn and 11 other tissues.
DR Genevisible; P20272; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:CACAO.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0004949; F:cannabinoid receptor activity; IMP:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IMP:RGD.
DR GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR GO; GO:0038171; P:cannabinoid signaling pathway; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; IMP:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0007613; P:memory; IDA:RGD.
DR GO; GO:0045759; P:negative regulation of action potential; IMP:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IMP:RGD.
DR GO; GO:0043271; P:negative regulation of ion transport; IDA:RGD.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IDA:RGD.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:RGD.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IMP:CACAO.
DR GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR GO; GO:0031622; P:positive regulation of fever generation; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:RGD.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0060405; P:regulation of penile erection; IMP:RGD.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0042220; P:response to cocaine; IMP:RGD.
DR GO; GO:0045471; P:response to ethanol; IMP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
DR GO; GO:0043278; P:response to morphine; IMP:RGD.
DR GO; GO:0035094; P:response to nicotine; IMP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0098921; P:retrograde trans-synaptic signaling by endocannabinoid; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; ISO:RGD.
DR InterPro; IPR000810; Canbinoid_rcpt_1.
DR InterPro; IPR002230; Cnbnoid_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR22750:SF47; PTHR22750:SF47; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PIRSF; PIRSF037995; Cnoid_rcpt_1; 1.
DR PRINTS; PR00522; CANABINOID1R.
DR PRINTS; PR00362; CANNABINOIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Cannabinoid receptor 1"
FT /id="PRO_0000069318"
FT TOPO_DOM 1..117
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 118..143
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 144..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 156..176
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 177..188
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 189..213
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 214..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 234..256
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 257..274
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 275..300
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 301..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 346..366
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 367..378
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 379..400
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 401..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT REGION 2..23
FT /note="Required for mitochondrial localization"
FT /evidence="ECO:0000250|UniProtKB:P47746"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47746"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47746"
FT LIPID 416
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21895628"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 52845 MW; E59A66AFE17B646C CRC64;
MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDIKGDMASK LGYFPQKFPL TSFRGSPFQE
KMTAGDNSPL VPAGDTTNIT EFYNKSLSSF KENEENIQCG ENFMDMECFM ILNPSQQLAI
AVLSLTLGTF TVLENLLVLC VILHSRSLRC RPSYHFIGSL AVADLLGSVI FVYSFVDFHV
FHRKDSPNVF LFKLGGVTAS FTASVGSLFL TAIDRYISIH RPLAYKRIVT RPKAVVAFCL
MWTIAIVIAV LPLLGWNCKK LQSVCSDIFP LIDETYLMFW IGVTSVLLLF IVYAYMYILW
KAHSHAVRMI QRGTQKSIII HTSEDGKVQV TRPDQARMDI RLAKTLVLIL VVLIICWGPL
LAIMVYDVFG KMNKLIKTVF AFCSMLCLLN STVNPIIYAL RSKDLRHAFR SMFPSCEGTA
QPLDNSMGDS DCLHKHANNT ASMHRAAESC IKSTVKIAKV TMSVSTDTSA EAL
