PRAF3_RAT
ID PRAF3_RAT Reviewed; 188 AA.
AC Q9ES40; Q9JKD1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=PRA1 family protein 3;
DE AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 5;
DE Short=ARL-6-interacting protein 5;
DE Short=Aip-5;
DE AltName: Full=GTRAP3-18;
DE AltName: Full=Glutamate transporter EAAC1-interacting protein;
DE AltName: Full=Prenylated Rab acceptor protein 2;
DE AltName: Full=Protein JWa;
GN Name=Arl6ip5; Synonyms=Gtrap3-18, Jwa, Pra2, Praf3;
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, INTERACTION WITH RAB1A AND RAB3A,
RP LACK OF INTERACTION WITH VAMP1; VAMP2 AND VAMP3, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 140-ARG--LYS-147;
RP 140-ARG--LYS-151; LYS-185 AND ARG-187.
RC TISSUE=Brain;
RX PubMed=11096102; DOI=10.1074/jbc.m009073200;
RA Abdul-Ghani M., Gougeon P.-Y., Prosser D.C., Da-Silva L.F., Ngsee J.K.;
RT "PRA isoforms are targeted to distinct membrane compartments.";
RL J. Biol. Chem. 276:6225-6233(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SLC1A1, FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11242046; DOI=10.1038/35065084;
RA Lin C.-L.G., Orlov I., Ruggiero A.M., Dykes-Hoberg M., Lee A., Jackson M.,
RA Rothstein J.D.;
RT "Modulation of the neuronal glutamate transporter EAAC1 by the interacting
RT protein GTRAP3-18.";
RL Nature 410:84-88(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Xia W., Ye J., Cao H.X., Chen J.F., Zhang Z.D., Zhao H., Shen Q., Lu H.,
RA Sheng R.L., Wang C.Y., Xu X.K., Wang X.R., Zhou J.W.;
RT "JWA and its role in the regulation of cell differentiation.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RA Li A.Q., Li A.P., Mao W.G., Chen H., Huang S., Qi H., Ye J., Zhang Z.D.,
RA Wang X.R., Sun F., Zou C., Zhou J.W.;
RT "JWA, a novel microtubule-associated protein, regulates homeostasis of
RT intracellular amino acids in PC12 cells.";
RL Chin. Sci. Bull. 48:1828-1834(2003).
RN [6]
RP FUNCTION, INTERACTION WITH RTN2, AND TISSUE SPECIFICITY.
RX PubMed=19720795; DOI=10.2337/db09-0756;
RA Ikemoto T., Hosoya T., Takata K., Aoyama H., Hiramatsu T., Onoe H.,
RA Suzuki M., Endo M.;
RT "Functional role of neuroendocrine-specific protein-like 1 in membrane
RT translocation of GLUT4.";
RL Diabetes 58:2802-2812(2009).
CC -!- FUNCTION: Regulates intracellular concentrations of taurine and
CC glutamate (Ref.5). Negatively modulates SLC1A1/EAAC1 glutamate
CC transport activity by decreasing its affinity for glutamate in a PKC
CC activity-dependent manner (PubMed:11242046). Plays a role in the
CC retention of SLC1A1/EAAC1 in the endoplasmic reticulum
CC (PubMed:19720795). {ECO:0000269|PubMed:11242046,
CC ECO:0000269|PubMed:19720795, ECO:0000269|Ref.5,
CC ECO:0000303|PubMed:11096102}.
CC -!- SUBUNIT: Homodimer. Heterodimer with ARL6IP1 (By similarity). Forms
CC multimers (PubMed:11242046). Interacts with ARL6 (By similarity).
CC Interacts with prenylated RAB1A and RAB3A (PubMed:11096102). Interacts
CC with SLC1A1/EAAC1 (PubMed:11242046). Interacts with RTN2 (via first
CC transmembrane domain) (PubMed:19720795). Does not interact with VAMP1,
CC VAMP2 or VAMP3 (PubMed:11096102). {ECO:0000250|UniProtKB:Q8R5J9,
CC ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:11242046,
CC ECO:0000269|PubMed:19720795}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11096102}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11242046}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:11242046}. Cytoplasm, cytoskeleton
CC {ECO:0000269|Ref.5}. Note=Also exists as a soluble form in the
CC cytoplasm (PubMed:11242046). Associated with microtubules (Ref.5).
CC {ECO:0000269|PubMed:11242046, ECO:0000269|Ref.5}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:11096102). Most abundant in
CC heart and brain (PubMed:11096102). In the embryonic brain cortex,
CC expressed in neurons and astrocytes (PubMed:19720795).
CC {ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:19720795}.
CC -!- INDUCTION: By methyl-beta-cyclodextrin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR EMBL; AF240182; AAG28598.1; -; mRNA.
DR EMBL; AF242391; AAF60354.1; -; mRNA.
DR EMBL; BC061548; AAH61548.1; -; mRNA.
DR RefSeq; NP_076462.1; NM_023972.3.
DR AlphaFoldDB; Q9ES40; -.
DR SMR; Q9ES40; -.
DR BioGRID; 249355; 1.
DR IntAct; Q9ES40; 1.
DR STRING; 10116.ENSRNOP00000010185; -.
DR iPTMnet; Q9ES40; -.
DR PhosphoSitePlus; Q9ES40; -.
DR SwissPalm; Q9ES40; -.
DR jPOST; Q9ES40; -.
DR PaxDb; Q9ES40; -.
DR PRIDE; Q9ES40; -.
DR Ensembl; ENSRNOT00000010185; ENSRNOP00000010185; ENSRNOG00000006818.
DR GeneID; 66028; -.
DR KEGG; rno:66028; -.
DR UCSC; RGD:708572; rat.
DR CTD; 10550; -.
DR RGD; 708572; Arl6ip5.
DR eggNOG; KOG4050; Eukaryota.
DR GeneTree; ENSGT00390000008631; -.
DR HOGENOM; CLU_097683_0_0_1; -.
DR InParanoid; Q9ES40; -.
DR OrthoDB; 1288023at2759; -.
DR PhylomeDB; Q9ES40; -.
DR TreeFam; TF105479; -.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR PRO; PR:Q9ES40; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Genevisible; Q9ES40; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:RGD.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; ISO:RGD.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0002037; P:negative regulation of L-glutamate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0051051; P:negative regulation of transport; IMP:RGD.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; IMP:SynGO.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR PANTHER; PTHR12859; PTHR12859; 1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..188
FT /note="PRA1 family protein 3"
FT /id="PRO_0000220885"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 103..117
FT /note="Required for homodimer formation and heterodimer
FT formation with ARL6IP1"
FT /evidence="ECO:0000250|UniProtKB:Q8R5J9"
FT REGION 136..188
FT /note="Targeting to endoplasmic reticulum membrane"
FT /evidence="ECO:0000269|PubMed:11096102"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75915"
FT MUTAGEN 140..151
FT /note="RLRNLKNKLENK->ELENLENELENE: Partial relocalization
FT to Golgi membranes."
FT /evidence="ECO:0000269|PubMed:11096102"
FT MUTAGEN 140..147
FT /note="RLRNLKNK->ALANLANA: No effect."
FT /evidence="ECO:0000269|PubMed:11096102"
FT MUTAGEN 185
FT /note="K->A: Partial relocalization to Golgi membranes."
FT /evidence="ECO:0000269|PubMed:11096102"
FT MUTAGEN 187
FT /note="R->A: Partial relocalization to Golgi membranes."
FT /evidence="ECO:0000269|PubMed:11096102"
FT CONFLICT 5
FT /note="L -> I (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="N -> D (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="V -> I (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> V (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="I -> V (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> R (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> T (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="K -> Q (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="K -> R (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> V (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..182
FT /note="DSINKFADY -> EGINRLTGC (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="AR -> VK (in Ref. 3; AAF60354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21549 MW; 6FEA29017333C24D CRC64;
MDVNLAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISVVGF
LSPFNMILGG IIVVLVFTGF VWAAHNKDIL RRMKKQYPTA FVMVVMLASY FLISMFGGVM
VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKKT PMGIILDALE QQEDSINKFA
DYISKARE
