ID PRAF3_MOUSE Reviewed; 188 AA. AC Q8R5J9; Q8C2Q1; Q9D838; Q9DB37; Q9WUG9; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 01-MAY-2007, entry version 32. DE PRA1 family protein 3 (ARL-6-interacting protein 5) (ADP-ribosylation- DE like factor 6-interacting protein 5) (Aip-5) (Glutamate transporter DE EAAC1-interacting protein) (GTRAP3-18) (Prenylated Rab acceptor DE protein 2) (Protein JWa) (Addicsin). GN Name=Arl6ip5; Synonyms=Aip5, Jwa, Pra2, Praf3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SLC1A1, AND RP TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Brain; RX MEDLINE=22114969; PubMed=12119102; DOI=10.1016/S0378-1119(02)00669-8; RA Butchbach M.E.R., Lai L., Lin C.-L.G.; RT "Molecular cloning, gene structure, expression profile and functional RT characterization of the mouse glutamate transporter (EAAT3) RT interacting protein GTRAP3-18."; RL Gene 292:81-90(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND RP TISSUE SPECIFICITY. RC TISSUE=Amygdala; RX MEDLINE=22327011; PubMed=12438930; RX DOI=10.1097/00001756-200211150-00018; RA Ikemoto M.J., Inoue K., Akiduki S., Osugi T., Imamura T., Ishida N., RA Ohtomi M.; RT "Identification of addicsin/GTRAP3-18 as a chronic morphine-augumented RT gene in amygdala."; RL NeuroReport 13:2079-2084(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; RA Xia W., Cao H.X., Zhou J.W.; RT "JWa and its biological evolution."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Cerebellum, Head, Small intestine, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-118, AND INTERACTION WITH ARL6. RX MEDLINE=99439712; PubMed=10508919; DOI=10.1016/S0014-5793(99)01188-6; RA Ingley E., Williams J.H., Walker C.E., Tsai S., Colley S., Sayer M.S., RA Tilbrook P.A., Sarna M., Beaumont J.G., Klinken S.P.; RT "A novel ADP-ribosylation like factor (ARL-6), interacts with the RT protein-conducting channel SEC61beta subunit."; RL FEBS Lett. 459:69-74(1999). RN [7] RP CHARACTERIZATION. RX PubMed=12562531; DOI=10.1046/j.1471-4159.2003.01588.x; RA Butchbach M.E.R., Guo H., Lin C.-L.G.; RT "Methyl-beta-cyclodextrin but not retinoic acid reduces EAAT3-mediated RT glutamate uptake and increases GTRAP3-18 expression."; RL J. Neurochem. 84:891-894(2003). CC -!- FUNCTION: Regulates intracellular concentrations of taurine and CC glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport CC activity by decreasing its affinity for glutamate. May be involved CC in membrane traffic. CC -!- SUBUNIT: Binds to prenylated RAB1A and RAB3A, and to the neuronal CC glutamate transporter SLC1A1/EAAC1. Does not bind to VAMP2 (By CC similarity). Forms multimers. Binds to the ADP-ribosylation like CC factor ARL6, a member of the Ras superfamily. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum CC membrane; multi-pass membrane protein. Cytoplasm. Note=Also exists CC as a soluble form in the cytoplasm. Associated with microtubules. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: By methyl-beta-cyclodextrin. Up-regulated upon chronic CC morphine injection, in amygdala only, other brain regions remain CC unaffected. CC -!- MISCELLANEOUS: Induction by morphine may affect glutamate uptake CC in the amygdala, causing mice to develop morphine tolerance and CC dependence. CC -!- SIMILARITY: Belongs to the PRA1 family. CC -!- CAUTION: Was originally (Ref.7) reported to be induced by retinoic CC acid. CC -!- CAUTION: Ref.6 (AAD33050) sequence differs from that shown due to CC a wrong choice of frame. CC -!- CAUTION: Ref.6 (AAD33050) sequence differs from that shown due to CC frameshifts in positions 94 and 108. 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; AF421860; AAL77876.1; -; mRNA. DR EMBL; D87211; BAC24103.1; -; mRNA. DR EMBL; AF265214; AAL74056.1; -; mRNA. DR EMBL; AK005259; BAB23912.1; -; mRNA. DR EMBL; AK008519; BAB25717.1; -; mRNA. DR EMBL; AK088205; BAC40209.1; -; mRNA. DR EMBL; AK076519; BAC36376.1; -; mRNA. DR EMBL; BC003897; AAH03897.1; -; mRNA. DR EMBL; AF133912; AAD33050.1; ALT_SEQ; mRNA. DR UniGene; Mm.291014; -. DR Ensembl; ENSMUSG00000035199; Mus musculus. DR MGI; MGI:1929501; Arl6ip5. DR ArrayExpress; Q8R5J9; -. DR GermOnline; ENSMUSG00000035199; Mus musculus. DR RZPD-ProtExp; IOM15333; -. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0015813; P:glutamate transport; IDA:MGI. DR InterPro; IPR004895; Prenylated_rab_accept_PRA1. DR Pfam; PF03208; PRA1; 1. KW Acetylation; Endoplasmic reticulum; Membrane; Transmembrane. FT CHAIN 1 188 PRA1 family protein 3. FT /FTId=PRO_0000220884. FT TOPO_DOM 1 39 Cytoplasmic (By similarity). FT TRANSMEM 40 60 Potential. FT TRANSMEM 64 84 Potential. FT TOPO_DOM 85 92 Cytoplasmic (By similarity). FT TRANSMEM 93 113 Potential. FT TRANSMEM 115 135 Potential. FT TOPO_DOM 136 188 Cytoplasmic (By similarity). FT REGION 136 188 Targeting to endoplasmic reticulum FT membrane (By similarity). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT CONFLICT 11 11 W -> R (in Ref. 4; BAC40209). FT CONFLICT 14 14 F -> S (in Ref. 4; BAC40209). FT CONFLICT 19 19 Missing (in Ref. 6). FT CONFLICT 86 86 Missing (in Ref. 6). FT CONFLICT 103 103 M -> T (in Ref. 4; BAB25717). FT CONFLICT 117 117 G -> R (in Ref. 6). FT CONFLICT 140 140 R -> K (in Ref. 4; BAB25717). FT CONFLICT 163 163 G -> V (in Ref. 1). FT CONFLICT 178 178 K -> E (in Ref. 4; BAC40209). SQ SEQUENCE 188 AA; 21558 MW; 5A679FC5071319F0 CRC64; MDVNLAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISVVGF LSPFNMILGG VIVVLVFMGF VWAAHNKDIL RRMKKQYPTA FVMVVMLASY FLISMFGGVM VFVFGITLPL LLMFIHASLR LRNLKNKLEN KMEGIGLKKT PMGIILDALE QQEDNINKFA DYISKARE //