Full text data of ARL6IP5
ARL6IP5
(DERP11, JWA, PRA2, PRAF3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
PRA1 family protein 3 (ADP-ribosylation factor-like protein 6-interacting protein 5; ARL-6-interacting protein 5; Aip-5; Cytoskeleton-related vitamin A-responsive protein; Dermal papilla-derived protein 11; GTRAP3-18; Glutamate transporter EAAC1-interacting protein; JM5; Prenylated Rab acceptor protein 2; Protein JWa; Putative MAPK-activating protein PM27)
PRA1 family protein 3 (ADP-ribosylation factor-like protein 6-interacting protein 5; ARL-6-interacting protein 5; Aip-5; Cytoskeleton-related vitamin A-responsive protein; Dermal papilla-derived protein 11; GTRAP3-18; Glutamate transporter EAAC1-interacting protein; JM5; Prenylated Rab acceptor protein 2; Protein JWa; Putative MAPK-activating protein PM27)
hRBCD
IPI00007426
IPI00007426 JWA protein regulates intracellular concentrations of taurine and glutamate JWA protein regulates intracellular concentrations of taurine and glutamate membrane n/a n/a 1 n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00007426 JWA protein regulates intracellular concentrations of taurine and glutamate JWA protein regulates intracellular concentrations of taurine and glutamate membrane n/a n/a 1 n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O75915
ID PRAF3_HUMAN Reviewed; 188 AA.
AC O75915; B2R6V5; Q53ES3; Q5KU08;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 103.
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=Cytoskeleton-related vitamin A-responsive protein;
DE AltName: Full=Dermal papilla-derived protein 11;
DE AltName: Full=GTRAP3-18;
DE AltName: Full=Glutamate transporter EAAC1-interacting protein;
DE AltName: Full=JM5;
DE AltName: Full=Prenylated Rab acceptor protein 2;
DE AltName: Full=Protein JWa;
DE AltName: Full=Putative MAPK-activating protein PM27;
GN Name=ARL6IP5; Synonyms=DERP11, JWA, PRA2, PRAF3; ORFNames=HSPC127;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12438930; 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=15757671; DOI=10.1016/j.febslet.2005.02.037;
RA Schweneker M., Bachmann A.S., Moelling K.;
RT "JM4 is a four-transmembrane protein binding to the CCR5 receptor.";
RL FEBS Lett. 579:1751-1758(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou J.W., Di Y.P., Wu R.;
RT "A novel differentially displayed vitamin A responsive gene that is
RT cytoskeleton related.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X.N., Yu L., Jin L., Hu P.R., Chen S.Y., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to human mRNA for JM4
RT protein.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Jiang C., Huang C., Wu T., Peng Y., Gu Y., Zhang L., Zhang C., Li Y.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Brain;
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 [13]
RP PROTEIN SEQUENCE OF 1-9, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 1-27; 152-158 AND 160-185, ACETYLATION AT MET-1,
RP AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [15]
RP INDUCTION.
RX PubMed=14761432;
RA Mao W.G., Li A.P., Ye J., Huang S., Li A.Q., Zhou J.W.;
RT "Effect of differentiation inducer and heat stress on the expression
RT of JWA protein and Hsp70 of K562 cells.";
RL Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi 21:253-256(2003).
RN [16]
RP NOMENCLATURE.
RX PubMed=16481131; DOI=10.1016/j.gene.2005.12.009;
RA Fo C.S., Coleman C.S., Wallick C.J., Vine A.L., Bachmann A.S.;
RT "Genomic organization, expression profile, and characterization of the
RT new protein PRA1 domain family, member 2 (PRAF2).";
RL Gene 371:154-165(2006).
RN [17]
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.,
RA Buerckstuemmer T., 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 (By similarity).
CC -!- SUBUNIT: Forms multimers. Binds to prenylated RAB1A and RAB3A, to
CC the neuronal glutamate transporter SLC1A1/EAAC1, and to the ADP-
CC ribosylation like factor ARL6, a member of the Ras superfamily.
CC Does not bind to VAMP2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity). Cytoplasm (By similarity).
CC Note=Also exists as a soluble form in the cytoplasm. Associated
CC with microtubules (By similarity).
CC -!- INDUCTION: By methyl-beta-cyclodextrin (By similarity). Up-
CC regulated upon induced differentiation and in heat stress.
CC -!- SIMILARITY: Belongs to the PRA1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97286.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB052638; BAD83603.1; -; mRNA.
DR EMBL; AY102608; AAM28950.1; -; mRNA.
DR EMBL; AB014765; BAC66462.1; -; mRNA.
DR EMBL; AF070523; AAC64360.1; -; mRNA.
DR EMBL; AF115965; AAP97237.1; -; mRNA.
DR EMBL; AF125530; AAF17224.1; -; mRNA.
DR EMBL; AF161476; AAF29091.1; -; mRNA.
DR EMBL; AB097051; BAC77404.1; -; mRNA.
DR EMBL; AK223566; BAD97286.1; ALT_INIT; mRNA.
DR EMBL; AK312731; BAG35602.1; -; mRNA.
DR EMBL; CH471055; EAW65473.1; -; Genomic_DNA.
DR EMBL; BC005143; AAH05143.1; -; mRNA.
DR EMBL; BC020797; AAH20797.1; -; mRNA.
DR RefSeq; NP_006398.1; NM_006407.3.
DR UniGene; Hs.518060; -.
DR UniGene; Hs.745255; -.
DR ProteinModelPortal; O75915; -.
DR IntAct; O75915; 1.
DR MINT; MINT-1339938; -.
DR STRING; 9606.ENSP00000273258; -.
DR PhosphoSite; O75915; -.
DR PaxDb; O75915; -.
DR PeptideAtlas; O75915; -.
DR PRIDE; O75915; -.
DR Ensembl; ENST00000273258; ENSP00000273258; ENSG00000144746.
DR GeneID; 10550; -.
DR KEGG; hsa:10550; -.
DR UCSC; uc003dnr.3; human.
DR CTD; 10550; -.
DR GeneCards; GC03P069216; -.
DR HGNC; HGNC:16937; ARL6IP5.
DR HPA; CAB019321; -.
DR HPA; HPA015540; -.
DR MIM; 605709; gene.
DR neXtProt; NX_O75915; -.
DR PharmGKB; PA134898937; -.
DR eggNOG; NOG272388; -.
DR HOGENOM; HOG000231363; -.
DR HOVERGEN; HBG053661; -.
DR InParanoid; O75915; -.
DR OMA; YPTAFVM; -.
DR PhylomeDB; O75915; -.
DR ChiTaRS; ARL6IP5; human.
DR GeneWiki; ARL6IP5; -.
DR GenomeRNAi; 10550; -.
DR NextBio; 40017; -.
DR PRO; PR:O75915; -.
DR ArrayExpress; O75915; -.
DR Bgee; O75915; -.
DR CleanEx; HS_ARL6IP5; -.
DR Genevestigator; O75915; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015813; P:L-glutamate transport; ISS:UniProtKB.
DR GO; GO:0051051; P:negative regulation of transport; IEA:Ensembl.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 188 PRA1 family protein 3.
FT /FTId=PRO_0000220883.
FT TOPO_DOM 1 35 Cytoplasmic (By similarity).
FT TRANSMEM 36 56 Helical; (Potential).
FT TRANSMEM 57 77 Helical; (Potential).
FT TOPO_DOM 78 93 Cytoplasmic (By similarity).
FT TRANSMEM 94 114 Helical; (Potential).
FT TRANSMEM 115 135 Helical; (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.
FT CONFLICT 28 28 D -> G (in Ref. 10; BAD97286).
SQ SEQUENCE 188 AA; 21615 MW; 3AA708C6D0901B44 CRC64;
MDVNIAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISIVGF
LSPFNMILGG IVVVLVFTGF VWAAHNKDVL RRMKKRYPTT FVMVVMLASY FLISMFGGVM
VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKRT PMGIVLDALE QQEEGINRLT
DYISKVKE
//
ID PRAF3_HUMAN Reviewed; 188 AA.
AC O75915; B2R6V5; Q53ES3; Q5KU08;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 103.
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=Cytoskeleton-related vitamin A-responsive protein;
DE AltName: Full=Dermal papilla-derived protein 11;
DE AltName: Full=GTRAP3-18;
DE AltName: Full=Glutamate transporter EAAC1-interacting protein;
DE AltName: Full=JM5;
DE AltName: Full=Prenylated Rab acceptor protein 2;
DE AltName: Full=Protein JWa;
DE AltName: Full=Putative MAPK-activating protein PM27;
GN Name=ARL6IP5; Synonyms=DERP11, JWA, PRA2, PRAF3; ORFNames=HSPC127;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12438930; 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=15757671; DOI=10.1016/j.febslet.2005.02.037;
RA Schweneker M., Bachmann A.S., Moelling K.;
RT "JM4 is a four-transmembrane protein binding to the CCR5 receptor.";
RL FEBS Lett. 579:1751-1758(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hair follicle dermal papilla;
RA Ikeda A., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou J.W., Di Y.P., Wu R.;
RT "A novel differentially displayed vitamin A responsive gene that is
RT cytoskeleton related.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang X.N., Yu L., Jin L., Hu P.R., Chen S.Y., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to human mRNA for JM4
RT protein.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RA Jiang C., Huang C., Wu T., Peng Y., Gu Y., Zhang L., Zhang C., Li Y.,
RA Han Z., Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in the human adrenal gland.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Brain;
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 [13]
RP PROTEIN SEQUENCE OF 1-9, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 1-27; 152-158 AND 160-185, ACETYLATION AT MET-1,
RP AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [15]
RP INDUCTION.
RX PubMed=14761432;
RA Mao W.G., Li A.P., Ye J., Huang S., Li A.Q., Zhou J.W.;
RT "Effect of differentiation inducer and heat stress on the expression
RT of JWA protein and Hsp70 of K562 cells.";
RL Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi 21:253-256(2003).
RN [16]
RP NOMENCLATURE.
RX PubMed=16481131; DOI=10.1016/j.gene.2005.12.009;
RA Fo C.S., Coleman C.S., Wallick C.J., Vine A.L., Bachmann A.S.;
RT "Genomic organization, expression profile, and characterization of the
RT new protein PRA1 domain family, member 2 (PRAF2).";
RL Gene 371:154-165(2006).
RN [17]
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.,
RA Buerckstuemmer T., 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 (By similarity).
CC -!- SUBUNIT: Forms multimers. Binds to prenylated RAB1A and RAB3A, to
CC the neuronal glutamate transporter SLC1A1/EAAC1, and to the ADP-
CC ribosylation like factor ARL6, a member of the Ras superfamily.
CC Does not bind to VAMP2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity). Cytoplasm (By similarity).
CC Note=Also exists as a soluble form in the cytoplasm. Associated
CC with microtubules (By similarity).
CC -!- INDUCTION: By methyl-beta-cyclodextrin (By similarity). Up-
CC regulated upon induced differentiation and in heat stress.
CC -!- SIMILARITY: Belongs to the PRA1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97286.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB052638; BAD83603.1; -; mRNA.
DR EMBL; AY102608; AAM28950.1; -; mRNA.
DR EMBL; AB014765; BAC66462.1; -; mRNA.
DR EMBL; AF070523; AAC64360.1; -; mRNA.
DR EMBL; AF115965; AAP97237.1; -; mRNA.
DR EMBL; AF125530; AAF17224.1; -; mRNA.
DR EMBL; AF161476; AAF29091.1; -; mRNA.
DR EMBL; AB097051; BAC77404.1; -; mRNA.
DR EMBL; AK223566; BAD97286.1; ALT_INIT; mRNA.
DR EMBL; AK312731; BAG35602.1; -; mRNA.
DR EMBL; CH471055; EAW65473.1; -; Genomic_DNA.
DR EMBL; BC005143; AAH05143.1; -; mRNA.
DR EMBL; BC020797; AAH20797.1; -; mRNA.
DR RefSeq; NP_006398.1; NM_006407.3.
DR UniGene; Hs.518060; -.
DR UniGene; Hs.745255; -.
DR ProteinModelPortal; O75915; -.
DR IntAct; O75915; 1.
DR MINT; MINT-1339938; -.
DR STRING; 9606.ENSP00000273258; -.
DR PhosphoSite; O75915; -.
DR PaxDb; O75915; -.
DR PeptideAtlas; O75915; -.
DR PRIDE; O75915; -.
DR Ensembl; ENST00000273258; ENSP00000273258; ENSG00000144746.
DR GeneID; 10550; -.
DR KEGG; hsa:10550; -.
DR UCSC; uc003dnr.3; human.
DR CTD; 10550; -.
DR GeneCards; GC03P069216; -.
DR HGNC; HGNC:16937; ARL6IP5.
DR HPA; CAB019321; -.
DR HPA; HPA015540; -.
DR MIM; 605709; gene.
DR neXtProt; NX_O75915; -.
DR PharmGKB; PA134898937; -.
DR eggNOG; NOG272388; -.
DR HOGENOM; HOG000231363; -.
DR HOVERGEN; HBG053661; -.
DR InParanoid; O75915; -.
DR OMA; YPTAFVM; -.
DR PhylomeDB; O75915; -.
DR ChiTaRS; ARL6IP5; human.
DR GeneWiki; ARL6IP5; -.
DR GenomeRNAi; 10550; -.
DR NextBio; 40017; -.
DR PRO; PR:O75915; -.
DR ArrayExpress; O75915; -.
DR Bgee; O75915; -.
DR CleanEx; HS_ARL6IP5; -.
DR Genevestigator; O75915; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015813; P:L-glutamate transport; ISS:UniProtKB.
DR GO; GO:0051051; P:negative regulation of transport; IEA:Ensembl.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 188 PRA1 family protein 3.
FT /FTId=PRO_0000220883.
FT TOPO_DOM 1 35 Cytoplasmic (By similarity).
FT TRANSMEM 36 56 Helical; (Potential).
FT TRANSMEM 57 77 Helical; (Potential).
FT TOPO_DOM 78 93 Cytoplasmic (By similarity).
FT TRANSMEM 94 114 Helical; (Potential).
FT TRANSMEM 115 135 Helical; (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.
FT CONFLICT 28 28 D -> G (in Ref. 10; BAD97286).
SQ SEQUENCE 188 AA; 21615 MW; 3AA708C6D0901B44 CRC64;
MDVNIAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISIVGF
LSPFNMILGG IVVVLVFTGF VWAAHNKDVL RRMKKRYPTT FVMVVMLASY FLISMFGGVM
VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKRT PMGIVLDALE QQEEGINRLT
DYISKVKE
//
MIM
605709
*RECORD*
*FIELD* NO
605709
*FIELD* TI
*605709 ADP-RIBOSYLATION-LIKE FACTOR 6-INTERACTING PROTEIN 5; ARL6IP5
;;PRA1 DOMAIN FAMILY, MEMBER 3; PRAF3;;
read moreGLUTAMATE TRANSPORTER EAAC1-ASSOCIATED PROTEIN;;
GTRAP3-18;;
JWA
*FIELD* TX
CLONING
Using the C-terminal intracellular domain of EAAC1 (SLC1A1; 133550) (the
last 87 amino acids) as bait in a yeast 2-hybrid screen of an adult rat
brain cDNA library, Lin et al. (2001) identified a clone, which they
designated E18. They noted that JWA protein, a human differentially
displayed vitamin A-responsive gene, is 95% identical to E18, suggesting
that E18 is a JWA protein homolog of rat. Lin et al. (2001) designated
the deduced 188-amino acid rat protein GTRAP3-18. Like EAAC1, GTRAP3-18
is expressed in numerous tissues. It localizes to the cell membrane and
cytoplasm.
Butchbach et al. (2002) cloned mouse Gtrap3-18 from a cerebral cortex
cDNA library. The deduced 188-amino acid protein is highly basic and has
a number of potential phosphorylation sites, but no apparent
transmembrane domains. Gtrap3-18 shares 95.2% similarity with human
GTRAP3-18 and appeared to be evolutionarily conserved. RT-PCR and EST
database analysis revealed ubiquitous Gtrap3-18 expression in mouse.
Immunohistochemical analysis of mouse brain revealed localization of
Gtrap3-18 predominantly in neuron-rich regions such as stratum
pyramidale of hippocampus and Purkinje cells of the cerebellum. Western
blot analysis showed that Gtrap3-18 formed dimers, trimers, and higher
order multimers, even under reducing conditions.
GENE FUNCTION
Lin et al. (2001) showed that rat GTRAP3-18 specifically interacts with
the carboxy-terminal intracellular domain of EAAC1. Increasing the
expression of GTRAP3-18 in cells reduces EAAC1-mediated glutamate
transport by lowering substrate affinity. The expression of GTRAP3-18
can be upregulated by retinoic acid, which results in a specific
reduction of EAAC1-mediated glutamate transport. Lin et al. (2001)
concluded that glutamate transport proteins can be regulated potently
and that GTRAP can modulate the transport functions ascribed to EAAC1.
GTRAP3-18 may be important in regulating the metabolic function of
EAAC1.
By transfecting HEK293 cells with mouse cDNAs, Butchbach et al. (2002)
showed that Gtrap3-18 inhibited Eaac1-mediated Na(+)-dependent glutamate
transport in a dose-dependent manner.
Huang et al. (2006) found that the expression of JWA was increased in a
time-dependent manner in most myeloid leukemia cell lines induced to
differentiate along different lineages by all-trans retinoic acid and
other chemical inducers. Inhibition of JWA by RNA interference reduced
the degree of differentiation.
GENE STRUCTURE
Butchbach et al. (2002) determined that the ARL6IP5 gene contains 3
exons. This gene structure is highly conserved in mouse and pufferfish.
MAPPING
By genomic sequence analysis, Butchbach et al. (2002) mapped the ARL6IP5
gene to chromosome 3p14. They mapped the mouse Arl6ip5 gene to a region
of chromosome 6D3 that shares homology of synteny with human chromosome
3p14.
*FIELD* RF
1. Butchbach, M. E. R.; Lai, L.; Lin, C. G.: Molecular cloning, gene
structure, expression profile and functional characterization of the
mouse glutamate transporter (EAAT3) interacting protein GTRAP3-18. Gene 292:
81-90, 2002.
2. Huang, S.; Shen, Q.; Mao, W.-G.; Li, A.-P.; Ye, J.; Liu, Q.-Z.;
Zou, C.-P.; Zhou, J.-W.: JWA, a novel signaling molecule, involved
in the induction of differentiation of human myeloid leukemia cells. Biochem.
Biophys. Res. Commun. 341: 440-450, 2006.
3. Lin, C. G.; Orlov, I.; Ruggiero, A. M.; Dykes-Hoberg, M.; Lee,
A.; Jackson, M.; Rothstein, J. D.: Modulation of the neuronal glutamate
transporter EAAC1 by the interacting protein GTRAP3-18. Nature 410:
84-88, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 1/20/2011
*FIELD* CD
Ada Hamosh: 2/28/2001
*FIELD* ED
mgross: 03/29/2011
carol: 1/20/2011
carol: 1/12/2011
alopez: 2/28/2001
*RECORD*
*FIELD* NO
605709
*FIELD* TI
*605709 ADP-RIBOSYLATION-LIKE FACTOR 6-INTERACTING PROTEIN 5; ARL6IP5
;;PRA1 DOMAIN FAMILY, MEMBER 3; PRAF3;;
read moreGLUTAMATE TRANSPORTER EAAC1-ASSOCIATED PROTEIN;;
GTRAP3-18;;
JWA
*FIELD* TX
CLONING
Using the C-terminal intracellular domain of EAAC1 (SLC1A1; 133550) (the
last 87 amino acids) as bait in a yeast 2-hybrid screen of an adult rat
brain cDNA library, Lin et al. (2001) identified a clone, which they
designated E18. They noted that JWA protein, a human differentially
displayed vitamin A-responsive gene, is 95% identical to E18, suggesting
that E18 is a JWA protein homolog of rat. Lin et al. (2001) designated
the deduced 188-amino acid rat protein GTRAP3-18. Like EAAC1, GTRAP3-18
is expressed in numerous tissues. It localizes to the cell membrane and
cytoplasm.
Butchbach et al. (2002) cloned mouse Gtrap3-18 from a cerebral cortex
cDNA library. The deduced 188-amino acid protein is highly basic and has
a number of potential phosphorylation sites, but no apparent
transmembrane domains. Gtrap3-18 shares 95.2% similarity with human
GTRAP3-18 and appeared to be evolutionarily conserved. RT-PCR and EST
database analysis revealed ubiquitous Gtrap3-18 expression in mouse.
Immunohistochemical analysis of mouse brain revealed localization of
Gtrap3-18 predominantly in neuron-rich regions such as stratum
pyramidale of hippocampus and Purkinje cells of the cerebellum. Western
blot analysis showed that Gtrap3-18 formed dimers, trimers, and higher
order multimers, even under reducing conditions.
GENE FUNCTION
Lin et al. (2001) showed that rat GTRAP3-18 specifically interacts with
the carboxy-terminal intracellular domain of EAAC1. Increasing the
expression of GTRAP3-18 in cells reduces EAAC1-mediated glutamate
transport by lowering substrate affinity. The expression of GTRAP3-18
can be upregulated by retinoic acid, which results in a specific
reduction of EAAC1-mediated glutamate transport. Lin et al. (2001)
concluded that glutamate transport proteins can be regulated potently
and that GTRAP can modulate the transport functions ascribed to EAAC1.
GTRAP3-18 may be important in regulating the metabolic function of
EAAC1.
By transfecting HEK293 cells with mouse cDNAs, Butchbach et al. (2002)
showed that Gtrap3-18 inhibited Eaac1-mediated Na(+)-dependent glutamate
transport in a dose-dependent manner.
Huang et al. (2006) found that the expression of JWA was increased in a
time-dependent manner in most myeloid leukemia cell lines induced to
differentiate along different lineages by all-trans retinoic acid and
other chemical inducers. Inhibition of JWA by RNA interference reduced
the degree of differentiation.
GENE STRUCTURE
Butchbach et al. (2002) determined that the ARL6IP5 gene contains 3
exons. This gene structure is highly conserved in mouse and pufferfish.
MAPPING
By genomic sequence analysis, Butchbach et al. (2002) mapped the ARL6IP5
gene to chromosome 3p14. They mapped the mouse Arl6ip5 gene to a region
of chromosome 6D3 that shares homology of synteny with human chromosome
3p14.
*FIELD* RF
1. Butchbach, M. E. R.; Lai, L.; Lin, C. G.: Molecular cloning, gene
structure, expression profile and functional characterization of the
mouse glutamate transporter (EAAT3) interacting protein GTRAP3-18. Gene 292:
81-90, 2002.
2. Huang, S.; Shen, Q.; Mao, W.-G.; Li, A.-P.; Ye, J.; Liu, Q.-Z.;
Zou, C.-P.; Zhou, J.-W.: JWA, a novel signaling molecule, involved
in the induction of differentiation of human myeloid leukemia cells. Biochem.
Biophys. Res. Commun. 341: 440-450, 2006.
3. Lin, C. G.; Orlov, I.; Ruggiero, A. M.; Dykes-Hoberg, M.; Lee,
A.; Jackson, M.; Rothstein, J. D.: Modulation of the neuronal glutamate
transporter EAAC1 by the interacting protein GTRAP3-18. Nature 410:
84-88, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 1/20/2011
*FIELD* CD
Ada Hamosh: 2/28/2001
*FIELD* ED
mgross: 03/29/2011
carol: 1/20/2011
carol: 1/12/2011
alopez: 2/28/2001