AR6P1_MOUSE
ID AR6P1_MOUSE Reviewed; 203 AA.
AC Q9JKW0; Q9JLI9; Q9WUG3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ADP-ribosylation factor-like protein 6-interacting protein 1;
DE Short=ARL-6-interacting protein 1;
DE Short=Aip-1;
DE AltName: Full=Protein TBX2;
GN Name=Arl6ip1; Synonyms=Arl6ip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ARL6.
RX 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 protein-
RT conducting channel SEC61beta subunit.";
RL FEBS Lett. 459:69-74(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Xie L.P., Chen W.F.;
RT "A novel gene cloned from mouse thymic stromal cell line.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10995579; DOI=10.1006/geno.2000.6278;
RA Pettersson M., Bessonova M., Gu H.F., Groop L.C., Jonsson J.I.;
RT "Characterization, chromosomal localization, and expression during
RT hematopoietic differentiation of the gene encoding Arl6ip, ADP-
RT ribosylation-like factor-6 interacting protein (ARL6).";
RL Genomics 68:351-354(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-59, FUNCTION, INTERACTION WITH ARL6IP5,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18684713; DOI=10.1074/jbc.m801570200;
RA Akiduki S., Ikemoto M.J.;
RT "Modulation of the neural glutamate transporter EAAC1 by the addicsin-
RT interacting protein ARL6IP1.";
RL J. Biol. Chem. 283:31323-31332(2008).
CC -!- FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate
CC transport by increasing its affinity for glutamate in a PKC activity-
CC dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1
CC probably by reducing its interaction with ARL6IP5, a negative regulator
CC of SLC1A1/EAAC1-mediated glutamate transport (PubMed:18684713). Plays a
CC role in the formation and stabilization of endoplasmic reticulum
CC tubules. Negatively regulates apoptosis, possibly by modulating the
CC activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent
CC substrates and downstream markers of apoptosis but not CASP9 itself.
CC May be involved in protein transport, membrane trafficking, or cell
CC signaling during hematopoietic maturation (By similarity).
CC {ECO:0000250|UniProtKB:Q15041, ECO:0000269|PubMed:18684713}.
CC -!- SUBUNIT: Homooligomer (By similarity). Heterodimer with ARL6IP5
CC (PubMed:18684713). Interacts with ARL6 (PubMed:10508919). Interacts
CC with TMEM33. Interacts with ATL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q15041, ECO:0000269|PubMed:10508919,
CC ECO:0000269|PubMed:18684713}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q15041}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15041}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:18684713}.
CC Note=Predominantly localized to intracytoplasmic membranes.
CC Preferentially localizes at the ER tubules and the edge of the ER
CC sheets, both of which are characterized by a high membrane curvature.
CC {ECO:0000250|UniProtKB:Q15041}.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex, cerebellum,
CC hippocampus, olfactory bulbs, medulla oblongate and limbic system (at
CC protein level). Ubiquitous (PubMed:18684713). Expressed in all
CC hematopoietic cell lineages, with highest levels in early myeloid
CC progenitor cells. {ECO:0000269|PubMed:10995579,
CC ECO:0000269|PubMed:18684713}.
CC -!- DOMAIN: The transmembrane domains are required for its ability to shape
CC the endoplasmic reticulum membrane into tubules.
CC {ECO:0000250|UniProtKB:Q15041}.
CC -!- SIMILARITY: Belongs to the ARL6ip family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD33046.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF27313.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF133669; AAD33046.1; ALT_FRAME; mRNA.
DR EMBL; AF172088; AAF27313.1; ALT_INIT; mRNA.
DR EMBL; AF223953; AAF34706.1; -; mRNA.
DR EMBL; BC010196; AAH10196.1; -; mRNA.
DR CCDS; CCDS21769.1; -.
DR RefSeq; NP_062292.1; NM_019419.2.
DR AlphaFoldDB; Q9JKW0; -.
DR BioGRID; 207603; 4.
DR STRING; 10090.ENSMUSP00000032888; -.
DR iPTMnet; Q9JKW0; -.
DR PhosphoSitePlus; Q9JKW0; -.
DR SwissPalm; Q9JKW0; -.
DR EPD; Q9JKW0; -.
DR jPOST; Q9JKW0; -.
DR MaxQB; Q9JKW0; -.
DR PaxDb; Q9JKW0; -.
DR PRIDE; Q9JKW0; -.
DR ProteomicsDB; 283251; -.
DR Antibodypedia; 11964; 286 antibodies from 31 providers.
DR DNASU; 54208; -.
DR Ensembl; ENSMUST00000032888; ENSMUSP00000032888; ENSMUSG00000030654.
DR GeneID; 54208; -.
DR KEGG; mmu:54208; -.
DR UCSC; uc009jjo.2; mouse.
DR CTD; 23204; -.
DR MGI; MGI:1858943; Arl6ip1.
DR VEuPathDB; HostDB:ENSMUSG00000030654; -.
DR eggNOG; ENOG502QTTI; Eukaryota.
DR GeneTree; ENSGT00940000154937; -.
DR HOGENOM; CLU_100749_0_0_1; -.
DR InParanoid; Q9JKW0; -.
DR OMA; VWYEYLF; -.
DR OrthoDB; 1268983at2759; -.
DR PhylomeDB; Q9JKW0; -.
DR TreeFam; TF105477; -.
DR BioGRID-ORCS; 54208; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Arl6ip1; mouse.
DR PRO; PR:Q9JKW0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JKW0; protein.
DR Bgee; ENSMUSG00000030654; Expressed in pigmented layer of retina and 259 other tissues.
DR ExpressionAtlas; Q9JKW0; baseline and differential.
DR Genevisible; Q9JKW0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005784; C:Sec61 translocon complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; IDA:MGI.
DR GO; GO:0071787; P:endoplasmic reticulum tubular network formation; ISS:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0002038; P:positive regulation of L-glutamate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:1903371; P:regulation of endoplasmic reticulum tubular network organization; ISO:MGI.
DR InterPro; IPR033301; ARL6IP.
DR PANTHER; PTHR20952:SF3; PTHR20952:SF3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..203
FT /note="ADP-ribosylation factor-like protein 6-interacting
FT protein 1"
FT /id="PRO_0000064656"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..65
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 203 AA; 23437 MW; 34D10BE315F7B669 CRC64;
MAEGDNRSSN LLAVETASLE EQLQGWGEVM LMADKVLRWE RAWFPPAIMG VVSLLFLIIY
YLDPSVLSGV SCFVMFLCLA DYLVPILAPR IFGSNKWTTE QQQRFHEICS NLVKTRRRAV
GWWKRLFSLK EEKPKMYFMT MIISLAAVAW VGQQVHNLLL TYLIVTFVLL LPGLNQHGII
LKYIGMAKRE INKLLKQKEK KNE
