IRAG2_MOUSE
ID IRAG2_MOUSE Reviewed; 539 AA.
AC Q60664; Q7TMU8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Inositol 1,4,5-triphosphate receptor associated 2 {ECO:0000305};
DE AltName: Full=Lymphoid-restricted membrane protein;
DE AltName: Full=Protein Jaw1;
DE Contains:
DE RecName: Full=Processed inositol 1,4,5-triphosphate receptor associated 2;
GN Name=Irag2;
GN Synonyms=Jaw1 {ECO:0000303|PubMed:29878215},
GN Lrmp {ECO:0000312|MGI:MGI:108424};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8021504;
RA Behrens T.W., Jagadeesh J., Scherle P., Kearns G., Yewdell J., Staudt L.M.;
RT "Jaw1, a lymphoid-restricted membrane protein localized to the endoplasmic
RT reticulum.";
RL J. Immunol. 153:682-690(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A/J; TISSUE=Lung;
RA Manenti G., Galbiati F., Pettinicchio A., Dragani T.A.;
RT "Complex in vitro allelic effects of mouse Pas1 candidate genes in human
RT lung cancer cell lines.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 [4]
RP MUTAGENESIS OF 480-ALA--VAL-539, SUBCELLULAR LOCATION, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=8798562; DOI=10.1074/jbc.271.38.23528;
RA Behrens T.W., Kearns G.M., Rivard J.J., Bernstein H.D., Yewdell J.W.,
RA Staudt L.M.;
RT "Carboxyl-terminal targeting and novel post-translational processing of
RT JAW1, a lymphoid protein of the endoplasmic reticulum.";
RL J. Biol. Chem. 271:23528-23534(1996).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=9314557; DOI=10.1084/jem.186.7.1087;
RA Snyder H.L., Bacik I., Bennink J.R., Kearns G., Behrens T.W., Baechi T.,
RA Orlowski M., Yewdell J.W.;
RT "Two novel routes of transporter associated with antigen processing (TAP)-
RT independent major histocompatibility complex class I antigen processing.";
RL J. Exp. Med. 186:1087-1098(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP POSSIBLE FUNCTION, INTERACTION WITH ITPR3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20071408; DOI=10.1093/chemse/bjp097;
RA Shindo Y., Kim M.R., Miura H., Yuuki T., Kanda T., Hino A., Kusakabe Y.;
RT "Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-expressing
RT cells.";
RL Chem. Senses 35:171-177(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SUN1 AND SUN2.
RX PubMed=29878215; DOI=10.1093/jb/mvy053;
RA Kozono T., Tadahira K., Okumura W., Itai N., Tamura-Nakano M., Dohi T.,
RA Tonozuka T., Nishikawa A.;
RT "Jaw1/LRMP has a role in maintaining nuclear shape via interaction with SUN
RT proteins.";
RL J. Biochem. 164:303-311(2018).
CC -!- FUNCTION: Plays a role in the delivery of peptides to major
CC histocompatibility complex (MHC) class I molecules; this occurs in a
CC transporter associated with antigen processing (TAP)-independent
CC manner. May play a role in taste signal transduction via ITPR3. May
CC play a role during fertilization in pronucleus congression and fusion
CC (PubMed:9314557). Plays a role in maintaining nuclear shape, maybe as a
CC component of the LINC complex and through interaction with microtubules
CC (PubMed:29878215). {ECO:0000269|PubMed:29878215,
CC ECO:0000269|PubMed:9314557}.
CC -!- SUBUNIT: Interacts (via coiled-coil domain) with ITPR3
CC (PubMed:20071408). Interacts with SUN1 and SUN2 (PubMed:29878215).
CC Interacts with microtubules (PubMed:29878215).
CC {ECO:0000269|PubMed:20071408, ECO:0000269|PubMed:29878215}.
CC -!- SUBCELLULAR LOCATION: [Processed inositol 1,4,5-triphosphate receptor
CC associated 2]: Cytoplasm {ECO:0000269|PubMed:8798562}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20071408}; Single-pass type IV membrane protein
CC {ECO:0000255}. Nucleus envelope {ECO:0000305|PubMed:29878215}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5RHB5}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q5RHB5}. Chromosome
CC {ECO:0000250|UniProtKB:Q5RHB5}. Note=Colocalized with ITPR3 on the
CC endoplasmic reticulum membrane. {ECO:0000269|PubMed:20071408}.
CC -!- TISSUE SPECIFICITY: Spleen and thymus. Expressed at high levels in pre
CC B-cells, mature B-cells and pre T-cells. Expressed at low levels in
CC mature T-cells and plasma B-cells. Expressed in circumvallate (CV),
CC foliate (FL) and fungiform (FF) taste papillae cells of the tongue
CC epithelium. {ECO:0000269|PubMed:20071408, ECO:0000269|PubMed:8021504}.
CC -!- PTM: The removal of the C-terminal lumenal domain occurs by proteolytic
CC processing. {ECO:0000269|PubMed:8798562, ECO:0000269|PubMed:9314557}.
CC -!- SIMILARITY: Belongs to the IRAG2 family. {ECO:0000305}.
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DR EMBL; U10484; AAA21603.1; -; mRNA.
DR EMBL; AY753324; AAV31716.1; -; mRNA.
DR EMBL; BC052909; AAH52909.1; -; mRNA.
DR CCDS; CCDS39704.1; -.
DR PIR; I49065; I49065.
DR RefSeq; NP_001268909.1; NM_001281980.1.
DR AlphaFoldDB; Q60664; -.
DR SMR; Q60664; -.
DR BioGRID; 201200; 3.
DR IntAct; Q60664; 4.
DR STRING; 10090.ENSMUSP00000032396; -.
DR iPTMnet; Q60664; -.
DR PhosphoSitePlus; Q60664; -.
DR EPD; Q60664; -.
DR jPOST; Q60664; -.
DR MaxQB; Q60664; -.
DR PaxDb; Q60664; -.
DR PRIDE; Q60664; -.
DR ProteomicsDB; 292110; -.
DR DNASU; 16970; -.
DR GeneID; 16970; -.
DR KEGG; mmu:16970; -.
DR CTD; 4033; -.
DR MGI; MGI:108424; Lrmp.
DR eggNOG; ENOG502QTH4; Eukaryota.
DR InParanoid; Q60664; -.
DR OrthoDB; 560334at2759; -.
DR PhylomeDB; Q60664; -.
DR BioGRID-ORCS; 16970; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lrmp; mouse.
DR PRO; PR:Q60664; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60664; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR InterPro; IPR008677; MRVI1.
DR PANTHER; PTHR15352; PTHR15352; 1.
DR Pfam; PF05781; MRVI1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Fertilization; Immunity; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..539
FT /note="Inositol 1,4,5-triphosphate receptor associated 2"
FT /id="PRO_0000084484"
FT CHAIN 1..?
FT /note="Processed inositol 1,4,5-triphosphate receptor
FT associated 2"
FT /id="PRO_0000296245"
FT TOPO_DOM 1..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..539
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..326
FT /evidence="ECO:0000255"
FT COMPBIAS 69..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12912"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12912"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12912"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 480..539
FT /note="Missing: Results in cytosolic distribution."
FT /evidence="ECO:0000269|PubMed:8798562"
FT CONFLICT 31
FT /note="D -> G (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..58
FT /note="GHF -> DHL (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> G (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="R -> G (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="G -> V (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="P -> L (in Ref. 3; AAH52909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 59588 MW; 4DA4639632E841F0 CRC64;
MLCVKGPPEQ EPEDGALDVT RGCQCPLPTE DSILGQELLD CTRMNEDQST DENGAGHFYS
ESPSQLREYL TQPSSEQTSS SESTVTSSES GSDILHMASG DLDCKPLCEK EEEARAASAM
QGTSLAPAAY GDYTSVGVAK AASQLEAGEE LRTTENGGKG SAPGETEISM PPKASVKLVN
FQQSENTSAN EKEVEAEFLR LSLGLKCDWF TLEKRVKLEE RSRDLAEENL KKEITNCLKL
LESLTPLCEE DNQAQEIVKK LEKSIVLLSQ CTARVASRAE MLGAINQESR VSRAVEVMIQ
HVENLKRMYA KEHAELEDLK QALLQNDRSF NSLPDEDDCQ IKKRSSSLNS KPSSLRRVTI
ASLPRNLGNV GLVSGMENND RFSRRSSSWR ILGTKQGEHR PSLHRFISTY SWADAEDERS
DVKARDAPEP QGEEAVERTR KPSLSERRSS TLAWDRGTIC SSVASWVTHL QASFRRANRA
LWLTGLIIIL IAALMSFLTG QLFQTAVEAA PTQEGDSWLS LEHILWPFTR LGHDGPPPV
