IRAG2_DANRE
ID IRAG2_DANRE Reviewed; 1447 AA.
AC Q5RHB5; J9WMP5;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Inositol 1,4,5-triphosphate receptor associated 2;
DE AltName: Full=Lymphoid-restricted membrane protein;
GN Name=irag2; Synonyms=lrmp; ORFNames=si:dkey-172o10.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22542100; DOI=10.1016/j.cub.2012.03.058;
RA Lindeman R.E., Pelegri F.;
RT "Localized products of futile cycle/lrmp promote centrosome-nucleus
RT attachment in the zebrafish zygote.";
RL Curr. Biol. 22:843-851(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION, AND DISEASE.
RX PubMed=12874114; DOI=10.1242/dev.00606;
RA Dekens M.P., Pelegri F.J., Maischein H.M., Nuesslein-Volhard C.;
RT "The maternal-effect gene futile cycle is essential for pronuclear
RT congression and mitotic spindle assembly in the zebrafish zygote.";
RL Development 130:3907-3916(2003).
CC -!- FUNCTION: A maternally expressed membrane and cytoskeletal linker
CC protein, which is essential for attachment of the centrosome to the
CC male pronucleus. Promotes male and female pronucleus congression and
CC subsequent fusion after fertilization. Congression is mediated by the
CC sperm aster microtubules. {ECO:0000269|PubMed:12874114,
CC ECO:0000269|PubMed:22542100}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22542100}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:22542100}. Nucleus envelope
CC {ECO:0000269|PubMed:22542100}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:22542100}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:22542100}. Chromosome
CC {ECO:0000269|PubMed:22542100}. Note=Localized at both male and female
CC pronuclear membranes during pronuclear congression and fusion.
CC Colocalized with tubulin at the centrosome adjacent to the nuclear
CC membrane. At prophase is localized at the centrosome on opposite sides
CC of the zygotic nucleus and at the reforming nuclear membrane. At
CC metaphase is juxtaposed with the centrosomes at the mitotic spindle
CC poles. During chromosome segregation is localized with the chromatin.
CC Undetectable at the centrosome at the onset of anaphase, but becomes
CC again apparent by late mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Lymphoid-restricted membrane protein maternal long
CC form, lrmp+EX36;
CC IsoId=Q5RHB5-1; Sequence=Displayed;
CC Name=2; Synonyms=Lymphoid-restricted membrane protein maternal short
CC form, lrmp-EX36;
CC IsoId=Q5RHB5-2; Sequence=VSP_053666;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and early cleavage stages (at
CC protein level). Maternally expressed. Expressed in early cleavage
CC embryos, weakly at 4 hours post-fertilization (hpf) and undetected at
CC 24 hpf. {ECO:0000269|PubMed:22542100}.
CC -!- DISEASE: Note=Defects in irag2 are a cause of pronuclear
CC congression/fusion and chromosomal segregation abnormalities in the
CC zygote named futile cycle (fue), a lethal recessive maternal-effect
CC mutant. Mutant embryos undergo several cycles of anucleate cleavage and
CC die. {ECO:0000269|PubMed:12874114}.
CC -!- SIMILARITY: Belongs to the IRAG2 family. {ECO:0000305}.
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DR EMBL; JX297440; AFS18272.1; -; mRNA.
DR EMBL; JX297441; AFS18273.1; -; mRNA.
DR EMBL; BX547928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001333212.1; NM_001346283.1. [Q5RHB5-2]
DR RefSeq; NP_001333213.1; NM_001346284.1. [Q5RHB5-1]
DR RefSeq; XP_009298592.1; XM_009300317.2. [Q5RHB5-1]
DR RefSeq; XP_009298593.1; XM_009300318.2. [Q5RHB5-2]
DR AlphaFoldDB; Q5RHB5; -.
DR SMR; Q5RHB5; -.
DR STRING; 7955.ENSDARP00000118448; -.
DR PaxDb; Q5RHB5; -.
DR PRIDE; Q5RHB5; -.
DR Ensembl; ENSDART00000135730; ENSDARP00000118448; ENSDARG00000045574. [Q5RHB5-1]
DR Ensembl; ENSDART00000178686; ENSDARP00000143787; ENSDARG00000045574. [Q5RHB5-2]
DR GeneID; 567234; -.
DR KEGG; dre:567234; -.
DR CTD; 567234; -.
DR ZFIN; ZDB-GENE-041210-152; lrmp.
DR eggNOG; ENOG502QTH4; Eukaryota.
DR GeneTree; ENSGT00530000063722; -.
DR HOGENOM; CLU_004927_0_0_1; -.
DR InParanoid; Q5RHB5; -.
DR PhylomeDB; Q5RHB5; -.
DR TreeFam; TF331789; -.
DR PRO; PR:Q5RHB5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045574; Expressed in mature ovarian follicle and 22 other tissues.
DR ExpressionAtlas; Q5RHB5; baseline and differential.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IMP:UniProtKB.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IDA:UniProtKB.
DR GO; GO:0007344; P:pronuclear fusion; IDA:UniProtKB.
DR GO; GO:0035046; P:pronuclear migration; IDA:UniProtKB.
DR InterPro; IPR028168; KASH5_coiled-coil.
DR InterPro; IPR039508; KASH5_EF-hand-like_dom.
DR InterPro; IPR008677; MRVI1.
DR PANTHER; PTHR15352; PTHR15352; 1.
DR Pfam; PF14658; EF-hand_9; 1.
DR Pfam; PF14662; KASH_CCD; 1.
DR Pfam; PF05781; MRVI1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Fertilization; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1447
FT /note="Inositol 1,4,5-triphosphate receptor associated 2"
FT /id="PRO_0000425286"
FT TOPO_DOM 1..1388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1389..1409
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1410..1447
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 64..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1265
FT /note="Necessary for spindle and spindle pole localization"
FT REGION 1267..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1447
FT /note="Necessary for nuclear membrane localization"
FT COILED 354..518
FT /evidence="ECO:0000255"
FT COILED 665..731
FT /evidence="ECO:0000255"
FT COMPBIAS 69..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1333..1362
FT /note="WNMAAKRPPLKRFVSSGTWADIDEPTLMNS -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:22542100"
FT /id="VSP_053666"
SQ SEQUENCE 1447 AA; 161888 MW; A21A1ADEFD72CF35 CRC64;
MDVGVTPRRH NPVDSICRKL QTIQRRDQEI NSPFQIPKFQ TNSYDSPHSG LRFNLEAILK
KHTVRPDDSD SASSAGMLTP TASPGPGSSC NTPRAPITPV NATYSITSTL GTLGTIGDRR
TSGTYSRPFR RNCSTPSAQT GDNYFNFTPR YSTQSQGPDT DVRTSKIPTP GLFSYNLNFS
SDISNMDSEL AYPALVVKRL SLGEGSLFTS EPKKESMAEV SLICEEDLLD TIFQACDTQC
RGKVYVSHIV DFLRHTTCRS SEDSGLEELC NMLDPERKDI SIDLDTYHAI MKEWIEDCRN
QGKDLKNDTQ QESSKLRDSL SAKRSALLNM TSGSLEAFGG EASRADLETS DLVFCVADLQ
LNNQKLQEEV RKLKQAVENM EDTNQKLIEE NEELKTQAKM GQQLLQKEKM LKEEVEEMKL
SLTSSEESRA QAAAQRKQME RENQSLISKI AALQEENMKV TLEAEELQKK MNDLCDLNAD
LQVQIHSFDA ILADKESLIQ EKNKQMDELK VAVVEYSSVT ELLRADKNKL ESQMQMMQPD
VTIPGLSLSV AYRLNQTSSG SLQTELALAQ NPLEGLEHLS TSVCFASSLD ETLDREVLLL
LQGPTPEQLS LEFKSLISRL KREFKEDGLT FLTAIRSLTE NSETQEANTD LKMQGLEVQL
EQRRTDWIRS LEQLDQYRDS LERELLKMAS NMRRSRTEIL HLSVKVQEQE NQKQQLREEV
DRLKTPLDNR EASSQTPDHL QQVVEELDGP SLEWDEEYVL SESPPLQELG PDQQMLEELC
CDEEVLQALK QEEEEPTETV SDKEKITAKS EGEGEATYDS GVENEEPQRD FTLSHMCLPD
KKSERESNEA PFVGEGGEQR PCMSLKEEDR LPECTGPEDA HEQAAPLPHT HCECAGDQPL
TYDNLEVTSV KDHILSTEPS SLMTCELVSP STGHPEVGNS ITGRTEQLVG TNGEPEEERL
TTGADMSDLQ RLGEGQLSKV SAKSDKSLLL PVAEEEEAMP EAVEVTSAGV NSPDKHKTGS
KKTVVTSDSN STGSADSLKD PSEKVKDMTF DPAASEDNIP TVPATQSPKK DPLASRNKLK
KEMSSMEVIE EQKAQEDGEP TVVTEKEGDT SVSSENASDS TKDDKNSLSP SDKEIEAEFH
RLSLGFKCDM FTLEKRLRLE ERSRDLAEEN VRKEVISCKA LLQALIPRCE EDNQSMEIIH
RVQKNLEILV QSMTRVSSRS EMLGAIHQET RVGKTVEVMI QHVENLRRMY TKEHAELLEL
RENLTPNERS FGSHSERDDF RNKKQTTSNI FKTTSRRISI ATIPRSIGGQ THFDMPKDMA
ETEVERLSRR SPWNMAAKRP PLKRFVSSGT WADIDEPTLM NSPTPSPTDN APPSLMEGRP
AVSRGARGIW IWVALFVVLA VLLALLASLM LQPAVDAAPV GTGDSWMTIQ QLLWPYTGLR
HNGQPPV
