IGBP1_MOUSE
ID IGBP1_MOUSE Reviewed; 340 AA.
AC Q61249;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Immunoglobulin-binding protein 1;
DE AltName: Full=Alpha4 phosphoprotein;
DE AltName: Full=CD79a-binding protein 1;
DE AltName: Full=Lymphocyte signal transduction molecule alpha 4;
DE AltName: Full=Protein phosphatase 2/4/6 regulatory subunit;
DE AltName: Full=p52;
GN Name=Igbp1; Synonyms=Pc52;
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].
RC STRAIN=NZC; TISSUE=B-cell;
RX PubMed=7876543;
RA Inui S., Kuwahara K., Mizutani J., Maeda K., Kawai T., Nakayasu H.,
RA Sakaguchi N.;
RT "Molecular cloning of a cDNA clone encoding a phosphoprotein component
RT related to the Ig receptor-mediated signal transduction.";
RL J. Immunol. 154:2714-2723(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9573385; DOI=10.1016/s0378-1119(98)00079-1;
RA Maeda K., Inui S., Sanjo H., Sakaguchi N.;
RT "The gene structure and promoter analysis of mouse lymphocyte signal
RT transduction molecule alpha 4 that is related to the yeast TAP42 involved
RT in a rapamycin-sensitive pathway.";
RL Gene 210:287-295(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-223, AND INTERACTION WITH MID1
RP AND PPP2CA.
RX PubMed=21454489; DOI=10.1074/jbc.m111.222414;
RA LeNoue-Newton M., Watkins G.R., Zou P., Germane K.L., McCorvey L.R.,
RA Wadzinski B.E., Spiller B.W.;
RT "The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains
RT of the Alpha4 protein are both required for Alpha4 to inhibit PP2A
RT degradation.";
RL J. Biol. Chem. 286:17665-17671(2011).
CC -!- FUNCTION: Associated to surface IgM-receptor; may be involved in signal
CC transduction. Involved in regulation of the catalytic activity of the
CC phosphatases PP2A, PP4 and PP6 by protecting their partially folded
CC catalytic subunits from degradative polyubiquitination until they
CC associate with regulatory subunits.
CC -!- SUBUNIT: Interacts with PPP2CB, and with PP4 and PP6. Interacts with
CC MID2. Interacts with ubiquitin (By similarity). Interacts with
CC partially folded PPP2CA, but not with the fully active protein.
CC Interacts with MID1. {ECO:0000250, ECO:0000269|PubMed:21454489}.
CC -!- INTERACTION:
CC Q61249; P63330: Ppp2ca; NbExp=2; IntAct=EBI-7002233, EBI-397144;
CC Q61249; P67775: PPP2CA; Xeno; NbExp=3; IntAct=EBI-7002233, EBI-712311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, liver and brain.
CC Ubiquitously expressed in B lineage cell lines.
CC -!- DOMAIN: The UIM domain is required for protective effect on PP2A.
CC -!- PTM: Phosphorylated.
CC -!- PTM: Monoubiquitination by MID1 triggers calpain-mediated cleavage and
CC switches IGBP1 activity from protective to destructive. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IGBP1/TAP42 family. {ECO:0000305}.
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DR EMBL; L31652; AAA67891.1; -; mRNA.
DR EMBL; AJ000633; CAA04190.1; -; Genomic_DNA.
DR EMBL; AJ223156; CAA11135.1; -; Genomic_DNA.
DR EMBL; AJ223157; CAA11135.1; JOINED; Genomic_DNA.
DR EMBL; AJ223158; CAA11135.1; JOINED; Genomic_DNA.
DR EMBL; AJ223159; CAA11135.1; JOINED; Genomic_DNA.
DR EMBL; AJ223160; CAA11135.1; JOINED; Genomic_DNA.
DR EMBL; AJ000634; CAA04191.1; -; Genomic_DNA.
DR CCDS; CCDS30302.1; -.
DR PIR; I49451; I49451.
DR RefSeq; NP_032810.4; NM_008784.3.
DR PDB; 3QC1; X-ray; 2.35 A; A=1-223.
DR PDBsum; 3QC1; -.
DR AlphaFoldDB; Q61249; -.
DR SMR; Q61249; -.
DR BioGRID; 202041; 28.
DR IntAct; Q61249; 5.
DR MINT; Q61249; -.
DR STRING; 10090.ENSMUSP00000033570; -.
DR iPTMnet; Q61249; -.
DR PhosphoSitePlus; Q61249; -.
DR REPRODUCTION-2DPAGE; Q61249; -.
DR EPD; Q61249; -.
DR jPOST; Q61249; -.
DR MaxQB; Q61249; -.
DR PaxDb; Q61249; -.
DR PeptideAtlas; Q61249; -.
DR PRIDE; Q61249; -.
DR ProteomicsDB; 269531; -.
DR DNASU; 18518; -.
DR Ensembl; ENSMUST00000033570; ENSMUSP00000033570; ENSMUSG00000031221.
DR GeneID; 18518; -.
DR KEGG; mmu:18518; -.
DR UCSC; uc009tvz.2; mouse.
DR CTD; 3476; -.
DR MGI; MGI:1346500; Igbp1.
DR VEuPathDB; HostDB:ENSMUSG00000031221; -.
DR eggNOG; KOG2830; Eukaryota.
DR GeneTree; ENSGT00390000002414; -.
DR HOGENOM; CLU_041824_1_0_1; -.
DR InParanoid; Q61249; -.
DR OMA; RAWDEFT; -.
DR OrthoDB; 1348942at2759; -.
DR PhylomeDB; Q61249; -.
DR TreeFam; TF313433; -.
DR BioGRID-ORCS; 18518; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Igbp1; mouse.
DR EvolutionaryTrace; Q61249; -.
DR PRO; PR:Q61249; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61249; protein.
DR Bgee; ENSMUSG00000031221; Expressed in vas deferens and 260 other tissues.
DR Genevisible; Q61249; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IGI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0060632; P:regulation of microtubule-based movement; ISO:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR Gene3D; 1.25.40.540; -; 1.
DR InterPro; IPR038511; TAP42/TAP46-like_sf.
DR InterPro; IPR007304; TAP46-like.
DR PANTHER; PTHR10933; PTHR10933; 1.
DR Pfam; PF04177; TAP42; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; B-cell activation; Chaperone; Cytoplasm;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..340
FT /note="Immunoglobulin-binding protein 1"
FT /id="PRO_0000218619"
FT DOMAIN 47..61
FT /note="UIM"
FT /evidence="ECO:0000305"
FT REGION 99..203
FT /note="Interaction with PPP2CA"
FT /evidence="ECO:0000250"
FT REGION 223..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..291
FT /note="Interaction with MID1"
FT /evidence="ECO:0000250"
FT REGION 291..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 256..257
FT /note="Cleavage; by calpain"
FT /evidence="ECO:0000250"
FT MOD_RES 242
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78318"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 37..60
FT /evidence="ECO:0007829|PDB:3QC1"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3QC1"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3QC1"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 147..181
FT /evidence="ECO:0007829|PDB:3QC1"
FT HELIX 187..219
FT /evidence="ECO:0007829|PDB:3QC1"
SQ SEQUENCE 340 AA; 38971 MW; 9C6BEF7C2E56BAE4 CRC64;
MAASEDELLL PRLPELFETS KKLLEDVEVA TEPTGSRTIQ DKVSKGLELL EKAAGMLSQL
DLFSRNEDLE EIASTDLKYL MVPALQGALT MKQVNPSKRL DHLQRAREHF VHFLTQCHCY
HVAEFQLPQT KTNSAENNTA SSSMAYPNLV AMASQRQAKI ERYKQKKEVE HRLSALKSAV
ESGQADDERV REYHLLHLRR WIAVSLEELE SIDQEIKILK EKDSPREETA CHSSLPEKPP
MKPFILTRNK AQAKVFGTGY PSLATMTVSD WYEQHQKYGV LPDRGIAKPA SADFQRAAQQ
QEDQEQKDEE SEEKALHRMR EWDDWKDTHP RGYGNRQNMG
