IGBP1_RAT
ID IGBP1_RAT Reviewed; 340 AA.
AC O08836;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Immunoglobulin-binding protein 1;
DE AltName: Full=Alpha4 phosphoprotein;
DE AltName: Full=CD79a-binding protein 1;
DE AltName: Full=Protein phosphatase 2/4/6 regulatory subunit;
GN Name=Igbp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Noble; TISSUE=T-cell lymphoma;
RX PubMed=9296381; DOI=10.1016/s0303-7207(97)00112-3;
RA Too C.K.;
RT "Differential expression of elongation factor-2, alpha4 phosphoprotein and
RT Cdc5-like protein in prolactin-dependent/independent rat lymphoid cells.";
RL Mol. Cell. Endocrinol. 131:221-232(1997).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Too C.K.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with partially folded PPP2CA, but not with the fully
CC active protein. Interacts with PPP2CB, and with PP4 and PP6. Interacts
CC with MID1 and MID2. Interacts with ubiquitin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The UIM domain is required for protective effect on PP2A.
CC {ECO:0000250}.
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; AF000577; AAD05364.2; -; mRNA.
DR EMBL; BC068202; AAH68202.1; -; mRNA.
DR RefSeq; NP_113812.1; NM_031624.3.
DR AlphaFoldDB; O08836; -.
DR SMR; O08836; -.
DR BioGRID; 248646; 3.
DR STRING; 10116.ENSRNOP00000054708; -.
DR PhosphoSitePlus; O08836; -.
DR jPOST; O08836; -.
DR PaxDb; O08836; -.
DR PRIDE; O08836; -.
DR Ensembl; ENSRNOT00000057900; ENSRNOP00000054708; ENSRNOG00000026267.
DR GeneID; 58845; -.
DR KEGG; rno:58845; -.
DR UCSC; RGD:62011; rat.
DR CTD; 3476; -.
DR RGD; 62011; Igbp1.
DR eggNOG; KOG2830; Eukaryota.
DR GeneTree; ENSGT00390000002414; -.
DR HOGENOM; CLU_041824_1_0_1; -.
DR InParanoid; O08836; -.
DR OMA; RAWDEFT; -.
DR OrthoDB; 1348942at2759; -.
DR PhylomeDB; O08836; -.
DR PRO; PR:O08836; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000026267; Expressed in ovary and 20 other tissues.
DR Genevisible; O08836; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0060632; P:regulation of microtubule-based movement; ISO:RGD.
DR GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; B-cell activation; Chaperone; Cytoplasm; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..340
FT /note="Immunoglobulin-binding protein 1"
FT /id="PRO_0000218620"
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 221..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 281..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"
SQ SEQUENCE 340 AA; 39135 MW; 391487769DE8E554 CRC64;
MAASEEELLL PRLPELFETS KKLLEELEVA TEPTGSRTIQ DKVSKGLELL EKAAGMLSQL
DLFSRNEDLE EIASIDLKYL MVPALQGALT MKQVNPSKRL DHLQRAREHF IHFLTQCHCY
HVAEFQLPQT KNNSAENNTA RSSMAYPNLV AMASQRQAKI ERYKQKKEVE HRLSALKSAV
ESGQADDERV REYYLLHLRR WIGISLEEIE SIDQEIKILK DKDSPREESA CQSSLPEKPP
MKPFILTRNK AQAKVFGTGY PSLATMTVSD WYEQHQKYGA LPDRGIAKPP SADFQRAAQQ
QEDQEQKDEE NEEKALHRMR EWDDWKDTHP RGYGNRQNMG
