APBP2_RAT
ID APBP2_RAT Reviewed; 585 AA.
AC A5HK05; Q5BJX9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Amyloid protein-binding protein 2 {ECO:0000305};
DE AltName: Full=Amyloid beta precursor protein-binding protein 2 {ECO:0000250|UniProtKB:Q92624};
DE Short=APP-BP2 {ECO:0000250|UniProtKB:Q92624};
GN Name=Appbp2 {ECO:0000312|RGD:1306488};
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].
RA Scholze P., Armsen W., Eulenburg V., Horiuchi M., Zeitelhofer M.,
RA Tuebing F., Dahm R., Betz H.;
RT "The neuronal glycine transporter GlyT2 interacts with subunits of
RT microtubule-dependent motor proteins.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-585.
RC TISSUE=Ovary;
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: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation. The C-degron recognized by the DesCEND pathway is usually
CC a motif of less than ten residues and can be present in full-length
CC proteins, truncated proteins or proteolytically cleaved forms. The
CC CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-
CC Xaa-Gly degron at the C-terminus, leading to their ubiquitination and
CC degradation. The CRL2(APPBP2) complex mediates ubiquitination and
CC degradation of truncated SELENOV selenoproteins produced by failed
CC UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron. May play a
CC role in intracellular protein transport: may be involved in the
CC translocation of APP along microtubules toward the cell surface.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- ACTIVITY REGULATION: E3 ubiquitin-protein ligase activity of the
CC CRL2(APPBP2) complex is inhibited by APP.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC APPBP2. Interacts with APP; APP interaction inhibits the E3 ubiquitin-
CC protein ligase activity of the CRL2(APPBP2) complex.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92624}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92624}. Membrane
CC {ECO:0000250|UniProtKB:Q92624}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q92624}. Note=Associated with membranes and
CC microtubules. {ECO:0000250|UniProtKB:Q92624}.
CC -!- PTM: Rapidly degraded by the proteasome upon overexpression of a C-
CC terminal fragment of APP. {ECO:0000250|UniProtKB:Q92624}.
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DR EMBL; EF535262; ABQ00241.1; -; mRNA.
DR EMBL; BC091285; AAH91285.1; -; mRNA.
DR RefSeq; NP_001094439.1; NM_001100969.1.
DR AlphaFoldDB; A5HK05; -.
DR SMR; A5HK05; -.
DR STRING; 10116.ENSRNOP00000032753; -.
DR iPTMnet; A5HK05; -.
DR PhosphoSitePlus; A5HK05; -.
DR PaxDb; A5HK05; -.
DR Ensembl; ENSRNOT00000033684; ENSRNOP00000032753; ENSRNOG00000027654.
DR GeneID; 303396; -.
DR KEGG; rno:303396; -.
DR CTD; 10513; -.
DR RGD; 1306488; Appbp2.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00390000010722; -.
DR HOGENOM; CLU_019378_1_0_1; -.
DR InParanoid; A5HK05; -.
DR OMA; YAESSHC; -.
DR OrthoDB; 578212at2759; -.
DR PhylomeDB; A5HK05; -.
DR TreeFam; TF314010; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A5HK05; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000027654; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; A5HK05; baseline and differential.
DR Genevisible; A5HK05; RN.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR042476; APPBP2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46575; PTHR46575; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Membrane; Microtubule; Nucleus; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport; Ubl conjugation pathway.
FT CHAIN 1..585
FT /note="Amyloid protein-binding protein 2"
FT /id="PRO_0000296299"
FT REPEAT 50..83
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 120..153
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 206..239
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 288..321
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 333..367
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 429..462
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 471..505
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 514..547
FT /note="TPR 8"
FT /evidence="ECO:0000255"
SQ SEQUENCE 585 AA; 66902 MW; 8C8985EAF844CB62 CRC64;
MAAVELEWIP ETLYNTAISA VVDNYIRSRR DIRSLPENIQ FDVYYKLYQQ GRLCQLGSEF
CELEVFAKVL RALDKRHLLH HCFQALMDHG VKVASVLAYS FSRRCSYIAE SDAAVKEKAI
QVGFVLGGFL SDAGWYSDAE KVFLSCLQLC TLHDEMLHWF RAVECCVRLL HVRNGNCKYH
LGEETFKLAQ TYMDKLSKHG QQANRAALYG ELCALLFAKS HYDEAYKWCV EAMKEITSGL
PVKVVVDVLR QASKACVVKR EFKKAEQLIK HAVYLARDHF GSKHPKYSDT LLDYGFYLLN
VDNICQSVAI YQAALDIRQS VFGGKNIHVA TAHEDLAYSS YVHQYSSGKF DNALFHAERA
IGIITHILPE DHLLLASSKR VKALILEEIA IDCHNKETEQ RLLQEAHDLH LSSLQLAKKA
FGEFNVQTAK HYGNLGRLYQ SMRKFKEAEE MHIKAIQIKE QLLGQEDYEV ALSVGHLASL
YNYDMNQYEN AEKLYLRSIA IGKKLFGEGY SGLEYDYRGL IKLYNSTGNY EKVFEYHNVL
SNWNRLRDRQ YSVTDALEDV NSSPQSTEEV VQSFLMSQNV EGPSC
