ZFN2B_RAT
ID ZFN2B_RAT Reviewed; 257 AA.
AC Q4KLG9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=AN1-type zinc finger protein 2B {ECO:0000305};
DE AltName: Full=Arsenite-inducible RNA-associated protein-like protein {ECO:0000305};
DE Short=AIRAP-like protein {ECO:0000305};
DE Flags: Precursor;
GN Name=Zfand2b {ECO:0000312|RGD:1306260};
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 [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in protein homeostasis by regulating both the
CC translocation and the ubiquitin-mediated proteasomal degradation of
CC nascent proteins at the endoplasmic reticulum. It is involved in the
CC regulation of signal-mediated translocation of proteins into the
CC endoplasmic reticulum. It also plays a role in the ubiquitin-mediated
CC proteasomal degradation of proteins for which signal-mediated
CC translocation to the endoplasmic reticulum has failed. May therefore
CC function in the endoplasmic reticulum stress-induced pre-emptive
CC quality control, a mechanism that selectively attenuates the
CC translocation of newly synthesized proteins into the endoplasmic
CC reticulum and reroutes them to the cytosol for proteasomal degradation.
CC By controlling the steady-state expression of the IGF1R receptor,
CC indirectly regulates the insulin-like growth factor receptor signaling
CC pathway. {ECO:0000250|UniProtKB:Q91X58}.
CC -!- SUBUNIT: Binds 'Lys-48'-linked polyubiquitin chains of ubiquitinated
CC proteins. Associates with the proteasome complex; upon exposure to
CC arsenite. Interacts (via VIM motif) with VCP; the interaction is
CC direct. Interacts with BAG6. Interacts with IGF1R (nascent precursor
CC form). Interacts with DERL1, FAF2, NPLOC4 and UFD1; probably through
CC VCP. {ECO:0000250|UniProtKB:Q91X58}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q91X58}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q91X58}.
CC -!- DOMAIN: The UIM domains specifically bind 'Lys-48'-linked ubiquitin
CC polymers. The UIM domains mediate interaction with polyubiquitinated
CC proteins. {ECO:0000250|UniProtKB:Q91X58}.
CC -!- PTM: Phosphorylated by MAPK14. Phosphorylation has no effect on
CC association with the proteasome complex.
CC {ECO:0000250|UniProtKB:Q91X58}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC099215; AAH99215.1; -; mRNA.
DR RefSeq; NP_001020916.1; NM_001025745.1.
DR AlphaFoldDB; Q4KLG9; -.
DR SMR; Q4KLG9; -.
DR STRING; 10116.ENSRNOP00000025219; -.
DR iPTMnet; Q4KLG9; -.
DR PhosphoSitePlus; Q4KLG9; -.
DR jPOST; Q4KLG9; -.
DR PaxDb; Q4KLG9; -.
DR PRIDE; Q4KLG9; -.
DR Ensembl; ENSRNOT00000025219; ENSRNOP00000025219; ENSRNOG00000018639.
DR GeneID; 363253; -.
DR KEGG; rno:363253; -.
DR UCSC; RGD:1306260; rat.
DR CTD; 130617; -.
DR RGD; 1306260; Zfand2b.
DR eggNOG; KOG3183; Eukaryota.
DR GeneTree; ENSGT00940000159648; -.
DR HOGENOM; CLU_061621_2_0_1; -.
DR InParanoid; Q4KLG9; -.
DR OMA; ETKQSTC; -.
DR OrthoDB; 1422113at2759; -.
DR PhylomeDB; Q4KLG9; -.
DR TreeFam; TF314219; -.
DR PRO; PR:Q4KLG9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018639; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q4KLG9; RN.
DR GO; GO:0031225; C:anchored component of membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0045047; P:protein targeting to ER; ISO:RGD.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; ISO:RGD.
DR Gene3D; 4.10.1110.10; -; 2.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01428; zf-AN1; 2.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00154; ZnF_AN1; 2.
DR SUPFAM; SSF118310; SSF118310; 2.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS51039; ZF_AN1; 2.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..254
FT /note="AN1-type zinc finger protein 2B"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT /id="PRO_0000232878"
FT PROPEP 255..257
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT /id="PRO_0000444337"
FT DOMAIN 197..216
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 221..240
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 4..52
FT /note="AN1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT ZN_FING 94..142
FT /note="AN1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 141..151
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250|UniProtKB:Q8WV99"
FT REGION 153..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..257
FT /note="CAAX motif"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 254
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
FT LIPID 254
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q91X58"
SQ SEQUENCE 257 AA; 27925 MW; D8A7A132511C1357 CRC64;
MEFPDLGAHC SEPSCQRLDF LPLKCDACSG IFCADHVAYA HHHCGSAYQK DIQVPVCPLC
NVPVPVARGE PPDRAVGEHI DRDCRSDPAQ QKRKIFTNKC ERSGCRQREM MKLTCDRCGR
NFCIKHRHPL DHDCSGEGHP TSRAGLAAIS RAQGLASTST VPSPSRTLPS SSSPSRATPQ
LPPRTTSPVI ALQNGLSEDE ALQRALELSL AEAKPQIPSS QEEEDLALAQ ALSASEAEYQ
QQQAQSRSLK PSNCSLC
