NBR1_PONAB
ID NBR1_PONAB Reviewed; 894 AA.
AC Q5RC94;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Next to BRCA1 gene 1 protein;
DE AltName: Full=Neighbor of BRCA1 gene 1 protein;
GN Name=NBR1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts probably as a receptor for selective autophagosomal
CC degradation of ubiquitinated targets. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SQSTM1,
CC titin/TTN, TRIM55, RNF29, USP8, SQSTM1, MAP1LC3A, MAP1LC3B, MAP1LC3C,
CC GABARAP, GABARAPL1 and GABARAPL2. Binds to ubiquitin and ubiquitinated
CC proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14596}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q14596}.
CC Lysosome {ECO:0000250|UniProtKB:Q14596}. Cytoplasm, myofibril,
CC sarcomere, M line {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac
CC muscles localizes to the sarcomeric M line (By similarity). Is targeted
CC to lysosomes for degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q14596, ECO:0000250|UniProtKB:Q501R9}.
CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1. {ECO:0000250}.
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DR EMBL; CR858386; CAH90613.1; -; mRNA.
DR RefSeq; NP_001127309.1; NM_001133837.1.
DR AlphaFoldDB; Q5RC94; -.
DR BMRB; Q5RC94; -.
DR SMR; Q5RC94; -.
DR STRING; 9601.ENSPPYP00000009400; -.
DR Ensembl; ENSPPYT00000057934; ENSPPYP00000043413; ENSPPYG00000008362.
DR GeneID; 100174370; -.
DR KEGG; pon:100174370; -.
DR CTD; 4077; -.
DR eggNOG; KOG4351; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00390000016335; -.
DR InParanoid; Q5RC94; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IEA:InterPro.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR CDD; cd14947; NBR1_like; 1.
DR CDD; cd06396; PB1_NBR1; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032350; N_BRCA1_central.
DR InterPro; IPR033513; NBR1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034852; PB1_NBR1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR20930:SF2; PTHR20930:SF2; 2.
DR Pfam; PF16158; N_BRCA1_IG; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Lysosome; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..894
FT /note="Next to BRCA1 gene 1 protein"
FT /id="PRO_0000096748"
FT DOMAIN 4..85
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 841..885
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 212..264
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 472..566
FT /note="ATG8 family proteins-binding"
FT /evidence="ECO:0000250"
FT REGION 630..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..666
FT /note="ATG8 family proteins-binding"
FT /evidence="ECO:0000250"
FT REGION 678..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..647
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14596"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501R9"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501R9"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14596"
SQ SEQUENCE 894 AA; 98943 MW; 79E91CF8925E5A68 CRC64;
MEPQVTLNVT FKNEIQSFLV SDPENTTWAD IEAMVKVSFD LNTIQIKYLD EENEEVSINS
QGEYEEALKM AVKQGNQLQM QVHEGHHVVD EAPPPVVGAK RLAARAGKKP LAHYSSLVRV
LGSDMKTPED SAVQSFPLAT CDTDQPQDKP PDWFTSYLET FREQVVKETV EKLEQKLHEK
LVLQNPSLGS CPSEVSMPTS EETLFLPENQ FSWHIACNNC QRRIVGVRYQ CSLCPSYNIC
EDCEAGPYGH DTNHVLLKLR RPVVGSSEPF CHSKYSTPRL PAALEQVRLP LQPCTPVMPT
LSAAFVDENL PDGTHLQPGT KFIKHWRMKN TGNVKWSADT KLKFMWGNLT LASTEKKDVL
VPCLKAGHVG VVSVEFIAPA LEGTYTSHWR LSHKGQQFGP RVWCSIIVDP FPSEESPDNI
EKGMISSSKT DDLTCQQEET FLLAKEERQL GEVTEQTEGT AACIPQKAKN VASERELYIP
SVDLLTAQDL LSFELLDINI VQELERVPHN TPVDMTPCMS PLPHDSPLIE KPGLGQIQEE
NEGAGFKALP DSMVSVKRKA ENIASVEEAE EDLSGTQFVC ETVIRSLTLD AAPDHNPPCR
QKSLQMKFAL PEEGPLGNER EEIVHIAEEE AVMEEEEDEE EEDELKDEVQ SQSSASSEDY
IIILPECFDT SRPLGDSMYS SALSQPGLER GAEGEPGVEA GQEPAEAGER LPGGENQPQE
HSISDIFTTS QTLETVPLIP EVVELPPPLP RSSPCVHHHG SPGVDLPVTI PEVSSVPDQI
RGEPRGSSGL VNSRQKSYDH SRHHHGSSIA GGLVKGALSV AASAYKALFA GPPVTAQPIV
SEDQTAALMA HLFEMGFCDR QLNLQLLKKH NYNILQVVTE LLQLNNNDWY SQRY
