PZR3B_DANRE
ID PZR3B_DANRE Reviewed; 1053 AA.
AC E7FDW2; K9K836;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase PDZRN3-B {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q69ZS0};
DE AltName: Full=PDZ domain-containing RING finger protein 3-B {ECO:0000305};
GN Name=pdzrn3b {ECO:0000312|ZFIN:ZDB-GENE-071022-4};
GN Synonyms=pdzrn3 {ECO:0000303|PubMed:22252497};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:AEN28595.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=22252497; DOI=10.1387/ijdb.113437ld;
RA Dente L., Gestri G., Tsang M., Kudoh T., Wilson S.W., Dawid I.B.,
RA Andreazzoli M.;
RT "Cloning and developmental expression of zebrafish pdzrn3.";
RL Int. J. Dev. Biol. 55:989-993(2011).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000305}
RP INTERACTION WITH KIDINS220B, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22609016; DOI=10.1016/j.biochi.2012.05.002;
RA Andreazzoli M., Gestri G., Landi E., D'Orsi B., Barilari M., Iervolino A.,
RA Vitiello M., Wilson S.W., Dente L.;
RT "Kidins220/ARMS interacts with Pdzrn3, a protein containing multiple
RT binding domains.";
RL Biochimie 94:2054-2057(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000250|UniProtKB:Q69ZS0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q69ZS0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q69ZS0}.
CC -!- SUBUNIT: Interacts (via PDZ domain 1) with kidins220b (via PDZ-binding
CC motif). {ECO:0000269|PubMed:22609016}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q69ZS0}. Cytoplasm
CC {ECO:0000269|PubMed:22609016}. Note=Localizes to the postsynaptic
CC region of neuromuscular junctions. {ECO:0000250|UniProtKB:Q69ZS0}.
CC -!- DEVELOPMENTAL STAGE: Detected in the presumptive hindbrain and
CC notochord from the 3-somite stage onwards (PubMed:22252497). Expression
CC in notochord becomes restricted to the posterior as development
CC proceeds (PubMed:22252497, PubMed:22609016). Shows particularly strong
CC expression at the hindbrain-rhombomere 1 boundary during the 12-18
CC somite stages (PubMed:22252497, PubMed:22609016). Expressed in ventral
CC spinal cord neurons and ventral somite cells at 24 hours post-
CC fertilization (hpf) (PubMed:22252497). Becomes restricted to trunk-tail
CC motor neurons at 32 hpf (PubMed:22252497, PubMed:22609016). Detected in
CC eye primordia from the 10-somite stage onwards (PubMed:22252497). At 24
CC hpf, expression in eye is found in the ventral retina and optic stalk,
CC and also weakly in dorsal retina (PubMed:22252497). Expressed in the
CC eye choroid fissure and ganglion cells at 32 hpf (PubMed:22252497,
CC PubMed:22609016). Also found in thalamus, posterior tuberculum, head
CC mesenchyme, pectoral fins and pronephric duct at 32 hpf
CC (PubMed:22252497). {ECO:0000269|PubMed:22252497,
CC ECO:0000269|PubMed:22609016}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250|UniProtKB:Q69ZS0}.
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DR EMBL; JN108761; AEN28595.1; -; mRNA.
DR EMBL; BX000434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR847862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001243321.1; NM_001256392.1.
DR AlphaFoldDB; E7FDW2; -.
DR SMR; E7FDW2; -.
DR STRING; 7955.ENSDARP00000101938; -.
DR PaxDb; E7FDW2; -.
DR PeptideAtlas; E7FDW2; -.
DR Ensembl; ENSDART00000114330; ENSDARP00000101938; ENSDARG00000073869.
DR GeneID; 100005518; -.
DR KEGG; dre:100005518; -.
DR CTD; 100005518; -.
DR ZFIN; ZDB-GENE-071022-4; pdzrn3b.
DR eggNOG; KOG0297; Eukaryota.
DR eggNOG; KOG0312; Eukaryota.
DR GeneTree; ENSGT00950000183062; -.
DR HOGENOM; CLU_011096_0_0_1; -.
DR InParanoid; E7FDW2; -.
DR OMA; HAGCGQL; -.
DR OrthoDB; 631580at2759; -.
DR PhylomeDB; E7FDW2; -.
DR TreeFam; TF315909; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:E7FDW2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000073869; Expressed in heart and 48 other tissues.
DR ExpressionAtlas; E7FDW2; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Repeat; Synapse;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1053
FT /note="E3 ubiquitin-protein ligase PDZRN3-B"
FT /id="PRO_0000442731"
FT DOMAIN 247..338
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 420..505
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ZN_FING 18..56
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 99..154
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT REGION 563..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 683..709
FT /evidence="ECO:0000255"
FT COMPBIAS 563..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 154
FT /note="Q -> H (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="R -> H (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="M -> V (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="G -> S (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="Q -> L (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
FT CONFLICT 998
FT /note="D -> A (in Ref. 1; AEN28595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 118456 MW; 377B76909AE6A168 CRC64;
MGFELDRFKG AVDPDFKCNL CNKVLEDPLT TPCGHVFCAG CVLPWVVQQS SCPVKCQRIS
TKELNHVLPL KNLILKLDIK CDNHARGCEK IVKLQHLAEH AEMCDYSPAK CRNKGCSEVL
NLKDMDAHMR ESCDYRAVGI CESGCGLMLT HKEQKLDNHC CLKALKAHNG ALQGKVVTLD
KELKKQALKS TKREKSLLAQ LSAVHNELQM TALKYQKKFT EYSARIDSLS KSLSPSPPCK
GGETKSVTAI LHRESGSLGF NIVGGRPCVD NKDGTSNEGI FVSKIVEKGA ADKEGGLQIH
DRIMEVNGKD LSKATHDQAV EAFRMAKEPI MVQVLRRAPR PKPTGPTGEG QVVDISTQTD
ITFQHIMALS KLPTSSTPVD VLEQYLLPEG HSPAHEYFDP NDFLEGMQHE IEREELEYEE
VDLYRTNIHD KLGFTVCYRT DDEDETGIYV SEIDPNSIAA KDGRIREGDR IIQINGIEIQ
NREEAVALLT SEEHPNVCLL LARPEIQLDE GWMDDDRNDY LDDLHMDMLE QQHHQAMQFT
ASMLQQKKHE EDGGTTDTAT LLSHHHEKDS GVGRTDDSTR NDESSEQENL ADDQTSASTT
LGSRRRLAYS QDTLGSGDLP FSSESFISAD YADAEFLGDF PADECERFRE LLELKCQMQS
AGSSGTPDQS LLWPSGGQGG VGEEGVDKEL ELLNEELRSI ELECLSIVRA HRMQQLREQC
REQSWMLHNS GFRNYNTSVD ARRHELADIS ELPEKSDKDS SSAYNTGESC RSTPLTLELS
PDNSLRRGNE SQAEAGASSS TSGPSRILKP LLSPVQEACS PTRGRPTLLK ESEVGTQPEV
RERKGGRHAH PQSPYKHAHI PAHAQHYQSY MQLIQQKSVE YAQSQMSLVS MCRDPVTSAD
LGPKMEWKVK IRSDGTRYIT KRPVRDKLLK ERALRIREER SGMTTDDDAV SEMKMGRYWS
KEERKQHAVR AKEQRQRREF MKQSRMDCQK ELGVTTEDKK DVNIIELSHK KMMKKRNKKI
FDNWMTIQEL LTHGTKSPDG TRVYNSLLSV TTV
