ID A0A2Y9N1U0_DELLE Unreviewed; 1030 AA.
AC A0A2Y9N1U0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=PDZ domain-containing RING finger protein 4 {ECO:0000313|RefSeq:XP_022428165.1};
GN Name=PDZRN4 {ECO:0000313|RefSeq:XP_022428165.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022428165.1};
RN [1] {ECO:0000313|RefSeq:XP_022428165.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022428165.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022428165.1; XM_022572457.2.
DR AlphaFoldDB; A0A2Y9N1U0; -.
DR STRING; 9749.A0A2Y9N1U0; -.
DR KEGG; dle:111174106; -.
DR InParanoid; A0A2Y9N1U0; -.
DR OrthoDB; 2879659at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 2.
DR CDD; cd16719; RING-HC_LNX4; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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 PANTHER; PTHR15545; PDZ DOMAIN CONTAINING RING FINGER PROTEIN 3, 4; 1.
DR PANTHER; PTHR15545:SF6; PDZ DOMAIN-CONTAINING RING FINGER PROTEIN 4; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 18..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 220..310
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 398..481
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 128..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 655..682
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 548..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 116196 MW; C96342406CFF2DAC CRC64;
MGFALERFAE AVDPDFQCRL CGQVLEEPLC TPCGHVFCAR CLLPWAARRR RCPLQCQPLA
PGDLYRVLPL RSLVQKLRTQ CDYRARGCGH SVGLRELAAH VELCDFGPAR RRRRGCVSGP
CGRGGGDASA RGGCGSAPGV RRGGTPGVRG GSGRAPGPQV LAWRRREKAL LAQLWALQEE
VLLTARRYQK KFTQYMAHVR NFARDPGGGR GRDGEHKPFT IVLERENDTL GFNIIGGRPN
QDNQEETPME GIYVSKILEN GPADRADGLE IHDKIIEVNG KDLSKATHEE AVEAFRNAKE
PIVVQVLRRT PLSKPAYGTA PEVRLVNAST QTDITFEHIM ALAKLRPPTP PVPDICPFLL
SDSCHSLHPM EHEFYEDDEY LSSLPADADR TEDFEYEEVE LCRVNSQEKL GLTVCYRTDD
EEDTGIYVSE VDPNSIAAKD GRIREGDRIL QINGEDAQDR EAAVALLSSD ECRRIVLLVA
RPESQLEEGW LEDERNEYLE ELNLSMLEEQ HNEAMQRTAS QVEQPKKQEE EEGTTDTATS
SSNNHEKDSG VGRTDESLRN DESSEQENAA EDPNGTSLKS KRELGQSKDT LGSTELQCNE
SFVSGEYIDS DCTGNQDEEC ERFRQLLELK CKIRKHGEYD LYYSSSTIEC NQGGREGVEH
ELQLLNEELR NIELECQNIM QAHRLRKVTD QYGDIWALHE GGFRNYNTSI DTQRGKLDDI
LEHPEKSDKD SSSAYNTAES CRSTPLTVDR SPDSSLPRVI NLTNKKNLRS TMAANQSSSG
QSSKESTKAK TTEQGCGIEG KEKTSESSKL SDPEKTSGEH IPYLSPYHSS SYRYANIPAH
ARHYQSYMQL IQQKSAVEYA QSQLSLLSVC KESQKCSEPK MEWKVKIRSD GTRYITKRPV
RDRILKERAL KIKEERSGMT TDDDTMSEMK MGRYWSKEER KQHLVRAKEQ RRRRESMMRS
RLECLKESPQ SGSESKKEVN IIELSHKKMM KKRNKKILDN WMTIQELMTH GAKSPDGTQV
PNAFLSVTAV
//
