ID A0A3B4F786_9CICH Unreviewed; 1044 AA.
AC A0A3B4F786;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=E3 ubiquitin-protein ligase PDZRN3 isoform X1 {ECO:0000313|RefSeq:XP_005726677.1};
DE SubName: Full=PDZ domain containing ring finger 3 {ECO:0000313|Ensembl:ENSPNYP00000005111.1};
GN Name=pdzrn3 {ECO:0000313|RefSeq:XP_005726677.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000005111.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000005111.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005726677.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_005726677.1; XM_005726620.2.
DR AlphaFoldDB; A0A3B4F786; -.
DR STRING; 303518.ENSPNYP00000005111; -.
DR Ensembl; ENSPNYT00000005241.1; ENSPNYP00000005111.1; ENSPNYG00000003966.1.
DR GeneID; 102208754; -.
DR CTD; 100005518; -.
DR GeneTree; ENSGT00950000183062; -.
DR OrthoDB; 2879659at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR15545:SF5; E3 UBIQUITIN-PROTEIN LIGASE PDZRN3; 1.
DR PANTHER; PTHR15545; PDZ DOMAIN CONTAINING RING FINGER PROTEIN 3, 4; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00207}; Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00207};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 18..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 100..145
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 244..336
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 417..502
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ZN_FING 100..145
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 543..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 117880 MW; AF0B3E8FE7B758C2 CRC64;
MGFELDRFKG TVDPDFKCNL CNKVLEDPLT TPCGHVFCSG CVLPWVVQQS SCPVKCQRIS
TKELNHVLPL KNLILKLEIK CDNHTRGCDA VVKLQHLAEH AEMCDYSPAK CRNRGCSEVL
NLRDVDAHMR ETCDYRPVEV CESGCGLMVT QKEQKSNSHC CLRALKAHNS ALQCRMIILD
REFKKQTIEA NKREKALLAQ LSAVHSELQM TALKYQKKFT EYSERIDSLT KTVAFSCKEG
ETKSVTVVLL REGGSLGFNI IGGRPCVDDN DSTSNEGIFV SKIVEKGPAD KEGGLQIHDR
IIEVNGKDLS KATHDQAVEA FRTAKEPIVV QVLRRAPYPK VANPAVDTQV TDISTQTDIT
LQHIMALTNL PPSSPPISEL EEYLLPEEHP PGHVYFDPDF LEGIQQDIER EELEYEEVDL
YRDNIQDKLG LTICYRTDDE DEAGIYISEI DPNSIAAKDG RIREGDKIIQ INGVEIQNRE
DAVALLTSES NQNISLLVAR PEIQLDEGWM DDDRNDFLDD LHMDMLEQQH HQAMQFTASM
LQQKKHEEDG GTTDTATLLS NHHEKDSGVG RTDESTRNDE SSEQENLGDD QTTASNTLGS
CRKLTYSQDT LGSTDLPFSS ESFMSVDYAD ADFLGIPVDE CERFRELLEL KCQMRSSGAQ
GLYGQGGGAV GQDQEGVDKE LEMLNEELRT IELECLNIVR AHKMQQLREQ CRESWMLHNS
GFRNYNTSID ARRHELSDIT ELPEKSDKDS SSAYNTGESC RSTPLTLELS PDNSLRRVAE
NQAGPSGSSG RMLKPLLSPV QEACSPSRSR SSSKDPDGAL QAEGKERKPG ESSKSGRGFS
QPHSPYKHAH IPAHAQHYQS YMQLIQQKSA VEYAQSQMSL VSMCRDPITP SDLEPKMEWK
VKIRSDGTRY ITKRPVRDKL LRERALRIHE ERSGMTTDDD AISELKMGRY WSKEERKQHA
VRAKEQRQRR EFMKQSRADC LKEQATLEDK KEPNIIELSH KKMMKKRNKK IFDNWMTIQE
LLTHGTKSPD GTRVYNSLLS VTTV
//
