ID   RN157_XENLA             Reviewed;         674 AA.
AC   Q6INH1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=E3 ubiquitin ligase Rnf157 {ECO:0000250|UniProtKB:Q96PX1};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96PX1};
DE   AltName: Full=RING finger protein 157;
DE   AltName: Full=RING-type E3 ubiquitin transferase Rnf157 {ECO:0000305};
GN   Name=rnf157;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase that ubiquitinates apbb1 for its
CC       degradation by the proteasome and thus prevents apoptosis and promotes
CC       survival of neurons (By similarity). Has a dual role in neurons as it
CC       is also required for dendrite growth and maintenance for which its
CC       ligase activity is not critical (By similarity). May act as a scaffold
CC       molecule to regulate this process (By similarity). Acts as a downstream
CC       effector of the interconnected PI3K and MAPK signaling pathways and
CC       thus participates in the regulation of the cell cycle (By similarity).
CC       {ECO:0000250|UniProtKB:Q96PX1}.
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:Q96PX1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:M0R5D6}.
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DR   EMBL; BC072310; AAH72310.1; -; mRNA.
DR   RefSeq; NP_001085159.1; NM_001091690.1.
DR   AlphaFoldDB; Q6INH1; -.
DR   DNASU; 432241; -.
DR   GeneID; 432241; -.
DR   KEGG; xla:432241; -.
DR   AGR; Xenbase:XB-GENE-5933428; -.
DR   CTD; 432241; -.
DR   Xenbase; XB-GENE-5933428; rnf157.S.
DR   OMA; MSIMLHK; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 432241; Expressed in camera-type eye and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   CDD; cd16817; mRING-HC-C3HC5_RNF157; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996:SF1; E3 UBIQUITIN LIGASE RNF157; 1.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..674
FT                   /note="E3 ubiquitin ligase Rnf157"
FT                   /id="PRO_0000261616"
FT   ZN_FING         277..316
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          376..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..601
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  73258 MW;  2A2BA067BDCB489C CRC64;
     MGALASRQHA GVEEMDMPCN SLYRYPPKSG SYFGSHFIMG GEKFESSHPE GYLFGENSDL
     NFLGSRPVTF PYTAPSPQEP VKTLRSLINI RKDTLRLVRC TEELKTTGVE GSRPKVHYNV
     EFTFDTDARV AITMYYQATE EFQGGIPSYL PKSSNLQSDT VHFKRGVSQQ FCFPSHTVDP
     SEWREEELTF DLDREVYPMV VHAVVEEGEE HLGHSHVLMA TFEKHADGSF CVKPLKQKQV
     VDGVSYLLQE IYGIENKYNS QDSKVAEDEL SDNSAECVVC LSDVRDTLIL PCRHLCLCNA
     CADTLRYQAS NCPICRLPFR ALLQIRAMRK VPGPHSPGGF SPIIAAPTSD SEEHTSEHVP
     PGYEVVSLLE ALNGPLTPSP SAPPLRALGE ARRPGGLPSY GSDIHLRMHS PLQHLCGGQA
     LKLKKSISRS ISQNSSVLQE DEMEKSFSEA EIQTPRKKTS QLAEENGVTP ESENLTLSSS
     GAIDQSSCTG TPLSPTISSP EDPLSSSLAQ SIMSMASSHS QQSQLSTDTV SSMSGSYTAG
     GMEEEEGGIT PSPPAAASGS PSIEGELSPA ESPEPHFVTV SAEEMDAEGN VTEEEFASPE
     EDDGQMTGRE CDNNNAAGVT LRDVLDNVRG SEGCLADVCY SSIPGQQRSN PYHGSDNCIS
     LQDDTQSHLS TKLV
//