ID A0A1L8EUH9_XENLA Unreviewed; 674 AA.
AC A0A1L8EUH9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
GN Name=rnf157.L {ECO:0000313|RefSeq:XP_018090839.1,
GN ECO:0000313|Xenbase:XB-GENE-17331968};
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 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018090839.1};
RN [1] {ECO:0000313|RefSeq:XP_018090839.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018090839.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018090839.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU369081};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR RefSeq; XP_018090839.1; XM_018235350.2.
DR AlphaFoldDB; A0A1L8EUH9; -.
DR STRING; 8355.A0A1L8EUH9; -.
DR MaxQB; A0A1L8EUH9; -.
DR PaxDb; 8355-A0A1L8EUH9; -.
DR GeneID; 108701126; -.
DR KEGG; xla:108701126; -.
DR AGR; Xenbase:XB-GENE-17331968; -.
DR CTD; 108701126; -.
DR Xenbase; XB-GENE-17331968; rnf157.L.
DR OMA; EDSCPVH; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 108701126; Expressed in camera-type eye and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
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 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369081};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Transferase {ECO:0000256|RuleBase:RU369081};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369081};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU369081}.
SQ SEQUENCE 674 AA; 73341 MW; D5973061ECE3073D CRC64;
MGALTSRQHA GVEEVDMPCS SLYRYPPKSG SYFGSHFIMG GEKFESSHPE GYLFGENSDL
NFLGSRPVTF PYTAPSPQEP VKTLRSLINI RKDTLRLVRC TEELKSTGVE GSRPKVHYNV
EFTFDTDAPV AITIYYQSTE EFQGGIASYL PKSSNLQSDT VHFKRGVSQQ FCFPSHTVDP
AEWREEELTF DLDREVYPMV VHAVVEEGEE HLGHSHVLMA IFEKHADGSF CVKPLKQKQV
VDGVSYLLQE IYGIENKYNS QDSKVAEDEV SDNSAECVVC LSDVRDTLIL PCRHLCLCNA
CADTLRYQAS NCPICRLPFR ALLQIRAMRK VPGPHSPAGF SPIIAAPTSD SEEHTSEHVP
PGYEVVSLLE ALNGPLTPSP SVPPLRALGE ARRPGALPSY GSDIHLRMHS PLQHLCGSQA
LKLKKSISRS ISQNSSVLQE DEMEKSFSEA EIRTPRKKTS QLAEECGVTP ESDNLTLSSS
GAIDQSSCTG TPLSPTITSP EDPLSSSLAQ SVMSMASSHS QQSQFSTDTV SSMSGSYTAG
GMEEEEGGVT PSPPAAASGS PSMEGELSPA ESPEPHFVTV SAEEMDAEGN VTEEEFASPE
EDDGQRTGRE CDNNNAAGVT LRDVLDNVRG SEGCLADVCY TSVPGQQRSN PYHGSDNCIS
LQEDKQSQMD TELV
//