ID   RN141_RAT               Reviewed;         230 AA.
AC   Q6IV57;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=RING finger protein 141;
GN   Name=Rnf141;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RA   Ma Y., Zhang S., Qiu W., Liu Y., Dong J., Xu W., Zhang G.;
RT   "Molecular cloning of rat Rnf141 gene.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in spermatogenesis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WVD5}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q8WVD5}.
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DR   EMBL; AY621087; AAT45392.1; -; mRNA.
DR   RefSeq; NP_001001800.1; NM_001001800.1.
DR   RefSeq; XP_006230112.1; XM_006230050.3.
DR   AlphaFoldDB; Q6IV57; -.
DR   BMRB; Q6IV57; -.
DR   BioGRID; 259183; 1.
DR   STRING; 10116.ENSRNOP00000024561; -.
DR   iPTMnet; Q6IV57; -.
DR   PhosphoSitePlus; Q6IV57; -.
DR   PaxDb; Q6IV57; -.
DR   GeneID; 308900; -.
DR   KEGG; rno:308900; -.
DR   UCSC; RGD:1303154; rat.
DR   CTD; 50862; -.
DR   RGD; 1303154; rnf141.
DR   eggNOG; KOG1039; Eukaryota.
DR   HOGENOM; CLU_080007_0_0_1; -.
DR   InParanoid; Q6IV57; -.
DR   OMA; TAANDSW; -.
DR   OrthoDB; 1106056at2759; -.
DR   PRO; PR:Q6IV57; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017900; Expressed in liver and 18 other tissues.
DR   Genevisible; Q6IV57; RN.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR   CDD; cd16545; RING-HC_RNF141; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR043400; RING-HC_RNF141.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Lipoprotein; Membrane; Metal-binding; Myristate; Reference proteome; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVD5"
FT   CHAIN           2..230
FT                   /note="RING finger protein 141"
FT                   /id="PRO_0000056104"
FT   ZN_FING         155..192
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVD5"
SQ   SEQUENCE   230 AA;  25471 MW;  108C42BCE49F8424 CRC64;
     MGQQISDQTQ LVINKLPEKV AKHVTLVRES GSLTYEEFLG RVAELNDVTA KIAAGQEKHL
     LFEVQPGSDS SAFWKVVVRV VCTKINKSSG IVEASRIMNL YQFIQLYKDI TSQAAGVLAQ
     SSTSEEPDGN PSSVTSCQAS LWMGRVKQLT DEEECCICMD GRADLILPCA HSFCQKCIDK
     WSDRHRNCPI CRLQMTGANE SWVVSDAPTE DDMANYILNM ADEAGQPHRP