ID E1B964_BOVIN Unreviewed; 416 AA.
AC E1B964;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=LON peptidase N-terminal domain and ring finger 1 {ECO:0000313|Ensembl:ENSBTAP00000012816.6};
GN Name=LONRF1 {ECO:0000313|Ensembl:ENSBTAP00000012816.6,
GN ECO:0000313|VGNC:VGNC:30949};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000012816.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000012816.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012816.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000012816.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000012816.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; E1B964; -.
DR SMR; E1B964; -.
DR STRING; 9913.ENSBTAP00000012816; -.
DR PaxDb; 9913-ENSBTAP00000012816; -.
DR Ensembl; ENSBTAT00000012816.6; ENSBTAP00000012816.6; ENSBTAG00000020084.6.
DR VEuPathDB; HostDB:ENSBTAG00000020084; -.
DR VGNC; VGNC:30949; LONRF1.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00440000033329; -.
DR HOGENOM; CLU_013989_1_1_1; -.
DR InParanoid; E1B964; -.
DR OMA; SSEVCMF; -.
DR TreeFam; TF327043; -.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000020084; Expressed in corpus epididymis and 106 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23327:SF4; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN 1; 1.
DR PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00464; LON; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 122..160
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 208..409
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 47866 MW; B806078FC5875FD3 CRC64;
MEESHSASEL SPEQNEEIAE VTSEPVKGSL NRARSAQAIN STDMPAREDC LKRVSSEPSL
CIQGKGVLLK RKLSLLDQDV IVNEDGRNKL KRQGEIPTEV CTFSLTYGDV PEELIDVSDF
ECSLCMRLFF EPVTTPCGHS FCKNCLERCL DHTPYCPLCK ESLKEYLADR RYCVTQLLED
LIVKYLPDEL SERKKIYDEE TAELSHLTKN VPIFVCTMAY PTVPCPLHVF EPRYRLMIRR
SIQTGTKQFG MCVSDTQNSF ADYGCMLQIR NVHFLPDGRS VVDTVGGKRF RVLKRGMKDG
YCTADIEYLE DIKVENEDEI ENLRQLHDLV YSQACSWFQN LRDRFRSQIL QHFGSMPGRE
ENLQAIPNGP AWCWWLLAVL PVDPRYQLSV LSMKSLKERL TKIQHILTYF SRDQSK
//
