ID H0V9T6_CAVPO Unreviewed; 837 AA.
AC H0V9T6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 18-JUN-2025, entry version 80.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19A {ECO:0000313|Ensembl:ENSCPOP00000006591.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000006591.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000006591.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000006591.2};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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DR EMBL; AAKN02000315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02000316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02000317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0V9T6; -.
DR FunCoup; H0V9T6; 1111.
DR STRING; 10141.ENSCPOP00000006591; -.
DR Ensembl; ENSCPOT00000007385.3; ENSCPOP00000006591.2; ENSCPOG00000007313.4.
DR VEuPathDB; HostDB:ENSCPOG00000007313; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000158703; -.
DR HOGENOM; CLU_016793_1_0_1; -.
DR InParanoid; H0V9T6; -.
DR OMA; HQCSISL; -.
DR TreeFam; TF324777; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000007313; Expressed in uterine cervix and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20362; BRcat_RBR_RNF19A; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 361..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..351
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 132..180
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 621..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..682
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 90548 MW; 4FA47CAD481D5D12 CRC64;
LQEQEIGFIL KYNEGLCVDT VPDSILIRIL DMSLHRQMGS DRDLQSSASS VSLPSVKKAP
KKRRISIGSL FRRKKGNKRK SRELNGGVDG IASIESIHSE MCTDKNSVFS TNASSDNGLT
SISKQVGDFI ECPLCLLRHS KDRFPDIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT
ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT
CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK
ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAIAGGV
TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI
NVGGTNTAVD TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA
LAGASITGSL SGSAMVNCFN RLEVQADVQK ERYSLSGESG TVSLGTVSDN ASTKAMAGSI
LNSYIPLDKE GNSLEVQVDI ESKPSKFRHN SGSSSVDDGS ATRSHACSSG GLPEGKSSTT
KWSKEATAGK KSKSGKLRKK GNMKINETRE DMDAQLLEQQ STNSSEFEAP SLSDSVPSVA
DSHSSHFSEF SCSDLESMKT SCSHGSSDYH TRFATVNILP EVENDRLENS PHQCSISLLS
KTVSCSEVPQ QSHIAEDHGN SGIKPNGDLY FGDALKETNN NHSHQTLELK VAIQTEI
//
