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Database: UniProt
Entry: H0V0N4_CAVPO
LinkDB: H0V0N4_CAVPO
Original site: H0V0N4_CAVPO 
ID   H0V0N4_CAVPO            Unreviewed;       617 AA.
AC   H0V0N4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   18-JUN-2025, entry version 75.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=RNF19B {ECO:0000313|Ensembl:ENSCPOP00000003025.3};
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:ENSCPOP00000003025.3, 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:ENSCPOP00000003025.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003025.3};
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; AAKN02028581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02028582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0V0N4; -.
DR   FunCoup; H0V0N4; 1375.
DR   STRING; 10141.ENSCPOP00000003025; -.
DR   Ensembl; ENSCPOT00000003390.3; ENSCPOP00000003025.3; ENSCPOG00000003347.4.
DR   VEuPathDB; HostDB:ENSCPOG00000003347; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000158451; -.
DR   HOGENOM; CLU_016793_3_0_1; -.
DR   InParanoid; H0V0N4; -.
DR   OMA; EQEQTCK; -.
DR   TreeFam; TF324777; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000003347; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0044194; C:cytolytic granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   CDD; cd20355; Rcat_RBR_RNF19; 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   Gene3D; 1.20.120.1750; -; 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; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 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}.
FT   TRANSMEM        231..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..221
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          504..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..568
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  66656 MW;  7ED3086EBD9C7428 CRC64;
     MVKAAARRGG PCLKMRRRAE GGRPGARRKV ECPLCLVRLP PERAPRLLSC PHRSCRDCLR
     HYLRLEISES RYEEFMLRRY LASDPDCRWC PAPDCGYAVI AYGCASCPKL TCEREGCQTE
     FCYHCKQIWH PNQTCDMARQ QRAQTLRVRT KHTSGLSYGQ ESGPADDIKP CPRCSAYIIK
     MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK ILWQLGTLIG
     APVGISLIAG IAIPAMVIGI PVYVGRKIHS RYEGRKTSKH KRNLAITGGV TLSVIASPVI
     AAVSVGIGVP IMLAYVYGVV PISLCRGGGC GVSTANGKGV KIEFDEDDGP ITVADAWRAL
     KNPSIGESSI EGLTSVLSTS GSPTDGLSVM QGPYSETASF AALSGGTLSG GILSSGKGKY
     SRLEVQADVQ KEIFPKDTAS LGAISDNAST RAMAGSIISS YNPQDRECNN MEIQVDIEAK
     PSHYQLVSGS STEDSLHVHA QMVENEEEGS GGGNSSNEED PAYRHQSCEQ KDCPPSKAWD
     ISLAQPESIR SDLESSDTQS DDVPDITSDE CGSPRSHTAV CPSTPRTQGA PSPSAHKSLS
     APAEGQTVLK SEEYEVE
//
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