ID H0UWN0_CAVPO Unreviewed; 802 AA.
AC H0UWN0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=SH3RF3 {ECO:0000313|Ensembl:ENSCPOP00000001471.3};
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:ENSCPOP00000001471.3, 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:ENSCPOP00000001471.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000001471.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; AAKN02027957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02027958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013009913.1; XM_013154459.1.
DR AlphaFoldDB; H0UWN0; -.
DR STRING; 10141.ENSCPOP00000001471; -.
DR Ensembl; ENSCPOT00000001652.3; ENSCPOP00000001471.3; ENSCPOG00000001631.4.
DR GeneID; 100713199; -.
DR KEGG; cpoc:100713199; -.
DR CTD; 344558; -.
DR VEuPathDB; HostDB:ENSCPOG00000001631; -.
DR eggNOG; KOG2177; Eukaryota.
DR eggNOG; KOG2995; Eukaryota.
DR GeneTree; ENSGT00940000160405; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; H0UWN0; -.
DR OMA; SEMRGAM; -.
DR OrthoDB; 5407056at2759; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000001631; Expressed in pituitary gland and 6 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; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR CDD; cd16750; RING-HC_SH3RF3; 1.
DR CDD; cd11925; SH3_SH3RF3_3; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR028502; SH3RF3_RING-HC_Zfn.
DR InterPro; IPR035612; SH3RF3_SH3_3.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50002; SH3; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 121..180
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 183..244
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 390..451
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 743..802
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 81..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 85160 MW; 4CC2306E90000D4A CRC64;
MDESSLLDLL ECAVCLERLD TTAKVLPCQH TFCRRCLESI VCSRRELRCP ECRILVGCGV
DELPANILLV RLLDGLRCRP RGGSGSGPGP GPPTLPGPAA PPGTACEPTA GRNVTTAKSL
PQLPYGKALY SYEGKEPGDL KFNKGDVIIL RRRVDDHWYH GELHGTRGFL PASYVQCLRP
LPQTPPQGTA LYDFEMKDRD QDCLTFTKDE VLTVIRRVDD NWAEGMLGDR IGIFPLLYVQ
LNDSAKQLIE MDKLCPAAAA ASDCAAPLPL DPSSVASSGQ GHAVGSSGAV SAFQRRMDSK
KNAKKRHSFT ALSVTHKSSQ AATHRHSMEI SAPVLISSSD PRAAARIGEL TGLPCAVPAQ
DPCLAGPVPT AVPRASEVDG EQGTSPKSAL PLNVYLALYA YKPQKSDELE LRKGEMYRVL
EKCQDGWFKG ASLRTGLSGV FPGNYVTPVS RAPGAAAPPR NSVLGGSPLA KGMATTMHPG
GGSLSRPAQP VTTPQVQAPH PAGSPPTSSC PRHTAQSATG QTQGPLSAAT HSSTQAQDRP
TATVTPLRSQ SSPSRLPATS LRPRSVVSPQ HGQQSLVQTS PRPAIPLTSA ASAVMPPSVS
TTSLSGDVSA GSGRGLSTSS PTGTGCRLED KRAEKKEKKS GLLKLLAGAS TRRKSHSPPS
FSPTHDPPVA ADTSLLGAMG PDVSSLSVHG RAGSCPIESE MRGAMGLEPL HRKTSSLDLN
FCSSPARQAT LSMAAIRPEP KLLPRERYRV VVSYPPQSEA EIELREGDVV FVHRKREDGW
YEGTLQRNGR TGLFPGSFVE SF
//
