ID G3SKD7_GORGO Unreviewed; 771 AA.
AC G3SKD7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSGGOP00000028580.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000028580.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000028580.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000028580.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000028580.2}
RP IDENTIFICATION.
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; CABD030010806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030010815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3SKD7; -.
DR STRING; 9593.ENSGGOP00000028580; -.
DR Ensembl; ENSGGOT00000041077.2; ENSGGOP00000028580.2; ENSGGOG00000034870.2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160405; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; G3SKD7; -.
DR OMA; SEMRGAM; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001519; Chromosome 2A.
DR Bgee; ENSGGOG00000034870; Expressed in testis and 4 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 GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16750; RING-HC_SH3RF3; 1.
DR CDD; cd11928; SH3_SH3RF3_1; 1.
DR CDD; cd11931; SH3_SH3RF3_2; 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; 3.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
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:UP000001519};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP};
KW 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 SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..771
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014186932"
FT DOMAIN 57..98
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 194..253
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 256..319
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 464..525
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 712..771
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 18..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 81181 MW; 855DAD1E871A3862 CRC64;
MLLGASWLCA SKAAAAAAQS EGDEDRPGER RRRRAAATAA GAGEDMDESS LLDLLECSVC
LERLDTTAKV LPCQHTFCRR CLESIVCSRH ELRCPECRIL VGCGVDELPA NILLVRLLDG
IRQRPRAGTS PGGSPPARPI PGQSAAPTLA GGGGGAAGST PGSPVFLSAA AGSTAGSLRE
LATSRTAPVA KNPCLLPYGK ALYSYEGKEP GDLKFNKGDI IVLRRKVDEQ WYHGELHGTQ
GFLPASYIQC IQPLPHAPPQ GKALYDFEMK DKDQDKDCLT FTKDEILTVL RRVDENWAEG
MLGDKIGIFP LLYVELNDSA KQLIEMDKPC PAAASSCNAS LPSDSGAVAS MAPSPTLSSS
GAVSAFQRRV DGKKNTKKRH SFTALSVTHR SSQAASHRHS MEISAPVLIS SSDPRAAARI
GDLAHLSCTA PTQDVSSSAG STPTAVPRAA SVSGEQGMPP KVQLPLNVYL ALYAYKPQKS
DELELHKGEM YRVLEKCQDG WFKGASLRTG VSGVFPGNYV TPVSRVPAGG AGPPRNNVVG
GSPLAKGITT TMHPGSGSLS SLATATRPAL PITTPQAHAQ HPTASPPTGS CLRHSAQPAA
SQARSTISTA AHSAAQAQDR PTATVSPLRT QNSPSRLPAT SLRPHSVVSP QHSHQPPVQM
CPRPAIPLTS AASAITPPNV SAANLNGEAG GGPIGVLSTS SPTNTGCKLD EKKSEKYRVV
VSYPPQSEAE IELKEGDIVF VHKKREDGWY KGTLQRNGRT GLFPGSFVES F
//
