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Database: UniProt
Entry: G3UHP2_LOXAF
LinkDB: G3UHP2_LOXAF
Original site: G3UHP2_LOXAF 
ID   G3UHP2_LOXAF            Unreviewed;       611 AA.
AC   G3UHP2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=SH3 domain containing ring finger 2 {ECO:0000313|Ensembl:ENSLAFP00000027350.1};
GN   Name=SH3RF2 {ECO:0000313|Ensembl:ENSLAFP00000027350.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000027350.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000027350.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027350.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000027350.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027350.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3UHP2; -.
DR   STRING; 9785.ENSLAFP00000027350; -.
DR   Ensembl; ENSLAFT00000027656.1; ENSLAFP00000027350.1; ENSLAFG00000000315.3.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000160067; -.
DR   InParanoid; G3UHP2; -.
DR   OMA; PRLHMEG; -.
DR   TreeFam; TF105571; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   CDD; cd11929; SH3_SH3RF2_1; 1.
DR   CDD; cd11932; SH3_SH3RF2_2; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035792; SH3RF2_SH3_1.
DR   InterPro; IPR035794; SH3RF2_SH3_2.
DR   PANTHER; PTHR14167:SF60; E3 UBIQUITIN-PROTEIN LIGASE SH3RF2; 1.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..58
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          61..126
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          133..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  66004 MW;  68B80DE77E3D5E82 CRC64;
     VPRAKALCNY RGQNPGDLRF NKGDVILLRR QLDENWYQGE INGVSGIFPA SSVEIIKQLP
     QPPPLCRALY NFDLRDRDKS ENQDCLTFLK DDIITVISRV DENWAEGKLG DKVGIFPILF
     VEPNLTARHL LEKNKGRPSS RTKNLPLGPS SPRGKAINSP VLRRGPGSRR KLPGQFSITT
     ALNTLNRMVH SPSGRHMVEI STPVLISSSN PSVITQHMEK ADIPPSSVGQ ERASSKHPGP
     TKPGGRESTA LIILPAPAHH HGVLRAFAVH SSKKGETERA DSRRGEQVGV GSEIWCGWGR
     GTANLPGRAS IFCPSSYLKI PTTRKTSSFP ESRSPGLYAT WTLSTSSVSS QGSISEGDPR
     QSRPFKSVFV PTAIVNPVRS STASPGTVAQ GSLRKGRSSM RKNGSLQRPV QSGIPTLVVG
     SLRRSPTMVV QPQQFQFYQP QGVPSSPSSV AVEMGPKPAP TGEPALTCVS RGNDTRIHSA
     ASSLIMEGKE NPIKSEPPLK PPASAPPSIL VKPENSRNGT EKQVKTVRFQ NYSPPPAKHY
     TYGKPEQPAT PKGSQPEAAP LGPEMTILFA HRSGCHSGQQ TDLRRKPTFG KAMSPVPVPT
     ASATQTVFPS K
//
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