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Database: UniProt
Entry: A0A3B1KI42_ASTMX
LinkDB: A0A3B1KI42_ASTMX
Original site: A0A3B1KI42_ASTMX 
ID   A0A3B1KI42_ASTMX        Unreviewed;       578 AA.
AC   A0A3B1KI42;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:ENSAMXP00000053369.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000053369.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000053369.1}
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}.
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DR   AlphaFoldDB; A0A3B1KI42; -.
DR   Ensembl; ENSAMXT00000033558.1; ENSAMXP00000053369.1; ENSAMXG00000012721.2.
DR   GeneTree; ENSGT00940000160405; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000012721; Expressed in brain and 10 other cell types or tissues.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd11931; SH3_SH3RF3_2; 1.
DR   CDD; cd11785; SH3_SH3RF_C; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 4.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR   PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF14604; SH3_9; 3.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 4.
DR   SUPFAM; SSF50044; SH3-domain; 4.
DR   PROSITE; PS50002; SH3; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..44
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          47..110
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          265..326
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          519..578
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          120..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  62599 MW;  94F1C1CB1FBDAA20 CRC64;
     PGDLKFNKGD IIILRRKVDE NWYHGELNGS HGFLPASYIQ CIRPLSQTPP QGKALYDFEV
     KDKDQDKDCL TFTKDEILTV IRRVDENWAE GMLGDKIGIF PILYVELNET AKQLMEMDKP
     VAVPGPSADP GSPPSGSSCN GNGQVSTAIQ RRLDGKKNAK KRHSFTALSM TQRTAQALAN
     NRHSMEISAP VLISSSDPRA AARIGDCPHL SSSAPTTQVP PSHFLLTHTP SSEVATGSSR
     SVFPVKWPFS VYNSCNKHSV VCCVVCAFSY LALYAYKPQK ADELELRKGE MYRVTEKCQD
     GWFKGTSLRS GASGVFPGNY VTPVSRAPRP APPAGRSPWW LYRSLTPPCP PSPRQRPAPS
     SPLNSAAAAI TPPNVTAALL NGGETAGIPL QPGSPGCLSF LCCFSQKEKK SSALLKLLSG
     AAAKKKSRSP PSVSPTHEPR SPATDPSSSP VQGAMASELQ PAGHGRAGSC PIESEMQGAM
     GMEPLHRKSG SLDLNFVSPP VRQPCSSSLL AIRPEPKPLS RERYRVVVPY PPQSEAEIEL
     KEGDIVFVHK KREDGWYKGT LQRTGRTGLF PGSFVESF
//
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