ID A0A3Q2WTZ3_HAPBU Unreviewed; 862 AA.
AC A0A3Q2WTZ3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF1 {ECO:0000256|ARBA:ARBA00019074};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Plenty of SH3s {ECO:0000256|ARBA:ARBA00031457};
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF1 {ECO:0000256|ARBA:ARBA00033431};
DE AltName: Full=SH3 domain-containing RING finger protein 1 {ECO:0000256|ARBA:ARBA00030936};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000029731.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000029731.1}
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}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR RefSeq; XP_005923409.1; XM_005923347.2.
DR RefSeq; XP_005923410.1; XM_005923348.1.
DR AlphaFoldDB; A0A3Q2WTZ3; -.
DR STRING; 8153.ENSHBUP00000029731; -.
DR Ensembl; ENSHBUT00000020087.1; ENSHBUP00000029731.1; ENSHBUG00000014351.1.
DR GeneID; 102310116; -.
DR CTD; 57630; -.
DR GeneTree; ENSGT00940000155875; -.
DR OMA; NMIIAPS; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16748; RING-HC_SH3RF1; 1.
DR CDD; cd11930; SH3_SH3RF1_2; 1.
DR CDD; cd11926; SH3_SH3RF1_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; IPR035795; SH3RF1_SH3_2.
DR InterPro; IPR027370; Znf-RING_euk.
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; PF13445; zf-RING_UBOX; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 130..189
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 192..255
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 429..490
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 803..862
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 93..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 91085 MW; 5E2D1EE59131EDB1 CRC64;
MDESVLLDLL ECPVCLERLD ASAKVLPCQH TFCRRCLQGI LGSRGELRCP ECRTLVDCAV
DELPSNILLV RLLDGIKQRP RRVGPGAAVC TNGTSGAMAR AHGSGSRDQG TPGAQPQRAQ
AKSTLVRGVP QLPCAKALYN YDGKEQGDLK FSKGDIIILR RQVDENWYHG EMGGVHGFFP
TNFVQVIKPL PQPPPQCKAL YDFELKDKEA DKDCLPFSKD DILTVIRRVD ENWAEGMLGD
KIGIFPISYV EFNSAARQLI ELDKPSDSSG DSGEGASSGP QTNGAHRAGE KKNSKKRHSF
TSLTMSHKPM LAPPPQRHSM EISGPVLISS SNPTAAARIG EISGGLSCSA PSQVHICTTG
LIVTPPPSSP VTTATVFTFP SETSYTSIPV DALPPPPPPP PQSSVGGAAY SLAAGQRPSP
SISDQSGRQR PTVYVAMFPY TPRKEDELEL RKGEMFLVLE RCQDGWFKGT SMHTGKIGVF
PGNYMSPVSR TASGSSQPKV PLSLCTQAGR GVTIVSPSSA PLGAIVSGPD FNKPLTVCPA
VAPANSQPAA VVTTAQTATG QQPKVSLHVT SQMTVNQARN AVRTAACHSQ DRPTAAVTPI
QSATPVTYLP HLAVCSQPGS SPAQGCTRVG VAMGCAAASL TPPNVSAASL DSDSLRPVPV
LAVPVNPGSN SALNPTSNNA APACRLDKDI KREKKSLLKL LSSNKKKSRP SPPSSPTLEA
EQAAAAGELL HGAVGPDTSP PSGPASCLDS EPAAASASSS SSSSVPESSH RKSSPLDGCV
PIAPPPRQPC SSLLSQQHDA RPIICERYRV VVSYPPQSEA ELELKEGDIV FVHRKREDGW
FKGTLQRNGR TGLFPGSFVD II
//
