SH3R1_DANRE
ID SH3R1_DANRE Reviewed; 867 AA.
AC A5D8S5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=E3 ubiquitin-protein ligase SH3RF1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q7Z6J0};
DE AltName: Full=Plenty of SH3s;
DE Short=Protein POSH;
DE AltName: Full=RING-type E3 ubiquitin transferase SH3RF1 {ECO:0000305};
DE AltName: Full=SH3 domain-containing RING finger protein 1;
GN Name=sh3rf1; Synonyms=posh; ORFNames=si:dkey-15j16.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of
CC an external substrate, it can catalyze self-ubiquitination. Acts as a
CC scaffold protein that contributes to the effective activation of the
CC JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1,
CC ECO:0000250|UniProtKB:Q7Z6J0}.
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:0000250|UniProtKB:Q7Z6J0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q69ZI1}.
CC -!- DOMAIN: The RING finger domain is required for ubiquitin ligase
CC activity and autoubiquitination. {ECO:0000250|UniProtKB:Q7Z6J0}.
CC -!- PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-
CC mediated degradation. {ECO:0000250|UniProtKB:Q71F54}.
CC -!- SIMILARITY: Belongs to the SH3RF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI41795.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC141794; AAI41795.1; ALT_INIT; mRNA.
DR RefSeq; NP_001038952.2; NM_001045487.2.
DR AlphaFoldDB; A5D8S5; -.
DR SMR; A5D8S5; -.
DR STRING; 7955.ENSDARP00000050558; -.
DR PaxDb; A5D8S5; -.
DR PeptideAtlas; A5D8S5; -.
DR GeneID; 556523; -.
DR KEGG; dre:556523; -.
DR CTD; 57630; -.
DR ZFIN; ZDB-GENE-030131-6288; sh3rf1.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; A5D8S5; -.
DR OrthoDB; 291531at2759; -.
DR Reactome; R-DRE-9013424; RHOV GTPase cycle.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:A5D8S5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0043370; P:regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR CDD; cd11930; SH3_SH3RF1_2; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 3.30.40.10; -; 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_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 3.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF50044; SSF50044; 4.
DR PROSITE; PS50002; SH3; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Golgi apparatus; Metal-binding;
KW Reference proteome; Repeat; SH3 domain; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..867
FT /note="E3 ubiquitin-protein ligase SH3RF1"
FT /id="PRO_0000334155"
FT DOMAIN 132..191
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 194..257
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 436..497
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 808..867
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 101..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 91632 MW; F766AD5D01C3D0A4 CRC64;
MDESALLDLL ECPVCLERLD ATAKVLPCQH TFCRRCLLGI VGSRGELRCP ECRTLVESGV
DELPSNILLV RLLDGIKQRP RRTGSVHGTC ANGSAVAGVR AQGAGGSQRD PGPTGGQSQR
VQAKSTPVRG VPQLPCAKAL YNYDGKEPGD LKFSKGDIII LRRQVDENWY HGEMGGVHGF
FPTNFVQVIK PLPQPPPQCK ALYDFELKDK EADKDCLPFS KDDILTVIRR VDENWAEGML
GDKIGIFPIS YVEFNSAARQ LIELDKPSEG GGDSSEGPSS SSSGPQANGS QKAPGEKKNS
KKRHSFTSLT MSHKPCLAPP PQRHSMEISG PVLISSSNPT AAARIGELSG GLSSSAPSQV
HICTTGLIVT PPPSSPVTTA TVFTFPPETS YASIPVDALP PPPPPPPQSQ SSVVGAAALN
AGQRPSPAAG DQSGRQRPTV YVAMFPYSPR KEDELELRKG EMFLVLERCQ DGWFKGTSMH
TGKIGVFPGN YMSPVSRTVS GSSQPKVPLT LCSQAGRGVT IVSPSSALGS MDLSKPLPVC
PNATPSCSLP AAVVTAAHLP TGQHPKVLMH VTSQMTVNQA RNAVRTAVSH SQDRPTAAVT
PIQSHNPVAY LPSTAVVLQA SPVLNSSSGC SSARVGVALG CAAASLTPPN VSAASLDTDA
MRPVPMVALP VNAGSTKPLG AASNHGVACR LDKDCKREKK GLLKLLSNKK KLRPSPPSSP
TLEAEQSVSM ELPQGAVGPE MALSGSAGHN GRIGACPMDS ELSMSSSSSN TDAVTHRSSP
QDNTAPIAPP PRQPCSSLLS MQHDGRPIVC ERYRVVVSYP PQSEAELELK EGDIVFVHKK
REDGWFKGTL QRNGRTGLFP GSFVDSI
