SH3R1_XENTR
ID SH3R1_XENTR Reviewed; 861 AA.
AC Q28E95;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=TNeu006c09.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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:Q6NRD3, 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}.
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DR EMBL; CR848380; CAJ83039.1; -; mRNA.
DR RefSeq; NP_001015973.1; NM_001015973.2.
DR AlphaFoldDB; Q28E95; -.
DR SMR; Q28E95; -.
DR STRING; 8364.ENSXETP00000010793; -.
DR PaxDb; Q28E95; -.
DR GeneID; 548727; -.
DR KEGG; xtr:548727; -.
DR CTD; 57630; -.
DR Xenbase; XB-GENE-950805; sh3rf1.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; Q28E95; -.
DR OMA; LVCERYR; -.
DR OrthoDB; 291531at2759; -.
DR TreeFam; TF105571; -.
DR Reactome; R-XTR-9013424; RHOV GTPase cycle.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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..861
FT /note="E3 ubiquitin-protein ligase SH3RF1"
FT /id="PRO_0000334157"
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 435..496
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 802..861
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 268..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 91754 MW; B1E872D84E157C4D CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VSSRNELRCP ECRTLVECGV
DELPSNILLV RLLDGIKQRP RKAGVGGSAG NSTNVLRAQG SLTTNCGLND AQNIHGGQQR
IQARSPPVRG VPQLPCAKAL YNYEGKEPGD LKFNKGDIIV LRRQVDENWY HGEINGIHGF
FPTNFVQIIK PLPQPPPQCK ALYDFEVKDK EADKDCLPFL KDDILTVIRR VDENWAEGML
GDKIGIFPIS YVEFNSAAKQ LIELDKPSGV DTGEGSSGTT HSSNSQKQAD AKKNTKKRHS
FTSLTMSNKS SQSVQNRHSM EISPPVLISS SNPTAAARIS ELTGLSCSAP SQVHISTTGL
IVTPPPSSPV VSGPAFTFPP EVTYQAALGD LNPPLLPPPP LATPVITSTS SGAAAAVQRS
ISGPAEQVTH LRTSTRPSVF VAIYPYIPRK EDELELRKGE MFLVFERCQD GWFKGTSMHT
SKIGVFPGNY VAPVTRALTT ATPAKVAMAT ASSSNVVNLV TPTPPGAPCQ KLQGNGAEFA
KTVSTNGVPP AGIPGSHIQS SPQAKVLLHM SGQMTVNQAR NAVRTAAAHS QDRPTAAVTP
IQAQIPSASV LPQQAATSQQ MPPPLSGPAA YINAAMNISR PSVPVASAAS SSVSSAAFET
ECNWKSGSGL AACSFPENVS APLNSAANKQ DKDSKKEKKG LLKLLSGAST KRKPRSSPPH
SPTQELEQTN SEAALEGAVG PDILPVNGNG RVASCTVDCD LVSASALVQD NRKPASLDTN
VPIAPPPRQP CSSLGTVLND SRPCERYRVV VSYPPQSEAE LELKEGDIVF VHKKREDGWF
KGTLQRNGKT GLFPGSFVEN I
