SH3R1_XENLA
ID SH3R1_XENLA Reviewed; 826 AA.
AC Q6NRD3; Q3L1I1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Short=xPOSH;
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=16125690; DOI=10.1016/j.ydbio.2005.07.033;
RA Kim G.-H., Park E., Han J.-K.;
RT "The assembly of POSH-JNK regulates Xenopus anterior neural development.";
RL Dev. Biol. 286:256-269(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) 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 (By similarity). Plays an essential role in the
CC anterior neural development. {ECO:0000250|UniProtKB:Q69ZI1,
CC ECO:0000250|UniProtKB:Q7Z6J0, ECO:0000269|PubMed:16125690}.
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 -!- INTERACTION:
CC Q6NRD3; O14964: HGS; Xeno; NbExp=3; IntAct=EBI-7734031, EBI-740220;
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 -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout early development. Becomes visible in the animal hemisphere
CC of the embryo during the cleavage and blastula stages. At the gastrula
CC stages, expressed broadly throughout the marginal zone and animal pole
CC tissues. At the neurula stages, it shows the restricted expression in
CC dorsal tissue. At later stages, expressed in the cement gland, brain,
CC somite, notochord and pronephros. {ECO:0000269|PubMed:16125690}.
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; AY762093; AAW83119.1; -; mRNA.
DR EMBL; BC070823; AAH70823.1; -; mRNA.
DR RefSeq; NP_001084814.1; NM_001091345.1.
DR AlphaFoldDB; Q6NRD3; -.
DR SMR; Q6NRD3; -.
DR BioGRID; 101221; 3.
DR IntAct; Q6NRD3; 2.
DR MINT; Q6NRD3; -.
DR DNASU; 431855; -.
DR GeneID; 431855; -.
DR KEGG; xla:431855; -.
DR CTD; 431855; -.
DR Xenbase; XB-GENE-950810; sh3rf1.S.
DR OrthoDB; 291531at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 431855; Expressed in egg cell and 19 other tissues.
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:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
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 1: Evidence at protein 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..826
FT /note="E3 ubiquitin-protein ligase SH3RF1"
FT /id="PRO_0000334156"
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 398..459
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 767..826
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 80..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..123
FT /note="Polar residues"
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 673..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 18
FT /note="R -> G (in Ref. 1; AAW83119)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="K -> E (in Ref. 1; AAW83119)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="V -> M (in Ref. 1; AAW83119)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="P -> S (in Ref. 1; AAW83119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 88041 MW; 32C0F09115DC33BF CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VSSRKELRCP ECRTLVECGV
DELPSNILLV RLLDGIRQRP RKAGDGGSAG NSTNALRAQG SVTTNGGLND AQNTQSGQQR
IQARSPPVRG VPQLPCAKAL YNYEGKEPGD LKFNKGDIIV LRRQVDENWY HGEINGIHGF
FPTNFVQIIK PLPQPPPQCK ALYDFEVKDK EADKDCLPFL KDDILTVIRR VDENWAEGML
GDKIGIFPIS YVEFNSAAKQ LIELDKPSGA DTGEGSSGTS HSGNSQKQAD AKKNTKKRHS
FTSLTMSNKS SQSVQNRHSM EISPPVLISS SNPTAAARIS ELTGLSCSAP SQDMNPPLLP
PPPMATPVIT SASSGAAAVA QRNIIGPVEQ VPHLRTSARP SVFIAIYPYI PRKEDELELR
KGEMFLVFER CQDGWFKGTS MHTSKIGVFP GNYVAPVTRA LTTATPAKVA MATATTSNVV
NLVTPTPPGA PCQKLPVSGV EFAKTSSTNG VSPAGVPGCH IQTSPQSKVL LHMSGQMTVN
QARNAVRTAA AHSQDRPTAA VTPIQAQTPA ASALPQQAAA SQQVPPPLSA PAAYINAAMN
ISRPSVPAAS AASSALPTAA FEAESSWKSS SGLSGCSFSE NVSAPLNSAA NKQDKDSKKE
KKGLLKLLSG ASTKRKPRSS PPHSPTQEVE QTNSEAAAAL EGAVGPDIVP VIVNGRAAPC
TVDCDSVSAS TPAQDNRKPA SLDNNIPIAP PPRQPCSSLG SVLNDSRPCE RYRVMVSYPP
QSEAELELKE GDIVFVHKKR EDGWFKGTLQ RNGKTGLFPG SFVENI
