ID M3Y8B8_MUSPF Unreviewed; 880 AA.
AC M3Y8B8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
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};
GN Name=SH3RF1 {ECO:0000313|Ensembl:ENSMPUP00000007575.1,
GN ECO:0000313|RefSeq:XP_004758169.1, ECO:0000313|RefSeq:XP_012914636.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007575.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007575.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004758169.1, ECO:0000313|RefSeq:XP_012914636.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004758169.1,
RC ECO:0000313|RefSeq:XP_012914636.1};
RG RefSeq;
RL Submitted (SEP-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 EMBL; AEYP01045453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01045461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004758169.1; XM_004758112.2.
DR RefSeq; XP_004758170.1; XM_004758113.2.
DR RefSeq; XP_012914636.1; XM_013059182.1.
DR STRING; 9669.ENSMPUP00000007575; -.
DR Ensembl; ENSMPUT00000007696.1; ENSMPUP00000007575.1; ENSMPUG00000007630.1.
DR GeneID; 101683084; -.
DR KEGG; mpuf:101683084; -.
DR CTD; 57630; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155875; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR OMA; HLICARQ; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR CDD; cd16748; RING-HC_SH3RF1; 1.
DR CDD; cd11930; SH3_SH3RF1_2; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF114; UBP4-INTERACTOR SFP47; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF13923; zf-C3HC4_2; 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:UP000000715};
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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
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 134..193
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 196..259
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 443..504
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 821..880
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 275..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 92815 MW; 8D366485023312BB CRC64;
MDESSLLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
EELPSNILLV RLLDGIKQRP WKPGPGGGSG TNCTNALRAQ SNTVANCSSK DLQSSQGGQQ
PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVNGIH
GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
MLADKIGIFP ISYVEFNSTA KQLIEWDKPP VPGVDAGECT SAAAQSSNAP KHSDTKKNTK
KRHSFTSLTM ASKSSQASQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS
TTGLIVTPPP SSPVTTGPSF TFPSDVPYPA ALGTMNPPLP PPPLLASTPP GAATTVAAAA
AAGMGPRPTA GPSDQIAHLR PQTRPSVYVA IYPYTPRKED ELELRKGEMF LVFERCQDGW
FKGTSMHTSK IGVFPGNYVA PVTRTVTNAS QAKVPMSTAG QTSRGVTIVS PSTAGGPTQK
LQGNGMAGSP SVVPTAVVSA AHIQTSPQAK VFLHMTGQMT VNQARSAVRT VAAHNQERPT
AAVTPIQVQN TACLGAASVG LPHHPLASPQ LPSPMGGPAT HMAAINMGRV SAPLACAAAA
SLTSANITTA SLESEPVGRA VTILPGLPTS PDSASLACGN SSATKPDKDN KKEKKGLLKL
LSGASTKRKP RASPPASPTL EVELGGCELP LQGAVGPELP LGGAHGRAGS CPTDGEGPAA
FVAQDALHRK TSSLDSAVPI APPPRQPCSS LGPVMNESRP LVCERHRVVV SYPPQSEAEL
ELKEGDIVFV HKKREDGWFK GTLQRNGKTG LFPGSFVENI
//