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Database: UniProt
Entry: M3Y8B8_MUSPF
LinkDB: M3Y8B8_MUSPF
Original site: M3Y8B8_MUSPF 
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
//
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