ID A0A1S3G1U7_DIPOR Unreviewed; 881 AA.
AC A0A1S3G1U7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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|RefSeq:XP_012882032.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012882032.1};
RN [1] {ECO:0000313|RefSeq:XP_012882032.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012882032.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012882032.1; XM_013026578.1.
DR AlphaFoldDB; A0A1S3G1U7; -.
DR STRING; 10020.ENSDORP00000004145; -.
DR GeneID; 105993334; -.
DR CTD; 57630; -.
DR OMA; NMIIAPS; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000081671; 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; cd11926; SH3_SH3RF1_3; 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:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 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:UP000081671};
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 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 133..192
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 195..258
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 445..506
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 822..881
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 268..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 92348 MW; 867387E11D775303 CRC64;
MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI LGSRNELRCP ECRTLVGSGV
EELPSNILLV RLLDGIKQRP WKPGPGGGSG TNCTNALRAQ GSTANCNAKD LQSSQGGQQP
RVQAWSPPVR GIPQLPCAKA LYNYEGKEPG DLKFSKGDII ILRRQVDENW YHGEVNGVHG
FFPTNFVQII KPLPQPPPQC KALYDFEVKD KEADKDCLPF AKDDVLTVIR RVDENWAEGM
LADKIGIFPI SYVEFNSAAK QLIEWDKPPT AGGDAGECTS AAVQGSAAPK HSDTKKNTKK
RHSFTSLTMA SKSSQASQHR HSMEISPPVL ISSSNPTAAA RISELSGLSC SAPSQVHIST
TGLIVTPPPS SPVTTGSAFT FPSDVSYQAA LGTMNPPLPP PPLLAATVLA STPPGSAAAA
AAATGVGPRP GTGPTDQIAH LRPQSRPSVY VAIYPYTPRK EDELELRKGE MFLVFERCQD
GWFKGTSMHT SKIGVFPGNY VAPVTRTVTN ASQAKVPVST AGQTSRVVTM VSPSSAGAPA
PKLQGNGVAG SPSVVPTAVV SAAHIQTSPQ AKVLLQMTGQ MTVNQARNAV RTVAAHNQER
PTAAVTPIQV QNTTCLGLAP VGLPHHSLAS PQPLPAMAGA AAAAAAAAGG ISRASAPLAS
SSITAACLET EPSGRTVTIL PGLPTSPDNV SSACGNSSTS KPDKDSKKEK KGLLKLLSGA
STKRKPRVSP PASPTLDMDL GGGELFLQGA VGPELPLGGS HGRTNSCSMD GEGTATGAAG
AASVQDAFHR KTSSLDSAVP IAPPPRQACS SLGPVLNESR PVVCERHRVV VSYPPQSEAE
LELKEGDIVF VHKKREDGWF KGTLQRNGKT GLFPGSFVEN I
//
