ID V8NN64_OPHHA Unreviewed; 871 AA.
AC V8NN64;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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};
DE Flags: Fragment;
GN Name=SH3RF1 {ECO:0000313|EMBL:ETE63734.1};
GN ORFNames=L345_10498 {ECO:0000313|EMBL:ETE63734.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE63734.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE63734.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE63734.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE63734.1}.
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DR EMBL; AZIM01002592; ETE63734.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NN64; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16748; RING-HC_SH3RF1; 1.
DR CDD; cd11927; SH3_SH3RF1_1; 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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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:UP000018936};
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 130..189
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 192..255
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 440..501
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 812..871
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 267..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE63734.1"
SQ SEQUENCE 871 AA; 94025 MW; 344C0E83F2A15213 CRC64;
MDESVLLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VSSRNELRCP ECRTLVDCNV
DDLPNNILLV RLLDGIKQRP QKLTNLMTCT NLLRAQTSTV ANCIQKDLHS SQSAQQQRVQ
ARSPPVRGVP QLPCAKALYN YEGKEPGDLK FNKGDIIILR RQVDENWYHG EVNGIHGFFP
TNFVQIIKPL PQPPPQCKAL YDFEVKDKEA DKDCLPFSKD DILTVIRRVD ENWAEGMLAD
KIGIFPISYV EFNSTAKQLI ELDKPSVSTV DSGEGTSGTS HCNSVQKHTD VKKNTKKRHS
FTSLTMSNKA SQSSQNRHSV EISPPVLISS SNPTAAARIT ELSGLSCSAP SQVHISTTGL
IVTPPPSSPV TTGHSFTFPP EVTYQAAFAV SSINPPLPPP PPPVLSAAII ASNSTCLPSG
SIQKSTSALT EQISHLRAQT RPSVYIAIYP YTPRKEDELE LRKGEMFLVF ERCQDGWFKG
TSMHTSKIGV FPGNYVAPVT RPMTSASQAK IPVSTAGQTG RVVTMVNAST AGGTVQKLQG
NGVTVTSDTI PTVSAAHIQK SPQSKIIMHM SSQMTLNQAR NAVRTVAIHS QERPTATVTP
IQTQNSACLI PAAVIIPHHP VASQQLQPQF SNAAAYITAV NINRTNVPLA CTTSSLSSPS
TSVSVDGDSS GKIVTVHTGA PASPENTLTA GGTPTMSKTE RDGKKEKKGL LKLLSGASTK
RKLRASPPSS PTLEVELATT ELSLQGAVGP EIPSISGQGR ADTCSMDSES PTIVLENTHC
KTSSLDSNIP VVPPPRQPCS SLAPVSNESR SVIYERYRVV VSYPPQSEAE LELKEGDVVF
VHKKHEDGWF KGTLQRNGKT GLFPGSFVES I
//
