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Database: UniProt
Entry: G1U127_RABIT
LinkDB: G1U127_RABIT
Original site: G1U127_RABIT 
ID   G1U127_RABIT            Unreviewed;       896 AA.
AC   G1U127;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
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:ENSOCUP00000023060.1};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023060.1, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000023060.1, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000023060.1,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000023060.1}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023060.1};
RG   Ensembl;
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   EMBL; AAGW02011155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02011156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02011157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02011158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02011159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002709514.1; XM_002709468.3.
DR   AlphaFoldDB; G1U127; -.
DR   SMR; G1U127; -.
DR   STRING; 9986.ENSOCUP00000023060; -.
DR   PaxDb; 9986-ENSOCUP00000023060; -.
DR   Ensembl; ENSOCUT00000031902.3; ENSOCUP00000023060.1; ENSOCUG00000003098.4.
DR   GeneID; 100354589; -.
DR   KEGG; ocu:100354589; -.
DR   CTD; 57630; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000155875; -.
DR   HOGENOM; CLU_015769_1_0_1; -.
DR   InParanoid; G1U127; -.
DR   OMA; NMIIAPS; -.
DR   OrthoDB; 5407056at2759; -.
DR   TreeFam; TF105571; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001811; Chromosome 2.
DR   Bgee; ENSOCUG00000003098; Expressed in frontal cortex and 14 other cell types or tissues.
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:UP000001811};
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          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          453..514
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          837..896
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          268..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   896 AA;  93674 MW;  F29549895B2C8A96 CRC64;
     MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
     EELPSNILLV RLLDGIKQRP WKPGPSGGSG TNCTNALRAQ GSTVANCSSK DLQSSQGGQQ
     PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVNGVH
     GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
     MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGTEAGECT SAAAQSSTAP KHSDTKKNTK
     KRHSFTSLTM ANKSSQACQH RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS
     TTGLIVTPPP SSPVTTGPSF TFPSDVPYQA ALGTMNPPLP PPPLLAATVV ASTPPGAAAA
     AAAAAAAAAA ASGMGPRPVA GSTDQIAHLR PQTRPSVYVA IYPYTPRKED ELELRKGEMF
     LVFERCQDGW FKGTSMHTSK IGVFPGNYVA PVTRAVTNAS QAKVPMSTAA QTSRGVTMVS
     PSTAGGPVQK LQGNGVAGNP SMVPTAVVSA AHLQTSPQAK VLLHMTGQMT VNQARNAVRT
     VAAHSQERPT AAVTPIQVQN AGCLGPASGG LPHHSLASPQ PPPPMAASAA HVAAVSISRA
     NAPLACAAAA SLTSPGVTTA SLETEPSGRA VTILPGLPAS SDSALSACGN SSATKPDKDS
     KKEKKGLLKL LSGASTKRKP RVSPPASPTL EVELGGSELP LQGAVGPELP LGGGHGRAGS
     CALDGDGPVA ASAVGAALAQ DAFHRKTSSL DSAVPIAPPP RQACSSLGPV MNESRPVVCE
     RHRVVVSYPP QSEAELELKE GDIVFVHKKR EDGWFKGTLQ RNGKTGLFPG SFVENI
//
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