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Database: UniProt
Entry: M3Y1J1_MUSPF
LinkDB: M3Y1J1_MUSPF
Original site: M3Y1J1_MUSPF 
ID   M3Y1J1_MUSPF            Unreviewed;       795 AA.
AC   M3Y1J1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=TRIM9 {ECO:0000313|Ensembl:ENSMPUP00000005192.1,
GN   ECO:0000313|RefSeq:XP_012911571.1};
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:ENSMPUP00000005192.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000005192.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_012911571.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_012911571.1};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   EMBL; AEYP01003553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01003554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012911571.1; XM_013056117.2.
DR   STRING; 9669.ENSMPUP00000005192; -.
DR   Ensembl; ENSMPUT00000005280.1; ENSMPUP00000005192.1; ENSMPUG00000005230.1.
DR   GeneID; 101683806; -.
DR   CTD; 114088; -.
DR   eggNOG; KOG4367; Eukaryota.
DR   GeneTree; ENSGT00940000154071; -.
DR   HOGENOM; CLU_013137_19_2_1; -.
DR   OMA; PDTICTI; -.
DR   OrthoDB; 5383069at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19843; Bbox1_TRIM9_C-I; 1.
DR   CDD; cd19826; Bbox2_TRIM9_C-I; 1.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR049582; TRIM9_Bbox1.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR   PANTHER; PTHR24099:SF13; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00024}.
FT   DOMAIN          10..50
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          163..212
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          224..266
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          374..432
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   DOMAIN          440..535
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          602..787
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          288..344
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   795 AA;  88815 MW;  FFD15EB94D9FA8EC CRC64;
     MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSR RASGSGVSDY
     DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV
     PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
     MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
     CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
     MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
     RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
     PLLQSIHQLD FVQMKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PAEGYILELD
     DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARIKAFNKTG VSQYSKTLVL QTSEDTDSEE
     QTLPFPVPSE RLPLRRMSPF SSTLNLQPSF PGRSYFDIRS SPHQLSLHSS LQSLNAPGCN
     FEPQSAPYSQ LVDIKKLLAV AWFAFDPGSA HADIIFSNDN LTVTCSSYDD RVVLGKTGFS
     KGVHYWELTV DRYDNHPDPA FGVARMDVMK DVMLGKDDKA WAMYVDNHRS WFMHNNSHTN
     RTEGGITKGA TIGVLLDLNR KTLTFFINDE QQGPIAFENV EGLFFPAVSL NRNVQVTLHT
     GLPVPDFYSS RASIA
//
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