ID G1T389_RABIT Unreviewed; 746 AA.
AC G1T389;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MID2 {ECO:0000313|Ensembl:ENSOCUP00000010681.4};
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:ENSOCUP00000010681.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010681.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010681.4,
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:ENSOCUP00000010681.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010681.4};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; AAGW02041286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02041287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02041288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017205334.1; XM_017349845.1.
DR AlphaFoldDB; G1T389; -.
DR SMR; G1T389; -.
DR STRING; 9986.ENSOCUP00000010681; -.
DR PaxDb; 9986-ENSOCUP00000010681; -.
DR Ensembl; ENSOCUT00000012409.4; ENSOCUP00000010681.4; ENSOCUG00000012407.4.
DR GeneID; 100358558; -.
DR KEGG; ocu:100358558; -.
DR CTD; 11043; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159460; -.
DR HOGENOM; CLU_013137_19_4_1; -.
DR InParanoid; G1T389; -.
DR OrthoDB; 5383069at2759; -.
DR TreeFam; TF333654; -.
DR Proteomes; UP000001811; Chromosome X.
DR Bgee; ENSOCUG00000012407; Expressed in upper lobe of left lung and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0035372; P:protein localization to microtubule; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR CDD; cd19837; Bbox1_MID2_C-I; 1.
DR CDD; cd19823; Bbox2_MID2_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16754; RING-HC_MID2; 1.
DR CDD; cd13739; SPRY_PRY_TRIM1; 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; IPR003879; Butyrophylin_SPRY.
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; IPR047064; MID2_Bbox1_Zfn.
DR InterPro; IPR047063; MID2_Bbox2_Zfn.
DR InterPro; IPR033491; MID2_HC-RING.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR035752; SPRY/PRY_TRIM1.
DR InterPro; IPR003877; SPRY_dom.
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:SF12; E3 UBIQUITIN-PROTEIN LIGASE MID2-RELATED; 1.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
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; PS50119; ZF_BBOX; 1.
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 Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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 41..91
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 201..243
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 351..410
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 527..720
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 244..285
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 746 AA; 84237 MW; EAD696C8151902CE CRC64;
MSTGLTATES GRGESPASVV VNASAGLFPL KMETLESELT CPICLELFED PLLLPCAHSL
CFNCAHRILV SSCSSGESIE PITAFQCPTC RYVISLNHRG LDGLKRNVTL QNIIDRFQKA
SVSGPNSPSE SRRERTYRPS TAMSSERIAC QFCEQDPPRD AVKTCITCEV SYCDRCLRAT
HPNKKPFTSH RLVEPVPDTH LRGITCLDHE NEKVNMYCVS DDQLICALCK LVGRHRDHQV
ASLNDRFEKL KQTLEMNLTN LVKRNSELEN QMAKLIQICQ QVEVNTAMHE AKLMEECDEL
IEIIQQRKQM IAVKIKETKV MKLRKLAQQV ANCRQCLERS TVLINQAEHI LKENDQARFL
QSAKNIAERV AMATASSQVL IPDINFNDAF ENFALDFSRE KKLLEGLDYL TAPNPPSIRE
ELCTASHDTI TVHWISDDEF SISSYELQYT IFTGQANFIS KSWCSWGLWP EIRKCKEAVS
CSRLAGAPRG LYNSVDSWMI VPNIKQNHYT VHGLQSGTRY IFIVKAINQA GSRNSEPTRL
KTNSQPFKLD PKMTHKKLKI SNDGLQMEKD ESSLKKSHTP ERFSGTGCYG AAGNIFIDSG
CHYWEVVMGS STWYAIGIAY KSAPKNEWIG KNASSWVFSR CNSNFVVRHN NKEMLVDVPP
QLKRLGVLLD YDNNMLSFYD PANSLHLHTF DVTFILPVCP TFTIWNKSLM ILSGLPAPDF
IDYPERQECN CRPQESPYVS GVKACH
//
