GenomeNet

Database: UniProt
Entry: H0VSW6_CAVPO
LinkDB: H0VSW6_CAVPO
Original site: H0VSW6_CAVPO 
ID   H0VSW6_CAVPO            Unreviewed;       685 AA.
AC   H0VSW6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 78.
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:ENSCPOP00000013736.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013736.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
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:ENSCPOP00000013736.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013736.3};
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; AAKN02040067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02040068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005002766.1; XM_005002709.2.
DR   AlphaFoldDB; H0VSW6; -.
DR   STRING; 10141.ENSCPOP00000013736; -.
DR   Ensembl; ENSCPOT00000015387.3; ENSCPOP00000013736.3; ENSCPOG00000015240.4.
DR   GeneID; 100719594; -.
DR   CTD; 11043; -.
DR   VEuPathDB; HostDB:ENSCPOG00000015240; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000159460; -.
DR   HOGENOM; CLU_013137_19_4_1; -.
DR   InParanoid; H0VSW6; -.
DR   OMA; YRPSTTM; -.
DR   OrthoDB; 5383069at2759; -.
DR   TreeFam; TF333654; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000015240; Expressed in heart left ventricle and 12 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; 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; 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; PF00041; fn3; 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; PS50853; FN3; 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:UP000005447};
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..60
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          170..212
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          320..379
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   DOMAIN          384..484
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          466..659
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          213..254
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   685 AA;  77987 MW;  6AD8FD9FBE5DC60B CRC64;
     METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS NCSSGETIEP LTAFQCPTCR
     YVISLNHRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSEN RRERIYRPSS AMSSERIACQ
     FCEQDPPRDA VKTCITCEVS YCDRCLRATH PNKKPFTSHR LVEPVPDTHL RGITCLDHEN
     EKVNMYCVSD DQLICALCKL VGRHRDHQVA SLNDRFEKLK QTLEMNLTNL VKRNSELENQ
     MAKLIQICQQ VEVNTAMHEA KLMEECDELV EIIQQRKQMI AVKIKETKVM KLRKLAQQVA
     NCRQCLERST VLINQAEHIL KENDQARFLQ SAKNIAERVA MATASSQVLI PDINFNDAFE
     NFALDFSREK KLLEGLDYLT APNPPSIREE LCTASHDTIT VHWISDDEFS ISSYELQYTI
     FTGQANFISL YNSVDSWMIV PNIKQNHYTV HGLQSGTRYI FIVKAINQAG SRNSEPTRLK
     TNSQPFKLDP KMTHRKLKIS NDGLQMEKDE SSLKKSHTPE RFSGTGCYGA AGNIFIDSGC
     HYWEVVMGSS TWYAIGIAYK SAPKNEWIGK NASSWVFSRC NSNFVVRHNN KEMLVDVPPQ
     LKRLGVLLDY DNNMLSFYDP ANSLHLHTFD VTFILPVCPT FTIWNKSLMI LSGLPAPDFI
     DYPERQECNC RPQESPYVSG MKACH
//
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