ID W5L098_ASTMX Unreviewed; 711 AA.
AC W5L098;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000013260.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000013260.2}
RP IDENTIFICATION.
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 AlphaFoldDB; W5L098; -.
DR Ensembl; ENSAMXT00000013260.2; ENSAMXP00000013260.2; ENSAMXG00000033345.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158373; -.
DR HOGENOM; CLU_013137_19_3_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000033345; Expressed in brain and 10 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19848; Bbox1_TRIM36_C-I; 1.
DR CDD; cd19778; Bbox2_TRIM36_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16756; RING-HC_TRIM36_C-I; 1.
DR CDD; cd12894; SPRY_PRY_TRIM36; 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; 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; IPR040859; Midline-1_COS.
DR InterPro; IPR035727; SPRY/PRY_TRIM36.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR047066; TRIM36_Bbox1_Zfn.
DR InterPro; IPR047065; TRIM36_Bbox2_Zfn.
DR InterPro; IPR027726; Trim36_HC-RING.
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:SF18; E3 UBIQUITIN-PROTEIN LIGASE TRIM36; 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; SM00184; RING; 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:UP000018467};
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 13..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 188..230
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 337..394
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 396..494
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 479..707
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 252..286
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 80291 MW; D5C2EBFCCAFBA260 CRC64;
FTGTNSDKRE LICPICKELF THPLILPCQH SVCHKCVKEL LMLNHDDSFS TDAGSECSNP
GSPRSRVPSP SMERLDRLVR SGARSSVTPR VTTFPCPGCQ HDIDLGERGI SMLFRNFTLE
SIVERYRQAA RAAMAIMCNM CKPPVQEATK SCMDCKASYC NECFKLHHPW GTPKAQHEYV
GPTTNFRPKV LMCPEHEMEK VNMYCEVCRR PVCHLCKLGG SHANHKVTSM SSAYKILKEK
LSKSIHYLIS KEDQVRTQIT ELEVLIRETE ENGQLAERRA NEHFEELFEI LQEKKTEMLR
SIAQSRNRRM DKLRSQVEEY QGMLENSGLV GYAQEVLKET DQSCFVQTAK QLHVRVQKAT
ESLKTFQAAA SPSFDEFALD TSKEECLLKD LSFGGVPDPP MIDLSQSRVY NEGLIHWRLP
EDSLPTDHHV LEYRKEAAED EEKSPWQTTD RVFGSSAVVC DLDSNCRYAF RVRSCRNTIY
SPYSPAVSFH TPPAPVFGFL FNEKCGFSAE RLILSKRRDS VESVAGMAFL LAAERVQTGS
YICLDYIIGD TGISHGRHYW AFRVEPSSYL VKVGVASDSK LIEWFHNPRD TSSPRYDHDS
GHDSGSEDTC YELSQPFTLI TMGMGKLFIP KASVSAAAGD HGNRVLPLPQ RIGVCLDYDA
GHVFFYDADT MRCLYERQVD CSGTMYPAFG LMGGGAVHLE EFITAKRLSY M
//
