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Database: UniProt
Entry: A0A2D0RHS5_ICTPU
LinkDB: A0A2D0RHS5_ICTPU
Original site: A0A2D0RHS5_ICTPU 
ID   A0A2D0RHS5_ICTPU        Unreviewed;       719 AA.
AC   A0A2D0RHS5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
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|RefSeq:XP_017330084.1,
GN   ECO:0000313|RefSeq:XP_017330085.1, ECO:0000313|RefSeq:XP_017330087.1,
GN   ECO:0000313|RefSeq:XP_017330088.1, ECO:0000313|RefSeq:XP_053538000.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017330087.1};
RN   [1] {ECO:0000313|RefSeq:XP_017330084.1, ECO:0000313|RefSeq:XP_017330085.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017330084.1,
RC   ECO:0000313|RefSeq:XP_017330085.1};
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   RefSeq; XP_017330084.1; XM_017474595.3.
DR   RefSeq; XP_017330085.1; XM_017474596.3.
DR   RefSeq; XP_017330086.1; XM_017474597.1.
DR   RefSeq; XP_017330087.1; XM_017474598.3.
DR   RefSeq; XP_017330088.1; XM_017474599.3.
DR   RefSeq; XP_053538000.1; XM_053682025.1.
DR   Ensembl; ENSIPUT00000000824; ENSIPUP00000000769; ENSIPUG00000000550.
DR   GeneID; 108269068; -.
DR   KEGG; ipu:108269068; -.
DR   CTD; 11043; -.
DR   OrthoDB; 5383069at2759; -.
DR   Proteomes; UP000221080; Chromosome 8.
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; cd00063; FN3; 1.
DR   CDD; cd13739; SPRY_PRY_TRIM1; 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; 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   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          182..224
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          354..413
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   DOMAIN          415..518
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          500..693
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          88..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          254..288
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        699..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  80387 MW;  10C2976BA238F9E5 CRC64;
     METLESELTC PICLELFEDP LLLPCAHSLC FSCAHRILVS HCSGAKPLES VSAFQCPTCR
     HVITLSPRGL DGLRRNVTLQ NIIDRFQKAS FSGPGSPNES RLRPPPRPRS ATPTGGSANG
     SAMSAELRVP CQFCEQEPPR DAVKTCATCQ ASYCERCLRA THPNKKPFTS HRLLEPAGDG
     HLRGLACLEH DSETVSLYCA TDEQLICTLC KLVGRHREHH VASLSERFDK LKGFHPSPGR
     VSEAVMEASK TSAAQTLENN LTNLVKRNSE LENQMAKLIQ ICQQVEVNTA MHEAKLVEEC
     DELVEIIRQR KQVIAVKIKE SKVMKLRKLA QQIANCRQCL ERSSALITQA EQSLKENDHA
     RFLQTARNVA ERVAMATASS QVLIPDVNLN EAFDNFALDF SREKKILEGL DYLTAPNPPS
     IRDELCTASH DTITVHWTSE DEFSVTSYEL QYTIYTGQTN FISLYNSVDS WMIVPNIKQN
     HYTVHGLQSG TRYIFFVKAI NQAGSRNSEP ARLKTNSQPF KLDPKTAHKK LRLSNDCLTM
     EKDESSLKKS HTPERFSGTG SYGAAGNVFI DSGCHYWEVL LGASTWYTVG VAYKSAPKNE
     WNGKNSSSWV FSRCNNNFLV RHNSKEMLVE ASLQLRRLGV LLDYDNNTLS FYDAMNSQHL
     HTFDISFLLP VAPTFMISNK SLMILSGLPV PDFVDCPEQQ DGSSRQHESP YGLTMKSCN
//
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