ID W5UCY6_ICTPU Unreviewed; 677 AA.
AC W5UCY6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1 {ECO:0000256|ARBA:ARBA00013586};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein Midline-1 {ECO:0000256|ARBA:ARBA00031380};
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000256|ARBA:ARBA00033203};
DE AltName: Full=Tripartite motif-containing protein 18 {ECO:0000256|ARBA:ARBA00032675};
GN Name=MID1 {ECO:0000313|EMBL:AHH39803.1};
GN Synonyms=mid1 {ECO:0000313|RefSeq:XP_017313548.1,
GN ECO:0000313|RefSeq:XP_047007131.1};
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|EMBL:AHH39803.1};
RN [1] {ECO:0000313|EMBL:AHH39803.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH39803.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017313548.1, ECO:0000313|RefSeq:XP_047007131.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017313548.1,
RC ECO:0000313|RefSeq:XP_047007131.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its
CC monoubiquitination, which results in deprotection of the catalytic
CC subunit of protein phosphatase PP2A, and its subsequent degradation by
CC polyubiquitination. {ECO:0000256|ARBA:ARBA00002369}.
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; JT412321; AHH39803.1; -; mRNA.
DR RefSeq; XP_017313548.1; XM_017458059.3.
DR RefSeq; XP_047007131.1; XM_047151175.2.
DR Ensembl; ENSIPUT00000019577; ENSIPUP00000018781; ENSIPUG00000012759.
DR Ensembl; ENSIPUT00000019584; ENSIPUP00000018787; ENSIPUG00000012759.
DR GeneID; 108258982; -.
DR KEGG; ipu:108258982; -.
DR CTD; 4281; -.
DR OMA; MEACKTC; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000221080; Chromosome 26.
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; cd19836; Bbox1_MID1_C-I; 1.
DR CDD; cd19822; Bbox2_MID1_C-I; 1.
DR CDD; cd00063; FN3; 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; IPR047095; MID1_Bbox1_Zfn.
DR InterPro; IPR027727; MID1_Bbox2_Zfn.
DR InterPro; IPR040859; Midline-1_COS.
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:SF23; E3 UBIQUITIN-PROTEIN LIGASE MIDLINE-1; 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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 180..222
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 330..389
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 391..494
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 476..669
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 75767 MW; D5AF49C3CC1C5D78 CRC64;
MESLESELTC PICLELFEDP LLLPCAHSLC FNCARRILVS HCTSGEPVDA ICAFQCPTCR
YAISLSPQRG LDALKRNVTL QNIIDRVQRA STSATLLLSS SGHSSPGDSP LGAMTTATAP
SSPTELVQCQ FCEQEPPQCA VKTCVTCEVS YCEECLRATH PNKKPFTGHR LIEPLPDSHL
RGLQCLEHEE EKVNMYCVTD EQLICSLCKL VGRHRDHQVA ALHERYEKLK QTLDSNLSNL
IKRSNELESL MGKLIQTCQH VEMNASRQEG KLMEECDILI SLIQERRQII GAKIKEGKAV
RLRKLAQQIA NCKQCIERSS ALITQADQML KETDHARFLQ TAKSISERVS MATASSQVLI
PEINLTDTFD TFALDFTREK KMLESLDYLT APSPPGIREE LCTASYDTIT VHWTSDDEFS
VVSYELQYTI YTGQSNIVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FIVKAINQAG
SRSSEPGTLK TNSQPFKLDP KSAHRKLKLS HDNLTVERDE ISSKKSHGQE RFSSQSSYGV
IGNVYIDSGR HYWEALIGGS TWYAVGIAYK SAPKHEWIGK NPLSWVLCRC NNSWVVRHNS
KEMAIDPSPH LRRVGVLLDY DAGSLAFYDA VSSQHLHTFH ITFTQPVCPV FNVWNKCLTV
LTGLPIPDHL EGVEAFN
//
