EVI1B_XENLA
ID EVI1B_XENLA Reviewed; 1050 AA.
AC B7ZRM8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=MDS1 and EVI1 complex locus protein EVI1-B;
DE AltName: Full=Ecotropic virus integration site 1 protein homolog-B;
GN Name=mecom-b; Synonyms=evi1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAI70222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor during pronephros development.
CC Plays a role in regionalization of the pronephros; may promote
CC formation of the distal tubule and duct over formation of the glomus
CC and proximal tubule (By similarity). {ECO:0000250|UniProtKB:B7ZRU9}.
CC -!- SUBUNIT: Homooligomer. Interacts with ctbp.
CC {ECO:0000250|UniProtKB:B7ZRU9, ECO:0000250|UniProtKB:Q03112}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03112}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q03112}.
CC -!- DOMAIN: The CTBP-binding motifs and the N-terminal group of zinc
CC fingers are required for repressor activity in the pronephros.
CC {ECO:0000250|UniProtKB:B7ZRU9}.
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DR EMBL; BC170222; AAI70222.1; -; mRNA.
DR RefSeq; NP_001154861.1; NM_001161389.2.
DR AlphaFoldDB; B7ZRM8; -.
DR PRIDE; B7ZRM8; -.
DR GeneID; 100301954; -.
DR KEGG; xla:100301954; -.
DR CTD; 100301954; -.
DR Xenbase; XB-GENE-6448217; mecom.S.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 100301954; Expressed in stomach and 12 other tissues.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039013; P:pronephric distal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0039022; P:pronephric duct development; ISS:UniProtKB.
DR GO; GO:0072196; P:proximal/distal pattern formation involved in pronephric nephron development; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1050
FT /note="MDS1 and EVI1 complex locus protein EVI1-B"
FT /id="PRO_0000392431"
FT ZN_FING 21..48
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 75..97
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 103..125
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 131..155
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 161..183
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 189..211
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 218..240
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 731..753
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 759..782
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 788..810
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 371..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 420..433
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 551..555
FT /note="CTBP-binding motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q03112"
FT MOTIF 582..586
FT /note="CTBP-binding motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q03112"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 118703 MW; 2868F46A14ADCBCC CRC64;
MKSEDYTYAR MAPDIHEERQ YHCEECDQLF ESKTELSNHQ KYSCGTPHSA FSLVENSFPP
ILNDDSDLTE MQHAHECKEC DQVFPDMQSL EKHLLSHTEE REYKCDQCPK AFNWKSNLIR
HQMSHDTGKH YECENCSKQV FTDPSNLQRH IRSQHVGARA HACSECGKTF ATSSGLKQHK
HIHSSVKPFV CEVCHKSYTQ FSNLCRHKRM HADCRTQIKC KDCGQMFSTT SSLNKHRRFC
EGKNHFTAGG LFRQGISLPG NTAMDKVSMI GMNHAGLADY FGASRHAAGL TFPTAPGFPF
SFPGLFPSSL YHRPHLIPPA SPVKGLPGVE QSNKSQSLHV NQPQVLPATQ DILKALNKHH
SVDENKALEF ITENNLNQRP HEKVSDHSES TDLDDVSTPS GSDLETTSGS DLESDIESDK
DKLKENGKLY KDKISPLQSL AALNSKREYN NHSVFSPCLE EQTVTGAVND SIKAIASIAE
KYFGSTGLVG LPDKKGTSLP YPSMFPLPFF PAISQSMYTF PERDVRPLPL KVEPESPKES
KKVQKGTTES AFDLTTKCKE EKASPNAPSK SSAPTSSKHE QPLDLSMGSR SRATTTKQTE
SRKNHIFGEK KDIDSELKKT SEHFLQHARP APFFMDPIYR VEKRKTMDPL EVLKEKYLRS
SSGFLFHPQF PLPDQRTWMS AIENMAEKLE SFNALKPEAN DLIQSVPSMF SFRASSSALP
ENLLRKGKER YTCRYCGKIF PRSANLTRHL RTHTGEQPYR CKYCDRSFSI SSNLQRHIRN
IHNKEKPFKC HLCDRCFGQQ TNLDRHLKKH ENGNLSGTAA SSPHSEIEGT GAILEEKEDS
YFNEIRNFIG NNSHNKQSPL NIDERINGSH DKIMLTGQNS DILDDDEIED EAILEDDEES
DIDVKVMKEP NASAMLKNCS DEFEEESKSE VNCKVSPSRH DDDDDDEEED FKKSLSALDH
IRHFTDSLKI RKMDDGQFND AELSPFTASH LTDDLKHPLY RKSKSQTYAM MLSLSDQESM
HPTTHTSSSM WHNLARAAAE STALHSVSHV
