EVI1A_XENLA
ID EVI1A_XENLA Reviewed; 1055 AA.
AC B7ZRU9; Q4JHF9; Q4QSE0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=MDS1 and EVI1 complex locus protein EVI1-A;
DE AltName: Full=Ecotropic virus integration site 1 protein homolog-A;
DE Short=Evi-1 {ECO:0000312|EMBL:AAY22202.1};
DE Short=xEvi-1 {ECO:0000303|PubMed:15905132};
GN Name=mecom-a; Synonyms=evi1 {ECO:0000312|EMBL:AAI70296.1}, evi1-a;
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:0000305, ECO:0000312|EMBL:AAY22202.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:15905132};
RX PubMed=15905132; DOI=10.1016/j.modgep.2005.03.007;
RA Mead P.E., Parganas E., Ohtsuka S., Morishita K., Gamer L., Kuliyev E.,
RA Wright C.V., Ihle J.N.;
RT "Evi-1 expression in Xenopus.";
RL Gene Expr. Patterns 5:601-608(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAY96416.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CTBP, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND DOMAIN.
RC TISSUE=Tadpole head {ECO:0000269|PubMed:16574097};
RX PubMed=16574097; DOI=10.1016/j.ydbio.2006.02.040;
RA Van Campenhout C., Nichane M., Antoniou A., Pendeville H., Bronchain O.J.,
RA Marine J.C., Mazabraud A., Voz M.L., Bellefroid E.J.;
RT "Evi1 is specifically expressed in the distal tubule and duct of the
RT Xenopus pronephros and plays a role in its formation.";
RL Dev. Biol. 294:203-219(2006).
RN [3] {ECO:0000312|EMBL:AAI70296.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=16818449; DOI=10.1242/dev.02458;
RA Taelman V., Van Campenhout C., Soelter M., Pieler T., Bellefroid E.J.;
RT "The Notch-effector HRT1 gene plays a role in glomerular development and
RT patterning of the Xenopus pronephros anlagen.";
RL Development 133:2961-2971(2006).
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. {ECO:0000269|PubMed:16574097}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with ctbp.
CC {ECO:0000250|UniProtKB:Q03112, ECO:0000269|PubMed:16574097}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03112}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q03112}.
CC -!- TISSUE SPECIFICITY: Expressed dynamically during embryonic development;
CC in the developing pronephros, specific areas of the brain (forebrain,
CC midbrain and hindbrain), and in the majority of the visceral arch, and
CC head mesenchyme derived from neural crest cells. Within the pronephros,
CC expressed in the ventroposterior region of the pronephros anlagen from
CC stage 20 (and is absent from the splanchnic layer that forms the
CC glomus), then expression becomes restricted to the distal tubule and
CC duct by the tadpole stage. In adults, expressed in various tissues
CC including kidney, lung, testis, spleen and stomach.
CC {ECO:0000269|PubMed:15905132, ECO:0000269|PubMed:16574097}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults. May be expressed
CC in oocytes. {ECO:0000269|PubMed:15905132, ECO:0000269|PubMed:16574097}.
CC -!- INDUCTION: By retinoic acid (RA) signaling. Repressed by wt1 and by
CC notch signaling. {ECO:0000269|PubMed:16574097,
CC ECO:0000269|PubMed:16818449}.
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:0000269|PubMed:16574097}.
CC -!- CAUTION: Although PubMed:15905132 report high expression throughout
CC oocyte development and throughout embryogenesis, PubMed:16574097 detect
CC no maternal expression, with zygotic expression beginning at stage 20
CC (end of neurulation). {ECO:0000305}.
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DR EMBL; AY939893; AAY22202.1; -; mRNA.
DR EMBL; DQ088677; AAY96416.1; -; mRNA.
DR EMBL; BC170296; AAI70296.1; -; mRNA.
DR RefSeq; NP_001089102.1; NM_001095633.1.
DR RefSeq; NP_001089139.1; NM_001095670.1.
DR AlphaFoldDB; B7ZRU9; -.
DR SMR; B7ZRU9; -.
DR GeneID; 733318; -.
DR GeneID; 734157; -.
DR KEGG; xla:734157; -.
DR CTD; 733318; -.
DR CTD; 734157; -.
DR Xenbase; XB-GENE-980198; mecom.L.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734157; Expressed in kidney 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:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0039013; P:pronephric distal tubule morphogenesis; IMP:UniProtKB.
DR GO; GO:0039022; P:pronephric duct development; IMP:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IEP:UniProtKB.
DR GO; GO:0072196; P:proximal/distal pattern formation involved in pronephric nephron development; IMP: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 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1055
FT /note="MDS1 and EVI1 complex locus protein EVI1-A"
FT /id="PRO_0000392430"
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 734..756
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 762..785
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 791..813
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 422..435
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 554..558
FT /note="CTBP-binding motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q03112"
FT MOTIF 585..589
FT /note="CTBP-binding motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q03112"
FT COMPBIAS 330..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 248
FT /note="A -> T (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="Missing (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> T (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="W -> L (in Ref. 1; AAY22202)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="L -> F (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="S -> L (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="C -> W (in Ref. 2; AAY96416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1055 AA; 118985 MW; D38C5B685ABD4B09 CRC64;
MKSEDYSYAR MAPDIHEERQ YRCEECDQLF ESKTELSDHQ KYPCVTPHSA FSLVENSFPP
SLNDDSDLTE MQHTHECKEC DQVFPDMQSL EKHLLSHTEE REYKCDQCPK AFNWKSNLIR
HQMSHDTGKH YECENCSKQV FTDPSNLQRH IRSQHVGARA HACSDCGKTF ATSSGLKQHK
HIHSSVKPFV CEVCHKSYTQ FSNLCRHKRM HADCRTQIKC KDCGQMFSTT SSLNKHRRFC
EGKNHFAAGG LFGQGISLPG TPAMDKASMI SMNHANAGLA DYFGASRHTA GLTFPTAPGF
PFSFPGLFPS SLYHRPPFIP PASPVKGLPG VEQSSKSQSP HVNQPQVLPA TQDILKALSK
HPSVDENKAL EFITESNLNQ RPHEKISDHS ESSDLDDVST PSGSDLETTS GSDLESDIES
DKDKLKENGK LYKDKMSPLQ SLAALNSKRE YNNHSVFSPC LEEQTAVTGA VNDSIKAIAS
IAEKYFGSTG LVGLPDKKGT TLPYPSMFPL PFFPAFSQSM YTFPDRDVRP VPLKIEPESP
KETKKVQKGK TESPFDLTTK RKEEKASPNV PSKSGAPTSS NHDQPLDLSM GSRSRAATTK
QTEPRKNHIF NEKKDMDPEL PKTSEHCLQH ARPAPFFMDP IYRVEKRKPM DPLEILKEKY
LRPSPGFLFH PQFPMPDQRT WMSAIENMAE KLESFNALKP EANNLIQSVP SMFNFRASSS
ALPENLLRKG KERYTCRYCG KIFPRSANLT RHLRTHTGEQ PYRCKYCDRS FSISSNLQRH
VRNIHNKEKP FKCHLCDRCF GQQTNLDRHL KKHENGNLSG TAASSPHSEI EGTGPILDEK
EDSYFNEIRN FIGNSSHNKQ SPLNSDERIN GSHDKIMLAG QNSDILDDDE DEAILDEDDE
ESDIAVKVMK EPNTSVMLEK CSVDEYEEGG KSEVNSKVSP SRYDDEDDDD DEEEDFKKSL
SALDHIRHFT DSLKMRKMDD GQFNDAELSA FTASHLTDDL KHPLYRKSKS QAYAMMLSLS
DQESLHPTTH TSSSMWHNLA RAAAESTALH SVSHV
