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CI_DROYA
ID   CI_DROYA                Reviewed;         403 AA.
AC   O77027;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein cubitus interruptus;
DE   Flags: Fragment;
GN   Name=ci;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9611206; DOI=10.1093/genetics/149.2.959;
RA   Takano T.S.;
RT   "Rate variation of DNA sequence evolution in the Drosophila lineages.";
RL   Genetics 149:959-970(1998).
CC   -!- FUNCTION: Involved in segment polarity. Required for the normal
CC       development of the posterior half of each embryonic segment. Engrailed
CC       protein directly represses ci expression in posterior compartment cells
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB005797; BAA33208.1; -; Genomic_DNA.
DR   AlphaFoldDB; O77027; -.
DR   SMR; O77027; -.
DR   STRING; 7245.FBpp0259541; -.
DR   EnsemblMetazoa; FBtr0405326; FBpp0363975; FBgn0022826.
DR   eggNOG; KOG1721; Eukaryota.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0007367; P:segment polarity determination; ISS:UniProtKB.
DR   InterPro; IPR043359; GLI-like.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45718; PTHR45718; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   3: Inferred from homology;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Segmentation polarity protein; Zinc; Zinc-finger.
FT   CHAIN           <1..>403
FT                   /note="Protein cubitus interruptus"
FT                   /id="PRO_0000046918"
FT   ZN_FING         <1..21
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         27..52
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         58..83
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          110..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         403
SQ   SEQUENCE   403 AA;  44089 MW;  467706D7D7E64359 CRC64;
     FEGCFKAYSR LENLKTHLRS HTGEKPYTCE YPGCSKAFSN ASDRAKHQNR THSNEKPYIC
     KAPGCTKRYT DPSSLRKHVK TVHGAEFYAN KKHKGLPLDD VNSRLQRDNS QGRHNLQEHN
     IDSSPCSEDS HIGKILGTSS PSIKSESDIS SSNHQLVNGV RASDGLLTYS PDDLAENLHL
     DDGWNCDDDV DVADLPIVLR AMVNIGSGNA SASAIGGAVL ARQRFRSRLQ TKGINSSTIM
     LCNIPESNRT IGISELNQRI TELKMEPCTA GDIKIPMSTN TAIEVFPEDL LQNHTTFRNT
     VLNKQGISTV SGSVQGQFRR DSQNSTASTY YGSMQSRRSS QSSQVSSIPT MRPIPSCTTT
     AASFYDPISP GCSRRSSQMS NGVNCYAFTS TSGLPIINKD LNA
 
 
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