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Reviewed, UniProtKB/Swiss-Prot P08045 (XFIN_XENLA)

Last modified January 19, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Zinc finger protein Xfin
Gene names
Name: xfin
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length1350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Binds RNA. Could function in post-translational regulation processes.

Subcellular location

Cytoplasm.

Tissue specificity

Oocytes and in specialized cell types such as neural retina cones.

Developmental stage

Expressed throughout oogenesis and embryogenesis.

Post-translational modification

Phosphorylated.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 37 C2H2-type zinc fingers.

Contains 1 KRAB domain.

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Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13501350Zinc finger protein Xfin
PRO_0000047087

Regions

Domain1 – 5858KRAB
Zinc finger108 – 13023C2H2-type 1
Zinc finger136 – 15823C2H2-type 2
Zinc finger164 – 18623C2H2-type 3
Zinc finger192 – 21423C2H2-type 4
Zinc finger220 – 24223C2H2-type 5
Zinc finger248 – 27023C2H2-type 6
Zinc finger276 – 29823C2H2-type 7
Zinc finger326 – 34823C2H2-type 8
Zinc finger354 – 37623C2H2-type 9
Zinc finger382 – 40423C2H2-type 10
Zinc finger410 – 43223C2H2-type 11
Zinc finger438 – 46023C2H2-type 12
Zinc finger466 – 48823C2H2-type 13
Zinc finger503 – 52523C2H2-type 14
Zinc finger531 – 55323C2H2-type 15
Zinc finger559 – 58123C2H2-type 16
Zinc finger587 – 60923C2H2-type 17
Zinc finger615 – 63723C2H2-type 18
Zinc finger643 – 66523C2H2-type 19
Zinc finger671 – 69323C2H2-type 20
Zinc finger699 – 72123C2H2-type 21
Zinc finger750 – 77223C2H2-type 22
Zinc finger778 – 80023C2H2-type 23
Zinc finger806 – 82823C2H2-type 24
Zinc finger834 – 85623C2H2-type 25
Zinc finger862 – 88423C2H2-type 26
Zinc finger890 – 91223C2H2-type 27
Zinc finger918 – 94023C2H2-type 28
Zinc finger988 – 101023C2H2-type 29
Zinc finger1016 – 103823C2H2-type 30
Zinc finger1044 – 106623C2H2-type 31
Zinc finger1136 – 115823C2H2-type 32
Zinc finger1164 – 118623C2H2-type 33
Zinc finger1192 – 121423C2H2-type 34
Zinc finger1220 – 124223C2H2-type 35
Zinc finger1248 – 127023C2H2-type 36
Zinc finger1276 – 129823C2H2-type 37

Secondary structure

1 ...... 1350
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P08045-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 27F10AB0851E0AD8

FASTA1,350155,805
        10         20         30         40         50         60 
MEEPKCLQRE MYKSVMTENY QCVLSLGYPI RKPEIVSMME VGEELWSKND SARPGQKEVE 

        70         80         90        100        110        120 
GETPKESDWA AENCKRAQMH KEVLDLDTLA AVKSEPVEEG SNSAKKSHIC SHYGKLFSCY 

       130        140        150        160        170        180 
AAVVRHQRMH QLQKSHHCPH CKKSFVQRSD FIKHQRTHTG ERPYQCVECQ KKFTERSALV 

       190        200        210        220        230        240 
NHQRTHTGER PYTCLDCQKT FNQRSALTKH RRTHTGERPY RCSVCSKSFI QNSDLVKHLR 

       250        260        270        280        290        300 
THTGEKPYEC PLCVKRFAES SALMKHKRTH STHRPFRCSE CSRSFTHNSD LTAHMRKHTE 

       310        320        330        340        350        360 
FRNVLNLDSV VGTDPLSSQN VASSPYSCSK CRKTFKRWKS FLNHQQTHSR EKPYLCSHCN 

       370        380        390        400        410        420 
KGFIQNSDLV KHFRTHTGER PYQCAECHKG FIQKSDLVKH LRTHTGEKPF KCSHCDKKFT 

       430        440        450        460        470        480 
ERSALAKHQR THTGEKPYKC SDCGKEFTQR SNLILHQRIH TGERPYKCTL CDRTFIQNSD 

       490        500        510        520        530        540 
LVKHQKVHAN LPLSDPHTAN SPHKCSKCDL TFSHWSTFMK HSKLHSGEKK FQCAECKKGF 

       550        560        570        580        590        600 
TQKSDLVKHI RVHTGEKPFK CLLCKKSFSQ NSDLHKHWRI HTGEKPFPCY TCDKSFTERS 

       610        620        630        640        650        660 
ALIKHHRTHT GERPHKCSVC QKGFIQKSAL TKHSRTHTGE KPYPCTQCGK SFIQNSDLVK 

       670        680        690        700        710        720 
HQRIHTGEKP YHCTECNKRF TEGSSLVKHR RTHSGEKPYR CPQCEKTFIQ SSDLVKHLVV 

       730        740        750        760        770        780 
HNGENPPAAT AFHEILIRRE NLTRSEPDPY PCTECGKVFH QRPALLKHLR THKTEKRYPC 

       790        800        810        820        830        840 
NECDKSFFQT SDLVKHLRTH TGERPYHCPE CNKGFIQNSD LVKHQRTHTG ERPYTCSQCD 

       850        860        870        880        890        900 
KGFIQRSALT KHMRTHTGEK PYKCEQCQKC FIQNSDLVKH QRIHTGEKPY HCPDCDKRFT 

       910        920        930        940        950        960 
EGSSLIKHQR IHSRIKPYPC GVCGKSFSQS SNLLKHLKCH SEQNPPVALS SELGFVAETQ 

       970        980        990       1000       1010       1020 
THPDPVDHIV YGDTASYISP EAAGERSFKC NDCGKCFAHR SVLIKHVRIH TGERPYKCSQ 

      1030       1040       1050       1060       1070       1080 
CTRSFIQKSD LVKHYRTHTG ERPYKCGLCE RSFVEKSALS RHQRVHKNES PVLNSAMEQQ 

      1090       1100       1110       1120       1130       1140 
QVTYWGESKD DPNSLVPQLH VIKEEESPHI VNAYSPLSIL QSYFPPILEP KGTPRYSCSE 

      1150       1160       1170       1180       1190       1200 
CGKCFTHRSV FLKHWRMHTG EQPYTCKECG KSFSQSSALV KHVRIHTGEK PYPCSTCGKS 

      1210       1220       1230       1240       1250       1260 
FIQKSDLAKH QRIHTGEKPY TCTVCGKKFI DRSSVVKHSR THTGERPYKC NECTKGFVQK 

      1270       1280       1290       1300       1310       1320 
SDLVKHMRTH TGEKPYGCNC CDRSFSTHSA SVRHQRMCNT GRPYQDEEYE NSLFYSADIT 

      1330       1340       1350 
WKGDYAQLLQ IPCGLEEPMK AIGWISEVAL

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References

[1]"Xfin: an embryonic gene encoding a multifingered protein in Xenopus."
Ruiz i Altaba A., Perry-O'Keefe H., Melton D.A.
EMBO J. 6:3065-3070(1987) [PubMed: 2826129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]"RNA binding properties and evolutionary conservation of the Xenopus multifinger protein Xfin."
Andreazzoli M., de Lucchini S., Costa M., Barsacchi G.
Nucleic Acids Res. 21:4218-4225(1993) [PubMed: 7692399] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Three-dimensional solution structure of a single zinc finger DNA-binding domain."
Lee M.S., Gippert G.P., Soman K.V., Case D.A., Wright P.E.
Science 245:635-637(1989) [PubMed: 2503871] [Abstract]
Cited for: STRUCTURE BY NMR OF FINGER 31.
[4]"Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure."
Lee M.S., Cavanagh J., Wright P.E.
FEBS Lett. 254:159-164(1989) [PubMed: 2506074] [Abstract]
Cited for: STRUCTURE BY NMR OF A FINGER.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06021 mRNA. Translation: CAA29425.1.
PIRS00647.
RefSeqNP_001095247.1.
UniGeneXl.25

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZNFNMR-A1044-1068[»]
ModBaseSearch...

Proteomic databases

PRIDEP08045.

Genome annotation databases

GeneID397958.
KEGGxla:397958.

Organism-specific databases

CTD397958.

Phylogenomic databases

HOVERGENP08045.

Family and domain databases

InterProIPR001909. Krueppel-associated_box.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 31 hits.
PfamPF00096. zf-C2H2. 19 hits.
[Graphical view]
SMARTSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 37 hits.
[Graphical view]
PROSITEPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 35 hits.
PS50157. ZINC_FINGER_C2H2_2. 37 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXFIN_XENLA
AccessionPrimary (citable) accession number: P08045
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 19, 2010
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents