XFIN_XENLA
ID XFIN_XENLA Reviewed; 1350 AA.
AC P08045;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger protein Xfin;
DE AltName: Full=Xenopus fingers protein;
DE Short=Xfin;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=2826129;
RA Ruiz i Altaba A., Perry-O'Keefe H., Melton D.A.;
RT "Xfin: an embryonic gene encoding a multifingered protein in Xenopus.";
RL EMBO J. 6:3065-3070(1987).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1782138; DOI=10.1016/0925-4773(91)90069-i;
RA De Lucchini S., Rijli F.M., Ciliberto G., Barsacchi G.;
RT "A Xenopus multifinger protein, Xfin, is expressed in specialized cell
RT types and is localized in the cytoplasm.";
RL Mech. Dev. 36:31-40(1991).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8398678;
RA Rijli F.M., De Lucchini S., Ciliberto G., Barsacchi G.;
RT "A Zn-finger protein, Xfin, is expressed during cone differentiation in the
RT retina of the frog Xenopus laevis.";
RL Int. J. Dev. Biol. 37:311-317(1993).
RN [4]
RP PUTATIVE FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=7692399; DOI=10.1093/nar/21.18.4218;
RA Andreazzoli M., de Lucchini S., Costa M., Barsacchi G.;
RT "RNA binding properties and evolutionary conservation of the Xenopus
RT multifinger protein Xfin.";
RL Nucleic Acids Res. 21:4218-4225(1993).
RN [5]
RP STRUCTURE BY NMR OF A FINGER.
RX PubMed=2506074; DOI=10.1016/0014-5793(89)81030-0;
RA Lee M.S., Cavanagh J., Wright P.E.;
RT "Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from
RT Xfin. Sequential resonance assignments and secondary structure.";
RL FEBS Lett. 254:159-164(1989).
RN [6]
RP STRUCTURE BY NMR OF FINGER 31.
RX PubMed=2503871; DOI=10.1126/science.2503871;
RA Lee M.S., Gippert G.P., Soman K.V., Case D.A., Wright P.E.;
RT "Three-dimensional solution structure of a single zinc finger DNA-binding
RT domain.";
RL Science 245:635-637(1989).
CC -!- FUNCTION: Binds to poly-G sequences in RNA. May function in post-
CC translational regulation processes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1782138,
CC ECO:0000269|PubMed:7692399, ECO:0000269|PubMed:8398678}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, and in specialized cell types
CC such as neural retina cones in adults. {ECO:0000269|PubMed:1782138,
CC ECO:0000269|PubMed:8398678}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout oogenesis and embryogenesis through to at least the tadpole
CC stage. Also expressed in adults. {ECO:0000269|PubMed:2826129,
CC ECO:0000269|PubMed:8398678}.
CC -!- PTM: Phosphorylated. Phosphorylation enhances RNA binding.
CC {ECO:0000269|PubMed:7692399}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; X06021; CAA29425.1; -; mRNA.
DR PIR; S00647; S00647.
DR RefSeq; NP_001095247.1; NM_001101777.1.
DR PDB; 1ZNF; NMR; -; A=1044-1068.
DR PDBsum; 1ZNF; -.
DR AlphaFoldDB; P08045; -.
DR SMR; P08045; -.
DR PRIDE; P08045; -.
DR GeneID; 397958; -.
DR KEGG; xla:397958; -.
DR CTD; 397958; -.
DR Xenbase; XB-GENE-6252152; znf208.L.
DR EvolutionaryTrace; P08045; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397958; Expressed in testis and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 32.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 37.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 22.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 35.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 37.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..1350
FT /note="Zinc finger protein Xfin"
FT /id="PRO_0000047087"
FT DOMAIN 1..58
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 108..130
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 136..158
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 164..186
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..214
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..270
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..298
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 503..525
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 531..553
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..581
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 587..609
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 615..637
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 643..665
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..693
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 699..721
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 750..772
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 778..800
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 806..828
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 834..856
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 862..884
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 890..912
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 918..940
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 988..1010
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1016..1038
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1044..1066
FT /note="C2H2-type 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1136..1158
FT /note="C2H2-type 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1164..1186
FT /note="C2H2-type 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1192..1214
FT /note="C2H2-type 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1220..1242
FT /note="C2H2-type 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1248..1270
FT /note="C2H2-type 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1276..1298
FT /note="C2H2-type 37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 1047..1049
FT /evidence="ECO:0007829|PDB:1ZNF"
FT HELIX 1056..1062
FT /evidence="ECO:0007829|PDB:1ZNF"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:1ZNF"
SQ SEQUENCE 1350 AA; 155805 MW; 27F10AB0851E0AD8 CRC64;
MEEPKCLQRE MYKSVMTENY QCVLSLGYPI RKPEIVSMME VGEELWSKND SARPGQKEVE
GETPKESDWA AENCKRAQMH KEVLDLDTLA AVKSEPVEEG SNSAKKSHIC SHYGKLFSCY
AAVVRHQRMH QLQKSHHCPH CKKSFVQRSD FIKHQRTHTG ERPYQCVECQ KKFTERSALV
NHQRTHTGER PYTCLDCQKT FNQRSALTKH RRTHTGERPY RCSVCSKSFI QNSDLVKHLR
THTGEKPYEC PLCVKRFAES SALMKHKRTH STHRPFRCSE CSRSFTHNSD LTAHMRKHTE
FRNVLNLDSV VGTDPLSSQN VASSPYSCSK CRKTFKRWKS FLNHQQTHSR EKPYLCSHCN
KGFIQNSDLV KHFRTHTGER PYQCAECHKG FIQKSDLVKH LRTHTGEKPF KCSHCDKKFT
ERSALAKHQR THTGEKPYKC SDCGKEFTQR SNLILHQRIH TGERPYKCTL CDRTFIQNSD
LVKHQKVHAN LPLSDPHTAN SPHKCSKCDL TFSHWSTFMK HSKLHSGEKK FQCAECKKGF
TQKSDLVKHI RVHTGEKPFK CLLCKKSFSQ NSDLHKHWRI HTGEKPFPCY TCDKSFTERS
ALIKHHRTHT GERPHKCSVC QKGFIQKSAL TKHSRTHTGE KPYPCTQCGK SFIQNSDLVK
HQRIHTGEKP YHCTECNKRF TEGSSLVKHR RTHSGEKPYR CPQCEKTFIQ SSDLVKHLVV
HNGENPPAAT AFHEILIRRE NLTRSEPDPY PCTECGKVFH QRPALLKHLR THKTEKRYPC
NECDKSFFQT SDLVKHLRTH TGERPYHCPE CNKGFIQNSD LVKHQRTHTG ERPYTCSQCD
KGFIQRSALT KHMRTHTGEK PYKCEQCQKC FIQNSDLVKH QRIHTGEKPY HCPDCDKRFT
EGSSLIKHQR IHSRIKPYPC GVCGKSFSQS SNLLKHLKCH SEQNPPVALS SELGFVAETQ
THPDPVDHIV YGDTASYISP EAAGERSFKC NDCGKCFAHR SVLIKHVRIH TGERPYKCSQ
CTRSFIQKSD LVKHYRTHTG ERPYKCGLCE RSFVEKSALS RHQRVHKNES PVLNSAMEQQ
QVTYWGESKD DPNSLVPQLH VIKEEESPHI VNAYSPLSIL QSYFPPILEP KGTPRYSCSE
CGKCFTHRSV FLKHWRMHTG EQPYTCKECG KSFSQSSALV KHVRIHTGEK PYPCSTCGKS
FIQKSDLAKH QRIHTGEKPY TCTVCGKKFI DRSSVVKHSR THTGERPYKC NECTKGFVQK
SDLVKHMRTH TGEKPYGCNC CDRSFSTHSA SVRHQRMCNT GRPYQDEEYE NSLFYSADIT
WKGDYAQLLQ IPCGLEEPMK AIGWISEVAL
