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Database: UniProt
Entry: A1YG48
LinkDB: A1YG48
Original site: A1YG48 
ID   ZN394_PANPA             Reviewed;         561 AA.
AC   A1YG48;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   01-OCT-2014, entry version 35.
DE   RecName: Full=Zinc finger protein 394;
GN   Name=ZNF394;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human
RT   lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 KRAB domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00119}.
CC   -!- SIMILARITY: Contains 1 SCAN box domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00187}.
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DR   EMBL; DQ977217; ABM54273.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1YG48; -.
DR   SMR; A1YG48; 58-145, 356-548.
DR   HOVERGEN; HBG018163; -.
DR   GO; GO:0005634; C:nucleus; 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:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 7.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR003309; Tscrpt_reg_SCAN.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF47353; SSF47353; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    561       Zinc finger protein 394.
FT                                /FTId=PRO_0000285473.
FT   DOMAIN       64    146       SCAN box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00187}.
FT   DOMAIN      155    230       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     358    380       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     386    408       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     414    436       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     442    463       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     469    491       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     497    519       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     525    547       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
SQ   SEQUENCE   561 AA;  64278 MW;  BB7B8CB00E1BA023 CRC64;
     MNSSLTAQRR GSDAELGPWV MAARSKDAAP SQRDGLLPVK VEEDSLGSWE PSYPAASPDP
     ETSRLHFRQL RYQEVAGPEE ALSRLRELCR RWLRPELLSK EQILELLVLE QFLTILPEEL
     QAWVREHCPE SGEEAVAVVR ALQRALDGTS SQGMVTFEDM AVSLTWEEWE RLDPARSDFC
     RESAQKDSGS TVPPSLESRV ENKELIPVQQ ILEEAEPQGR LQEAFQGKRP LFSKCVSTHE
     DRVEKQSGDP LPLKLENSPE AEGFNSISDV NKNGSIEGED SKNNELQNSA RCSNLVLCQH
     IPKAERPTDS EEHGNKCKQS FHMVTWHVLK PHKSDSGDSF HHSSLFETQR QLHEERPYKC
     GNCGKSFKQR SDLFRHQRIH TGEKPYGCQE CGKSFSQSAA LTKHQRTHTG EKPYTCLKCG
     ERFRQNSHLN RHQSTHSRDK HFKCEECGET CHISNLFRHQ RLHKGERPYK CEECEKSFKQ
     RSDLFKHHRI HTGEKPYGCS VCGKRFNQSA TLIKHQRIHT GEKPYKCLEC GERFRQSTHL
     IRHQRIHQNK VLSAGRGGSR L
//
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