ZN521_XENLA
ID ZN521_XENLA Reviewed; 1310 AA.
AC Q6NUD7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Zinc finger protein 521;
GN Name=znf521;
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 [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that can both act as an activator or a
CC repressor depending on the context. Involved in BMP signaling and in
CC the regulation of the immature compartment of the hematopoietic system
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC068658; AAH68658.1; -; mRNA.
DR RefSeq; NP_001084597.1; NM_001091128.1.
DR AlphaFoldDB; Q6NUD7; -.
DR MaxQB; Q6NUD7; -.
DR PRIDE; Q6NUD7; -.
DR GeneID; 414550; -.
DR KEGG; xla:414550; -.
DR CTD; 414550; -.
DR Xenbase; XB-GENE-6252560; znf521.S.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 414550; Expressed in brain and 19 other tissues.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 30.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24.
PE 2: Evidence at transcript level;
KW Activator; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1310
FT /note="Zinc finger protein 521"
FT /id="PRO_0000306873"
FT ZN_FING 48..68
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 119..141
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 147..169
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 175..197
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 203..225
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 247..270
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..305
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 311..333
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..428
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..459
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..499
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 512..535
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..584
FT /note="C2H2-type 13; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 663..685
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 693..716
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 721..744
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..774
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 782..804
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 808..831
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 885..907
FT /note="C2H2-type 21; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 929..951
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 958..980
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1019..1041
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1064..1082
FT /note="C2H2-type 25; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1138..1161
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1194..1216
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1224..1246
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1255..1278
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1285..1308
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 148640 MW; 75D9B7680EB7B270 CRC64;
MSRRKQAKPR SLKDPNCKLE DTSEDGESPD CKKRQEEGDE LEEEEAVHSC DSCLQVFESL
SDITEHKISQ CQLTDGADIE DDPTCSWPAS SPSSKDQASP IHGEGFDFGE EEGIPGLPYP
CQFCDKSFSR LSYLKHHEQS HSDKLPFKCT YCSRLFKHKR SRDRHIKLHT GDKKYHCSEC
DASFSRSDHL KIHLKTHTSN KPYKCAICRR GFLSSSSLHG HMQVHERNKD CSQSGSRMEE
WKMKDTQKCS QCEEGFDFPE DLQKHIAECH PECSPNDDRG ALQCMYCHEL FMEETSLLNH
MEQIHNSEKK NSCNICSENF HSVEELYSHM DSHQHPESCN PSNSPSLVTV GYTSVSSTTP
DSNLSVDSST MVEVAPPLAK GRGRKRAVQQ TGDAPTSKQA RVSYSCIYCS KQLFSSLAVL
QIHLKTMHLD KPEQAHICQY CLEVLPSLFN LNEHLKQVHE TQDPALIVST MSAMVYQCNF
CSEIFNDLNM LQDHIRSSHG FPNPVTKDSN AFFCPHCYMG FLTDTSLEEH IRQVHCELGN
SRFGSPVLGT PKEPVVEVYS CSYCTNSPIF NSVLKLNKHI KENHKNIPLA LNYIHNGKKS
RALSPLSPIT LEQSSLKMMQ SLGGTPSRLA GEYICNQCGA KYTSLDGFQT HLKTHLDTVL
PKLTCPQCNK EFPNQESLLK HVTIHFMITS TYYICESCDK QFTSVDDLQK HLLDMHTFGF
FRCTLCQEVF DSKVSIQLHL AVKHSNEKKV YRCTSCNWDF RTETDLQLHV KHNHLENQGK
MHKCIFCGES FGTEVELQCH ITTHSKKYNC KFCSKAFHAI ILLEKHLREK HCVFEDKTQN
CGTNGASEQI QKEEVELQTL LTNNQESHNS HDGSEEDIDT SEPMYGCDIC GAAYTMESLL
QNHQLRDHNI RPGESAIVKK KAELIKGNYK CNVCSRTFFS EGGLREHMQT HLGPVKHYMC
PICGERFPSL LTLTEHKVTH SKSLDTGNCR ICKLPLQCEE DFLEHCQMHP DLRNSLTGFR
CVVCMQTVTS TLELKIHGTF HMQKTGTASV VQSAGRVQNL QKLYKCASCL KEFRSKQDLV
KLDINGLPYG LCASCVNLSK SASPNANVTL STNRQVISQT DSLTCVEAKN YKTSVLKTRC
SSCNVKFESE TELQNHIQTI HRELTSENSA TQLKTPQVSP MARISPQSDE KKTYQCIKCQ
MVFYNEWDIQ VHVANHMIDE GLNHECKLCS QTFDSPAKLQ CHLIEHSFEG MGGTFKCPVC
FTVFVQANKL QQHIFSAHGQ EDKIYDCAQC PQKFFFQTEL QNHTMSQHSS
