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Database: UniProt
Entry: A0A340YDB0_LIPVE
LinkDB: A0A340YDB0_LIPVE
Original site: A0A340YDB0_LIPVE 
ID   A0A340YDB0_LIPVE        Unreviewed;      1300 AA.
AC   A0A340YDB0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Zinc finger protein 536 {ECO:0000313|RefSeq:XP_007470993.1};
GN   Name=ZNF536 {ECO:0000313|RefSeq:XP_007470993.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007470993.1};
RN   [1] {ECO:0000313|RefSeq:XP_007470993.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000256|ARBA:ARBA00006991}.
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DR   RefSeq; XP_007470993.1; XM_007470931.1.
DR   STRING; 118797.A0A340YDB0; -.
DR   GeneID; 103078740; -.
DR   KEGG; lve:103078740; -.
DR   CTD; 9745; -.
DR   InParanoid; A0A340YDB0; -.
DR   OrthoDB; 3849084at2759; -.
DR   Proteomes; UP000265300; Unplaced.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR45925:SF2; ZINC FINGER PROTEIN 536; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   Pfam; PF16606; zf-C2H2_assoc; 1.
DR   Pfam; PF13909; zf-H2C2_5; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          130..157
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          158..180
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          274..302
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          345..372
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          373..400
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          632..659
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          752..779
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          780..807
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1129..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..977
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1300 AA;  140810 MW;  CAEFD30E249B68AD CRC64;
     MEEASLCLGV SSAAPEAEPH LSSPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKA
     PVPLDEKAHV PMSGQPMGSQ MALLANQLGR DVDTSLNGRV DLQQFLNGQN LGIMSQMSDI
     EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
     KLGNLGKGRG RVREENRLLH ELEERAILRD RQLKSSLLQP RPDLKPLPHA QQPPLAACNL
     ALPTNHSVPD VANPVPSPKP ASVQEDSATP AAGFRCTFCK GKFKKREELD RHIRILHKPY
     KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNGGGEQ SANEFRCEVC GQVFSQAWFL
     KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKSKSPSDAE VPVPMGGMSQ
     EAHANLYSRY LSCLQSGSFM AADKASLSEP SQLYGKGEIP VKEKEVAGKL PTPISSMAHG
     VPEGDKHSLL GCLNLVPPLK SSCIERLQAA AKAAEMDPVN SYQAWQLMAR GMAMEHGFLS
     KEHQLQRNHE DTLANAGVLF DKEKREYVLV GADGSKQKMP ADLVHSTKAG SQRDLPNTLD
     PLEGSRDFLS HGLHQALEYN LQGPGSLKEK PTECPDCGRV FRTYHQVVVH SRVHKRDRKG
     DEDGLHGGPD ERRGSGSDQE SQSVSRSTTP GSSNITEESG VGGGLSQTGS AQEDSPHPSS
     PSSSDIGEEA GRSAGVQQPA LLRDRSLGSA MKDCPYCGKT FRTSHHLKVH LRIHTGEKPY
     KCPHCDYAGT QSASLKYHLE RHHRERQNGA GPLSGQPLNQ DHRDELSNKA ALFIRPDILR
     GAFKGLPGID FRGGPASQQW TSGVFSSGDH SGQATGLSSE APSDTLKGTD LPSKSTHFSE
     IGRAYQSIVN NGVNFQGSLQ AFVDSFVLSS LRKQKDMKGK APSDPPPMKV RGADGGEEKA
     GSKAAPRKSE KSQYEPLDLS VRPDAASLPG SSATVQDSIA WHGCLFCAFT TSSMELMALH
     LQANHLGKSE RKDSAVGVTV NCTDQAREAS KVALLPSVQS SKEMALSNMM GPLDSPSEKM
     AQGQVKETLG EQKGSPWPGH MDPTFCNFPS DFYKQFGVYP GLLGSGASGS CPNREPDGKA
     HLEDDAPILI PETTNKNTTD DLSDIASSED MDSSKGENNE EEDIDTEPEV MSKPPALSKD
     GGSDGGDGLL PAGAPQPIQG LVSPLPQASE KQWHSPGLLP AQDPVASLPK PERGPQGLEK
     PMNVLSVLRA YSADGLAAFN GLASSTANSG CIKRPDLCGK
//
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