ZNF7_PONAB
ID ZNF7_PONAB Reviewed; 686 AA.
AC Q5RBX0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Zinc finger protein 7;
GN Name=ZNF7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CR858512; CAH90740.1; -; mRNA.
DR RefSeq; NP_001125413.1; NM_001131941.1.
DR AlphaFoldDB; Q5RBX0; -.
DR SMR; Q5RBX0; -.
DR STRING; 9601.ENSPPYP00000021300; -.
DR PRIDE; Q5RBX0; -.
DR GeneID; 100172320; -.
DR KEGG; pon:100172320; -.
DR CTD; 7553; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5RBX0; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000001595; 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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 8.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..686
FT /note="Zinc finger protein 7"
FT /id="PRO_0000290336"
FT DOMAIN 4..76
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 223..245
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..603
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17097"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17097"
SQ SEQUENCE 686 AA; 77899 MW; 0397BC3B4EECAE4F CRC64;
MEVVTFGDVA VHFSREEWQC LDPGQRALYR EVMLENHSSV AGLAGFLVFK PELISRLEQG
EEPWVLDLQG AEGTEAPRTS KTDSTIRTEN EQACEDMDIL KSESYGTVVR ISPQDFPQNP
GFGDVSDSEV WLDSHLGSPG LKVTGFTFQN NCLNEETVVP KTFTKDAPQG CKELGSSGLD
CQPLESQGES AEGMSQRCEE CGKGIRATSD IALHWEINTQ KISRCQECQK KLSDCLQGKH
TNNCHGEKPY ECAECGKVFR LCSQLNQHQR IHTGEKPFKC TECGKAFRLS SKLIQHQRIH
TGEKPYRCEE CGKAFGQSSS LIHHQRIHTG ERPYGCRECG KAFSQQSQLV RHQRTHTGER
PYPCKECGKA FSQSSTLAQH QRMHTGEKAQ ILKASDSPSL VAHQRIHAVE KPFKCDECGK
AFRWISRLSQ HQLIHTGEKP YKCNKCTKAF GCSSRLIRHQ RTHTGEKPFK CDECGKGFVQ
GSHLIQHQRI HTGEKPYVCN DCGKAFSQSS SLIYHQRIHK GEKPYECLQC GKAFSMSTQL
TIHQRVHTGE RPYKCNECGK AFSQNSTLFQ HQIIHAGVKP YECSECGKAF SRSSYLIEHQ
RIHTRAQWFY EYGNALEGSI FVSRKKVNTI KKLHQCEDCE KIFRWRSHLI IHQRIHTGEK
PYKCNDCGKA FNRSSRLTQH QKIHMG
