ID A0A2K6E2Z7_MACNE Unreviewed; 664 AA.
AC A0A2K6E2Z7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zinc finger protein 17 {ECO:0000313|Ensembl:ENSMNEP00000042538.1};
GN Name=ZNF17 {ECO:0000313|Ensembl:ENSMNEP00000042538.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000042538.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000042538.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6E2Z7; -.
DR Ensembl; ENSMNET00000067041.1; ENSMNEP00000042538.1; ENSMNEG00000043999.1.
DR GeneTree; ENSGT00940000164515; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000043999; Expressed in cerebellum and 12 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 17.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23226:SF403; ZINC FINGER PROTEIN 59-LIKE; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 17.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 18.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 10..103
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 192..219
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 220..247
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 248..275
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 276..303
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 304..331
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 332..359
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 360..387
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 388..415
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 416..443
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 444..471
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 472..499
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 500..527
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 528..555
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 556..583
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 584..611
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 612..639
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 640..664
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
SQ SEQUENCE 664 AA; 77340 MW; 3487764A4A087E9F CRC64;
VLMDAGQDCM VFEDVAIHFS QEEWGILNGV QRHLHSDVML ENFALLSSVG CWHGAKDEEA
PSKQCVSVGV SQVTTLKPAL CTQKAQPCET CSSLLKDILH LAEHDRTHPK CTAELYLHQK
EHVREKLTRS DEGRPSFVND SVHLAKRNFT CMHGGKDFTG DSDLQQQALP SGWKPHRDTR
GVEAFQSGQN DYSCSQCGKD FCHQRMLFEH QKIHTEERPY ECSECGKFFR YNSDLIKHQR
NHTGERPYKC SECGKAFSLK YNVVQHQKIH TGERPYECSE CGKAFLRKSH LLQHQRIHTR
PRPYLCSECG KTFLTQAHLV GHQKIHTGER PYGCNECGKY FMYSSALIRH QKVHTGERPF
YCCECGKFFM DSCTLIIHQR VHTGEKPYEC NECGKFFRYR STLIRHQKVH TGEKPYECSE
CGKFFMDTST LIIHQRVHTG EKPYECSECG KFFRYCFTLN RHQRVHSGER PYECSECGKF
FVDSCTLKSH QRVHTGERPF ECSICGKSFR CRSTLDTHQR IHTGERPYEC SECGKFFRHN
SNHIRHRRNH FGERSFECAE CGRVFSQNSH LIRHQKVHTR ERTYKCSKCG KFFMDSSTLI
SHQRVHTGEK PYECSECGKV FRYNSSLIKH RRIHTGERPY QCSECGRVFN QNSHLIQHQK
VHTR
//