ID A0A2K5YK09_MANLE Unreviewed; 1279 AA.
AC A0A2K5YK09;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000015882.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000015882.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC {ECO:0000256|ARBA:ARBA00003767}.
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}.
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 AlphaFoldDB; A0A2K5YK09; -.
DR STRING; 9568.ENSMLEP00000015882; -.
DR Ensembl; ENSMLET00000039347.1; ENSMLEP00000015882.1; ENSMLEG00000032075.1.
DR GeneTree; ENSGT00940000154437; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR InterPro; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222:SF3; ZINC FINGER PROTEIN 532; 1.
DR PANTHER; PTHR47222; ZINC FINGER PROTEIN 532-RELATED; 1.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 948..976
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1042..1070
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1164..1192
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 66..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 140735 MW; F4AE6FA45531394A CRC64;
CLLFFEVGTQ FFPSRSISIE SFFPKGQGSQ EHLLKFMTMG DVKTPDFDDP LAAFDIPDMA
DPKAAIENGH DDHESHMKQN AHREDDSHTP SFSNVDVSMI FKNVRNVDSS EGGRKTVTTT
SNGRHNGFLT ASSLYSYGKD GAKSLKEDMP ASQVTLKDAT FSQFSPISSA EEFDDDEKME
VDEPPDKEDV RSSFRPNLKA LGGENSSKTG LSTSGNIEKN KIVKREAKAN SINPSVYEPF
KVRKAEDKLK ENSDKVLENR VLAGKPSSEK KDTGLHGITK SSSKLSSCIA AIAALSAKKA
ASDSCKEPVA NSRESSPLPK EVNDSPRAAN KSPESQNLID GTKTPSPKPP NSPRSISREN
SSKGSPSSPA GSTPAIPKVR IKTIKTSSAV IKRTVTRVLP EVDLDSRKKP SEQTASVMAS
VTSLLSSPAS AAILSSLPKA PPQSVVITNA VSPVTIKPVA TTFLPVSSVK TTGSQVINLK
LTNNTMVKAT LISAASVQSA ISAIIKANNA IQQQIVVVPA SSLANAKLLP KIVHLANLNL
LPQGAQATSE LCLVLTKPQQ QIKQVIINAA TSKTPPQKMS QVQVVSSLQN SVVEAFNKVP
SSVNPVPVYI PNLSPPANAG IMLPMHGCKC LECGDSCSPA LWETKSLTQS CDRWIVCIKV
TCNHCTKNLI FYNKCSLLSY ARGHKEKGVV MQCSHLILKP VPADQMTVSP SSNTSTSTST
LQSPVGASTH TVAKIQSGIT GTVILAPSST PIIAAMPLDE DPSKLLKRLE CNEVFPDETS
LATHFQQAAD TSGQKTCTIC QMLLPNQCSY ASHRRIHQHK SPYTCPECRA ISRSVHFQTH
VTKNCLHYTR SVGFRCVHCN VVYSDGAALK SHIQGSRCEV FDKCPICPMA FKSAPSTHSH
TYTQHPGIKI EEPKIIWKCS MCDTVLTLQT LLYHHFDQHI ENQKVSVFKC PDCSLLYAQR
QLMMDHIKSA HGTLKSIEGP PNLGINLPLS IKPATQNSAN QNKEDTKSMP GWTYWECDCL
FMQRDVYISH ARKEHGKQVK KHPCRQCDKP FSSSHSLRRH NRIKHRVIRE VYKHVQLVHG
IKDPALKEMT PEIKEDTEVP RPKRKLEEPV LEFRPPRGAI TQPLKKLKIN VLQVHRCVVC
GFTTENLLQF HEHIPQHKSD GSSYQCRECG LYYTSHVSLS RHLFIVHRSK QNGAGDDNQQ
ENKPSHEDES PNGAVSDRNA KCAQKLLKLN IFWIHQSKRM SSAEKQPQML HEENPCPHWN
KKDIFVTKSL QYNRVNSTV
//