ID A0A2K5YK23_MANLE Unreviewed; 1254 AA.
AC A0A2K5YK23;
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:ENSMLEP00000015906.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000015906.1}
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}.
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DR AlphaFoldDB; A0A2K5YK23; -.
DR Ensembl; ENSMLET00000039372.1; ENSMLEP00000015906.1; 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 910..938
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1021..1049
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1139..1167
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 137872 MW; DA4F5E86D3F2FB84 CRC64;
MTMGDVKTPD FDDPLAAFDI PDMADPKAAI ENGHDDHESH MKQNAHREDD SHTPSFSNVD
VSMIFKNVRN VDSSEGGRKT VTTTSNGRHN GFLTASSLYS YGKDGAKSLK EDMPASQVTL
KDATFSQFSP ISSAEEFDDD EKMEVDEPPD KEDVRSSFRP NLKALGGENS SKTGLSTSGN
IEKNKIVKRE AKANSINPSV YEPFKVRKAE DKLKENSDKV LENRVLAGKP SSEKKDTGLH
GISSSKLSSC IAAIAALSAK KAASDSCKEP VANSRESSPL PKEVNDSPRA ANKSPESQNL
IDGTKTPSPK PPNSPRSISR ENSSKGSPSS PAGSTPAIPK VRIKTIKTSS AVIKRTVTRV
LPEVDLDSRK KPSEQTASVM ASVTSLLSSP ASAAILSSLP KAPPQSVVIT NAVSPVTIKP
VATTFLPVSS VKTTGSQVIN LKLTNNTMVK ATLISAASVQ SAISAIIKAN NAIQQQIVVV
PASSLANAKL LPKIVHLANL NLLPQGAQAT SELCLVLTKP QQQIKQVIIN AATSKTPPQK
MSQVQVVSSL QNSVVEAFNK VPSSVNPVPV YIPNLSPPAN AGIMLPMHGC KCLECGDSCS
PALWETKSLT QSCDRWIVCI KVTCNHCTKN LIFYNKCSLL SYARGHKEKG VVMQCSHLIL
KPVPADQMTV SPSSNTSTST STLQSPVGAS THTVAKIQSG ITGTVILAPS STPIIAAMPL
DEDPSKLLKR LECNEVFPDE TSLATHFQQA ADTSGQKTCT ICQMLLPNQC SYASHRRIHQ
HKSPYTCPEC RAISRSVHFQ THVTKNCLHY TRSVGFRCVH CNVVYSDGAA LKSHIQGSRC
EVFDKCPICP MAFKSAPSTH SHTYTQHPGI KIEEPKIIWK CSMCDTVLTL QTLLYHHFDQ
HIENQKVSVF KCPDCSLLYA QRQLMMDHIK SAHGTLKSIE GPPNLGINLP LSIKPATQNS
ANQNKEDTKS MYGKEKLEKK SPSPKVSRPG WTYWECDCLF MQRDVYISHA RKEHGKQVKK
HPCRQCDKPF SSSHSLRRHN RIKHRVIREV YKHVQLVHGI KDPEEAEIKE DTEVPRPKRK
LEEPVLEFRP PRGAITQPLK KLKINVLQVH RCVVCGFTTE NLLQFHEHIP QHKSDGSSYQ
CRECGLYYTS HVSLSRHLFI VHRSKQNGAG DDNQQENKPS HEDESPNGAV SDRNAKCAQK
LLKLNIFWIH QSKRMSSAEK QPQMLHEENP CPHWNKKDIF VTKSLQYNRV NSTV
//
