ID A0A2K5XUZ4_MANLE Unreviewed; 1283 AA.
AC A0A2K5XUZ4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Zinc finger protein 532 {ECO:0000313|Ensembl:ENSMLEP00000007128.1};
GN Name=ZNF532 {ECO:0000313|Ensembl:ENSMLEP00000007128.1};
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:ENSMLEP00000007128.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000007128.1}
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 Ensembl; ENSMLET00000030415.1; ENSMLEP00000007128.1; ENSMLEG00000027509.1.
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; 5.
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 Pfam; PF13912; zf-C2H2_6; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
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 616..634
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 852..880
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 887..914
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 918..946
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1007..1035
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1037..1065
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1185..1213
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1246..1268
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 26..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 139060 MW; AEE289F97B82A723 CRC64;
MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDHESH MKQNAHGEDD SHAPSSSDVG
VSVIVKNVRN IDSSEGGEKD GHNPTGNGLH NGFLTTSSLD SYSKDGANSL KGDVPASEVT
LKDSTFSQFS PISSAEEFDD DEKIEVDDPP DKEDVRSSFR SNVLTGSAPQ QDYDKLKALG
GENSSKTGLS TSGNMEKNKV VKREAEANSI NLSVYEPFKV RKAEDKLKEN SDKVLENRVL
DGKPSSEKND AGLPGVAPSK TKSSSKLSSC IAAIAALSAK KAASDSCKEP VANSRESSPL
PKEVNDSPRA ADKSPESQNL IDGTKKPSLK QPDSPRSISS ENSSKGSPSS PAGSTPAIPK
VRIKTIKTSS GEIKRTVTRV LPEVDLDSGK KPSEQTASVM ASVTSLLSSP ASAAVLSSPP
RAPLQSAVVT NAVSPAELTP KQVTIKPVAT AFLPVSAVKT AGSQVINLKL ANNTTVKATV
ISAASVQSAS SAIIKAANAI QQQTVVVPAS SLANAKLVPK TVHLANLNLL PQGAQATSEL
RQVLTKPQQQ IKQAIINAAA SQPPKKVSRV QVVSSLQSSV VEAFNKVLSS VNPVPVYIPN
LSPPANAGIT LPTRGYKCLE CGDSFALEKS LTQHYDRRSV RIEVTCNHCT KNLVFYNKCS
LLSHARGHKE KGVVMQCSHL ILKPVPADQM IVSPSSNTST STSTLQSPVG AGTHTVTKIQ
SGITGTVISA PSSTPITPAM PLDEDPSKLC RHSLKCLECN EVFQDETSLA THFQQAADTS
GQVEYHLNFR VSMSLILGWE CSEMDGCVCA CMPVHKDCSH RIEKISWGCG GGGGDGGGSR
SGSGGSHCEV FYKCPICPMA FKSAPSTHSH AYTQHPGIKI GEPKIIYKCS MCDTVFTLQT
LLYRHFDQHI ENQKVSVFKC PDCSLLYAQK QLMMDHIKSM HGTLKSIEGP PNLGINLPLS
IKPTTQNSAN QNKEDTKSMN GKEKLEKKSP SPVKKSMETK KVASPGWTCW ECDRLFMQRD
VYISHVRKEH GKQMKKHPCR QCDKSFSSSH SLCRHNRIKH KGIRKVYACS HCPDSRRTFT
KRLMLEKHVQ LMHGIKDPDL KEMTDATNEE ETEIKEDTKV PSPKRKLEEP VLEFRPPRGA
ITQPLKKLKI NVFKVHKCAV CGFTTENLLQ FHEHIPQHKS DGSSYQCREC GLCYTSHVSL
SRHLFIVHKL KEPQPVSKQN GAGEDNQQEN KPSHEDESPD GAVSDRKCKV CAKTFETEAA
LNTHMRTHGM AFIKSKRMSS AEK
//
