ID A0A2U4BHL1_TURTR Unreviewed; 1301 AA.
AC A0A2U4BHL1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc finger protein 532 isoform X4 {ECO:0000313|RefSeq:XP_019792703.1, ECO:0000313|RefSeq:XP_019792704.1};
GN Name=ZNF532 {ECO:0000313|RefSeq:XP_019792703.1,
GN ECO:0000313|RefSeq:XP_019792704.1, ECO:0000313|RefSeq:XP_019792705.1,
GN ECO:0000313|RefSeq:XP_019792706.1, ECO:0000313|RefSeq:XP_019792707.1,
GN ECO:0000313|RefSeq:XP_019792708.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019792703.1};
RN [1] {ECO:0000313|RefSeq:XP_019792703.1, ECO:0000313|RefSeq:XP_019792704.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019792703.1,
RC ECO:0000313|RefSeq:XP_019792704.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019792703.1; XM_019937144.2.
DR RefSeq; XP_019792704.1; XM_019937145.2.
DR RefSeq; XP_019792705.1; XM_019937146.2.
DR RefSeq; XP_019792706.1; XM_019937147.2.
DR RefSeq; XP_019792707.1; XM_019937148.2.
DR RefSeq; XP_019792708.1; XM_019937149.2.
DR GeneID; 101319941; -.
DR OrthoDB; 5400362at2759; -.
DR Proteomes; UP000245320; Chromosome 13.
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; 6.
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; PF00096; zf-C2H2; 1.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
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:UP000245320};
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 754..784
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 870..898
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 905..932
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 936..964
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1025..1053
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1055..1083
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1203..1231
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1264..1286
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 26..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1261
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 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar 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 976..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 141472 MW; E3885C46DA9905F9 CRC64;
MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDQEGH IKQNAHVDDD SHTPSSSDVG
VSVIVKNVRN IDSSEGAEKD GHNPTGNGLH NGFLSASSLD TYSKDGSKSL KGDVPTSEVT
LKDSAFSQFS PISSAEEFDD DEKIEVDDPP DKEDMRSGFR SNVLTGSVPQ QDYDKLKALG
GEGLSKTGIS TPGNLEKNKV VKRETETNSI NLSVYEPFKV RKMEDKLKEN SEKVLENRVP
EGKLSSEKND ASLGGVVPSR TKPSSKLSSC IAAIAALSAK KAASDSSKEP VTNSREASPL
PKEVNDSPRA IEKSPESQSL IDGTKKASLK QPDSPRSISS ENSSKGSPSS PAGSTPAIPK
VRIKTIKTSS GEIKRTVTRV LPEVDLDAGK KPSEQTGSMV ASVTSLLSSP TSAAVLSSPP
RAPLQSAVVT NAVAPAELTP KQVTIKPVAT AFLPVSAVKT AGSQVINLKL ANNTTVKATV
ISAASVQSAS SAIIKAANAI QQQTVVVPAS SLANAKLVPK TVHLANLNLL PQGAQATSEL
RQVLTKPQQQ IKQAIISAAA SQPPKKVSRV QVVSSLQSSV VEAFNKVLSS VNPVPVYIPN
LSPPANAGIT LPTRGYKCLE CGDSFALEKS LTQHYDRRSV RIEVTCNHCT KNLVFYNKCS
LLSHARGHKE KGVVMQCSHL ILKPVPADQM IVSPSSNTPA SSSALPSSSG AGTHTVTKIQ
SGITGTVISA PSSTPIIPAM PLDEDPSKLC RHSLKCLECN EVFQDETSLA THFQQAADTS
GQKTCTVCQM LLPNQCSYAS HQRIHQHKSP YTCPECGAIC RSVHFQTHVT KNCLHYTRRV
GFRCVHCNVV YSDVAALKSH IQGSHCEVFY KCPICPMAFK SAPSTHSHAY TQHPGIKIGE
PKIIYKCSMC DTVFTLQTLL YRHFDQHIEN QKVSVFKCPD CSLLYAQKQL MMDHIKSMHG
TLKSIEGPPN LGINLPLSIK PTTQNSANQN KEDTRSVNGK EKLEKKSPSP VKKSLEPKKV
ASPGWTCWEC DRLFTQRDVY ISHVRKEHGK QMKKHPCRQC DKSFSSSHSL CRHNRIKHKG
IRKVYTCSHC PDSRRTFTKR LMLEKHIQLM HGIKDPDLKE MTEATNEEEA EIKEDTKVPS
PKRKLEEPVL EFRPPRGAIT QPLKKLKINV FKVHKCAVCG FTTENLLQFH EHIPQHKSDG
SSHQCRECGL CYTSHVSLSR HLFIVHKLKE PQPAAKQNGA GEESQQENKP GPEDAPADGP
VSDRTCKVCA KTFETEAALN AHMRTHGMAF IKSKRVSSAE K
//
