ID A0A2U4BHK8_TURTR Unreviewed; 1365 AA.
AC A0A2U4BHK8;
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 X1 {ECO:0000313|RefSeq:XP_019792690.1, ECO:0000313|RefSeq:XP_019792691.1};
GN Name=ZNF532 {ECO:0000313|RefSeq:XP_019792690.1,
GN ECO:0000313|RefSeq:XP_019792691.1, ECO:0000313|RefSeq:XP_019792692.1,
GN ECO:0000313|RefSeq:XP_019792694.1, ECO:0000313|RefSeq:XP_019792695.1,
GN ECO:0000313|RefSeq:XP_019792696.1, ECO:0000313|RefSeq:XP_019792697.1,
GN ECO:0000313|RefSeq:XP_019792698.1, ECO:0000313|RefSeq:XP_019792699.1,
GN ECO:0000313|RefSeq:XP_019792700.1};
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_019792697.1};
RN [1] {ECO:0000313|RefSeq:XP_019792690.1, ECO:0000313|RefSeq:XP_019792691.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019792690.1,
RC ECO:0000313|RefSeq:XP_019792691.1};
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_019792690.1; XM_019937131.2.
DR RefSeq; XP_019792691.1; XM_019937132.2.
DR RefSeq; XP_019792692.1; XM_019937133.2.
DR RefSeq; XP_019792694.1; XM_019937135.2.
DR RefSeq; XP_019792695.1; XM_019937136.2.
DR RefSeq; XP_019792696.1; XM_019937137.2.
DR RefSeq; XP_019792697.1; XM_019937138.2.
DR RefSeq; XP_019792698.1; XM_019937139.2.
DR RefSeq; XP_019792699.1; XM_019937140.2.
DR RefSeq; XP_019792700.1; XM_019937141.2.
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 680..698
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 818..848
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 934..962
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 969..996
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1000..1028
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1089..1117
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1119..1147
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1267..1295
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1328..1350
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1365 AA; 149113 MW; 9CCA93FD43FE6061 CRC64;
MWKTQRSFLL QSFRLTCECL ELGGVMRGVG QELRVKLLEE AEKQFELSHR WFFKSGILEH
LIKFMTMGDM KTPDFDDLLA AFDIPDMVDP KAAIESGHDD QEGHIKQNAH VDDDSHTPSS
SDVGVSVIVK NVRNIDSSEG AEKDGHNPTG NGLHNGFLSA SSLDTYSKDG SKSLKGDVPT
SEVTLKDSAF SQFSPISSAE EFDDDEKIEV DDPPDKEDMR SGFRSNVLTG SVPQQDYDKL
KALGGEGLSK TGISTPGNLE KNKVVKRETE TNSINLSVYE PFKVRKMEDK LKENSEKVLE
NRVPEGKLSS EKNDASLGGV VPSRTKPSSK LSSCIAAIAA LSAKKAASDS SKEPVTNSRE
ASPLPKEVND SPRAIEKSPE SQSLIDGTKK ASLKQPDSPR SISSENSSKG SPSSPAGSTP
AIPKVRIKTI KTSSGEIKRT VTRVLPEVDL DAGKKPSEQT GSMVASVTSL LSSPTSAAVL
SSPPRAPLQS AVVTNAVAPA ELTPKQVTIK PVATAFLPVS AVKTAGSQVI NLKLANNTTV
KATVISAASV QSASSAIIKA ANAIQQQTVV VPASSLANAK LVPKTVHLAN LNLLPQGAQA
TSELRQVLTK PQQQIKQAII SAAASQPPKK VSRVQVVSSL QSSVVEAFNK VLSSVNPVPV
YIPNLSPPAN AGITLPTRGY KCLECGDSFA LEKSLTQHYD RRSVRIEVTC NHCTKNLVFY
NKCSLLSHAR GHKEKGVVMQ CSHLILKPVP ADQMIVSPSS NTPASSSALP SSSGAGTHTV
TKIQSGITGT VISAPSSTPI IPAMPLDEDP SKLCRHSLKC LECNEVFQDE TSLATHFQQA
ADTSGQKTCT VCQMLLPNQC SYASHQRIHQ HKSPYTCPEC GAICRSVHFQ THVTKNCLHY
TRRVGFRCVH CNVVYSDVAA LKSHIQGSHC EVFYKCPICP MAFKSAPSTH SHAYTQHPGI
KIGEPKIIYK CSMCDTVFTL QTLLYRHFDQ HIENQKVSVF KCPDCSLLYA QKQLMMDHIK
SMHGTLKSIE GPPNLGINLP LSIKPTTQNS ANQNKEDTRS VNGKEKLEKK SPSPVKKSLE
PKKVASPGWT CWECDRLFTQ RDVYISHVRK EHGKQMKKHP CRQCDKSFSS SHSLCRHNRI
KHKGIRKVYT CSHCPDSRRT FTKRLMLEKH IQLMHGIKDP DLKEMTEATN EEEAEIKEDT
KVPSPKRKLE EPVLEFRPPR GAITQPLKKL KINVFKVHKC AVCGFTTENL LQFHEHIPQH
KSDGSSHQCR ECGLCYTSHV SLSRHLFIVH KLKEPQPAAK QNGAGEESQQ ENKPGPEDAP
ADGPVSDRTC KVCAKTFETE AALNAHMRTH GMAFIKSKRV SSAEK
//