ID A0A1L8I2M2_XENLA Unreviewed; 1341 AA.
AC A0A1L8I2M2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Zinc finger protein 532 {ECO:0000313|RefSeq:XP_018122122.1, ECO:0000313|RefSeq:XP_018122128.1};
GN Name=znf532.L {ECO:0000313|RefSeq:XP_018122122.1,
GN ECO:0000313|RefSeq:XP_018122128.1, ECO:0000313|RefSeq:XP_018122132.1,
GN ECO:0000313|RefSeq:XP_018122136.1, ECO:0000313|RefSeq:XP_041425780.1,
GN ECO:0000313|RefSeq:XP_041425788.1, ECO:0000313|RefSeq:XP_041425801.1,
GN ECO:0000313|Xenbase:XB-GENE-17341037};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018122122.1};
RN [1] {ECO:0000313|RefSeq:XP_018122122.1, ECO:0000313|RefSeq:XP_018122128.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018122122.1,
RC ECO:0000313|RefSeq:XP_018122128.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018122122.1,
RC ECO:0000313|RefSeq:XP_018122128.1};
RG RefSeq;
RL Submitted (APR-2022) 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_018122119.1; XM_018266630.1.
DR RefSeq; XP_018122122.1; XM_018266633.2.
DR RefSeq; XP_018122126.1; XM_018266637.1.
DR RefSeq; XP_018122128.1; XM_018266639.2.
DR RefSeq; XP_018122132.1; XM_018266643.2.
DR RefSeq; XP_018122136.1; XM_018266647.2.
DR RefSeq; XP_041425780.1; XM_041569846.1.
DR RefSeq; XP_041425788.1; XM_041569854.1.
DR RefSeq; XP_041425801.1; XM_041569867.1.
DR STRING; 8355.A0A1L8I2M2; -.
DR PaxDb; 8355-A0A1L8I2M2; -.
DR GeneID; 108718430; -.
DR KEGG; xla:108718430; -.
DR AGR; Xenbase:XB-GENE-17341037; -.
DR CTD; 108718430; -.
DR Xenbase; XB-GENE-17341037; znf532.L.
DR OMA; HIKQNVH; -.
DR OrthoDB; 5400362at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 108718430; Expressed in brain and 15 other cell types or tissues.
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; 7.
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; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
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:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 653..671
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 908..936
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 943..970
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 974..1002
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1065..1093
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1095..1123
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1243..1271
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1304..1326
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 147052 MW; FFAA1BEB85AE97BA CRC64;
MQGGVASAPT REHVRRDTTR MPVASSRRGR LYIKNKELHD NHHVIMGDMK TPDFDDLLAA
FDIPDMVDPK AAIESGHDDQ ESSIKQNSQE EDDAHVPSSS DVGVSVIVKN VRTVDSEASE
KDHHSAGNGL HNGFLTTSNL DRFNKEDHKP LKDNADTIMK ASSFNQFSPI SSAEEFDEDE
KIEVVDPPDR EALKSNFNSN ILEDSNDEKM YEDGKMHTGD HFIKAGIDLP GSSEKNKSSK
RDLEASSTNF SVYDTFKIQK LDEKLKESAQ RLLLETKDNE KIDTEKSEAN GGTISQLRAN
SSAKLSSCIA AIAALSAKKT VCDLKDLEPS SGGASPVLKE GDCSPTAADK SPDSQLTVQN
LIDGTKKVQA RQPDSPGSVS SETSSKGSPS SSGGSTPAIP KVRIKTIKTS SGEIKRMVTR
VLPDFDGEEL KKNLEPSSPV VVSSLLPSPS STPVLASPTR ASLQPIIGSP VATTDVTPKQ
VSIKPVATAF LPVSAVKTAG SQVINLKFGN NTTVKATVIS AASVQSASNA IIKAANAIQQ
QTVVVPASSL ANTKLVPKTV HFANLNLLPQ GSQTSELRQV LAKPQQQIKQ TLVAAAPTTP
PKRVSRVQVV ASSQSSVVEA FNKVLSSINP VPVYVPNLTP PANAGITLPT RGYKCLECGD
AFALEKSLLQ HYDRRSVRIE VTCNHCSKNL VFYNKCSLLS HARGHKEKGV VMQCSHLILK
PVPTDQMIVS SQNNASTTPS ATRQSAVAVV AHTVNKIQPG LQGPVISAPS SAPVTPAMPL
DEDPANLCRH SLKCLECSEV FQDETALATH YQQASDATAQ KTCSICMMML PNPCSYNCHQ
RIHQHKSPYT CPECGAICRS VHFQTHVTKN CLHYTRRVGY RCMHCNVVYS ELAALKCHIQ
GSHCEVFYKC PICPMAFKSA PSTHSHAYTQ HPGVKIGEPK IIYKCSMCDT VFTLQPLLFR
HFDQHLEHQK VSVFKCPDCS LLYAQKQLMM DHIKSMHGTL KSVEGPPKLG VNLPLSTKPT
TQNSTSPSKE DPKQVSKMEK SEKKNISPNK NSDSVVVKKA SNAGWTCWDC EQLFNQRDVY
ISHMRKEHGK QMKKHPCRQC DKSFSSSHSL CRHNRIKHKG IRKVYTCTHC PDSKRVFAKR
ILLEKHIQLM HGIKHLNVKE TPEEPAAEPA EHKKGPKVPH VKRKLEEPEV DFRPPKGAIA
QPLKKLKINV FKVHKCAVCG FTTENLLQFH EHIPQHKSNG SSYQCRECGL CYTSHVSLSR
HLFIVHKLKE PQPSPKQNGS GKDSQQENKP SAEKEAADPI ASGRTCKVCG KTFETDAVLN
THMRTHGMAF IKSKRMSSIE K
//
