ID A0A2D0QZ01_ICTPU Unreviewed; 1439 AA.
AC A0A2D0QZ01;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Zinc finger protein 335 isoform X2 {ECO:0000313|RefSeq:XP_017323544.1};
GN Name=LOC108265565 {ECO:0000313|RefSeq:XP_017323544.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017323544.1};
RN [1] {ECO:0000313|RefSeq:XP_017323544.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017323544.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_017323544.1; XM_017468055.3.
DR GeneID; 108265565; -.
DR OrthoDB; 4239435at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
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; 8.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24403:SF36; ZINC FINGER PROTEIN 335; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 606..633
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 636..663
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 664..691
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 703..730
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 731..753
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 762..789
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 790..818
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1115..1142
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1171..1198
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1199..1227
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 158956 MW; 54E7469B5388360A CRC64;
MDSEDMEVES SSDVGHSGME EPSESGMAME SSEAMSADSS DAATLPALAP ESDCHVGQSS
EGIVVFIPET SSSTDVRGVH LPDSSSVAQS TSVSSVSTVT QSLLVSESPQ VLVHSSAVSE
GGMMVSDSTA STSSDLGSAI DKIIESTIGP DIMNGCIAVT SAEDDHAEAT QYLILQGPDD
GAPMVGQMSS SALCSRLTID ALSDGPTSTC LDQADLSESL QPDQPGHSDY SEHEDGSSSS
SSISRPDPDQ TGDPGQSRFE DYGADESEEP LRGYVAECSG AVECSDSSCV DDGTVRHSLA
DTAGSHLQDQ MECSESQAGP YISSSGTYST LPEPEAAPRE DDGVVVESGV AAGPGDRAPD
LAELEEMMEV VIVQQFKCKM CPYKSVSKDT LINHMRDRHF KPAGDPPKKR GRGRPRKSET
LAQLGAKMKK EPAEEDEDDI IDAGAIDDPE EDSDYNPADE QLRARTPTQR PSPASCSSSF
SSNSLKRPRR TVGPPRKFLY PQSYTETAVS VSQTSTIVDP QAPEEASSSG LENGTVSISN
GCTVEQGVSQ SDSENKDPSS NNGPDDEEFF PRRRGRPSRR FLRKKYKKYI NRNKYYKSLK
PLLRPHNCWI CGSRFLSQED LRFHVDSHEG NDPERFKCQQ CSYRCKRWSS LKEHMFNHQG
TKPFKCDVCD YSSVYKKDVV RHSAVHSKEK SKKTGLIPKV SEFPCPICHR VYPMQKRLTQ
HMKTHSSEKP HMCDKCGKSF KKRYTFKMHL LTHIQNCGNS LFKCEFCEVT CNDKKQLLNH
QLSHTNDKPF KCDYCKYSTS KEDFLLSHIA IKHTGEKPFC CDLCHFMTKH KKNLRLHMQC
RHPEAFERWC ESNPEEPVRR RRKPFFTLQQ IEALKQQHES QTLGSTIVTV DPLTLQTMEP
MGNASVSQDA LGNTTIIYEQ GQSSDLSAQN ALDLLLNMSN ARELVGNSLQ VAVLKSDGKT
LEAGPWVTAE SAGQDSSLQP QNIVTYHVSE NGETLVQEAL TQEEAAEGEQ EFAQIAISAY
ATAREFSVME QAAEEIHSTA TAYSVEESSA DHQTVEVSSE SVSLSTPLKE HKDKFYLSSS
LTDGVLQQVE LSSEAPGSPS QSSSSQPQQV NTKRFCCRVC METFHGRSDM ENHKRAHLDP
NTFKCPDCEF TATLWPEVKT HMAMHAYLRP HKCPSCSFAS KNKKDLRRHM MTHTNEKPFS
CEVCGQRFNR NGHLKFHMER LHTQDPPPRK PRSSSSQQTI IVNSDEEALA TLQTLQAGQT
VISPEQLQQA LGQEHIIVAQ EQSLSDQEDA AYIQQITTVD GQTVQHLMTA DNQVQYIISQ
DSVQHLIPQE YVVVSNGNHI QMEDGQIAHI QYEHDGTLLQ EQQIAVTHNG QIQYFPISTE
QQIVSSEDLE AAAHSAVTAV ADAAMAQGQT VYTTEATPEQ LEQMQQQGIQ YDVITFTRE
//
