ID A0A1V9XLB8_9ACAR Unreviewed; 339 AA.
AC A0A1V9XLB8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Nucleoporin NUP42 {ECO:0000256|ARBA:ARBA00039886};
DE AltName: Full=Nucleoporin-like protein 2 {ECO:0000256|ARBA:ARBA00042384};
GN ORFNames=BIW11_09259 {ECO:0000313|EMBL:OQR74162.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR74162.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR74162.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR74162.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- FUNCTION: Required for the export of mRNAs containing poly(A) tails
CC from the nucleus into the cytoplasm. {ECO:0000256|ARBA:ARBA00037262}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000256|ARBA:ARBA00004335};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004335};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004335}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR74162.1}.
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DR EMBL; MNPL01008591; OQR74162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XLB8; -.
DR STRING; 418985.A0A1V9XLB8; -.
DR InParanoid; A0A1V9XLB8; -.
DR OrthoDB; 232322at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46527:SF1; NUCLEOPORIN NUP42; 1.
DR PANTHER; PTHR46527; NUCLEOPORIN-LIKE PROTEIN 2; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 170..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37166 MW; 398764A6AD4381E8 CRC64;
MTVCRYFLNG NCRYGQSCRY DHVYDGVSSR GGRHGSGNHY SNYHYSNNNH PQQQSINRGG
GVLQEGSAFN FSQAALELSS HKTQETDQVR QELKHMLEGH FYPFTVVPGA TQQMNFSHLS
DLSPEEIRLR AYESLAANRF HEYQSEMAKH TSHVMQIIRQ IIASPQLMQE SRAKPGAGPV
VPSIVTPSAP LPSQHQSNSA NFPQPGIGGT QMKRITACMA QVSPAPFAEH APLANNTQRQ
FSQHSSSGFA PGHTTQGPST DTAAVQNSVP NIQPFSNPPV MPPASSKITD PPGPSNQQHN
KDTTYSPMDA LSEIDLAAFR DRMFTLDNLP LAAPPKELC
//