ID A0A084WP03_ANOSI Unreviewed; 1121 AA.
AC A0A084WP03;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14 {ECO:0000256|ARBA:ARBA00015071};
GN ORFNames=ZHAS_00020114 {ECO:0000313|EMBL:KFB51947.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB51947.1};
RN [1] {ECO:0000313|EMBL:KFB51947.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC020114-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ZC3H14 family.
CC {ECO:0000256|ARBA:ARBA00008423}.
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DR EMBL; ATLV01024805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525361; KFB51947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WP03; -.
DR STRING; 74873.A0A084WP03; -.
DR EnsemblMetazoa; ASIC020114-RA; ASIC020114-PA; ASIC020114.
DR VEuPathDB; VectorBase:ASIC020114; -.
DR VEuPathDB; VectorBase:ASIS008254; -.
DR OMA; FCEYYHP; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
DR Gene3D; 4.10.1000.30; -; 2.
DR Gene3D; 1.20.1390.10; PWI domain; 1.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR PANTHER; PTHR14738:SF29; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 14; 1.
DR Pfam; PF14608; zf-CCCH_2; 3.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 960..985
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 986..1006
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1055..1079
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 960..985
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 986..1006
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 1055..1079
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 87..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 125635 MW; 11678C3D995B2307 CRC64;
MDSLGTEIGQ KMRSAVKAKL IELGTGSASG YIDDELPDYV MIMVANKRSR QQMIDDLSLF
LGAQTEVFVN WLHQVLQKLQ EVTLPASAAT KKKPSEAEEK RKDKKRKDKK AKRRDRSTDN
EEEATDEPGP TRSTDGNNTP PQPAVVLPGS SITEVFANQY IEKAKKSLES APITKKTPQE
SAAARDQRSK TPPTTRALPS ITEIASATVV RKHHKELCEL EEIQQRINEA KRHLKTLGTD
ISDDDDEDLL HLKANEDDLE TEESRNERTS TAVARSNKPV DREATVNKQR QRITIASPEP
SKQVTAARNT TPPKTSEKDT SASSTVAKKR SVLDRLGTKS SVTSDSAKNE KSKASEPDAN
EISSKTATKP AATGTESTNN TKSTIISLSA HRREEREIYV PLFRRKEESS YRRGARAENP
PVREARTRER SRSRERNSAS GRERSASIGR QSKNGIDSVR GRIGSRIIVL PPKPEFQEDE
IEVPVASVIK VQPRPTMPKS KQPSKNLLLK AMAEAQRSTV ATVRKTIDNT PSMMDSKLSH
YSRMEGKRKL VIEIPGGHSV HPGMEVQYAD EDEEHYQLHR NVPLYGEFLD DEEVHEVDLA
KQVLMEECDV DEEFKDILQS ENEAATHRIH QREQPHHSEY AAEDSENMVH PATTMAESEN
TKFVVTLDGA YKSILDGDGS PSHTPPPPAS SVVGGTVKGR LSVKDRIGPK QPSSSSRERS
PKAKDSKELE ETLKKRKERF SEKLVAVSAP KSPQPKKSLS PPPPSTTTNR GSKQQSQPRS
PKLPSSTRSS HSTQSHASSQ RRTPSPGHLN ELLLQRTREL MDDSVSSSPI YMSKSDYDKM
EPSSRKRKRV SPIQFDLTDE DDMHDSEDDY HRDRRARSRD ERNPRRSRQR DSEERRSAPR
KDSRREWDRE SERRDSNAAR QSPGKKIKKL ESSRKFDDLP PLLSAVTVSD GKTHKSVGGG
AIKERCKYFP NCRQGDACEF LHPSTPCKAF PNCKFGDKCL YLHPMCKYDL TCHRLDCTFM
HTKGSSVAGS SSSLAAPPLA SSVVPVQNYK TISAKPLPPL CKFYPNCVNG QCPFYHPKMC
RFGRHCVNKV ECNFYHHELP PSEMHEASAK DKFKWISPFS A
//
