ZC11A_PONAB
ID ZC11A_PONAB Reviewed; 811 AA.
AC Q5REG6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Zinc finger CCCH domain-containing protein 11A;
GN Name=ZC3H11A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in nuclear mRNA export; probably mediated by
CC association with the TREX complex. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with THOC2, DDX39 and POLDIP3; the interactions are
CC ATP-dependent and indicative for an association with the TREX complex.
CC {ECO:0000250}.
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DR EMBL; CR857563; CAH89841.1; -; mRNA.
DR RefSeq; NP_001124854.1; NM_001131382.1.
DR AlphaFoldDB; Q5REG6; -.
DR STRING; 9601.ENSPPYP00000000361; -.
DR GeneID; 100171715; -.
DR KEGG; pon:100171715; -.
DR CTD; 9877; -.
DR eggNOG; KOG4791; Eukaryota.
DR InParanoid; Q5REG6; -.
DR OrthoDB; 265128at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISS:UniProtKB.
DR InterPro; IPR041686; Znf-CCCH_3.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF15663; zf-CCCH_3; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Isopeptide bond; Metal-binding; mRNA transport;
KW Phosphoprotein; Reference proteome; Repeat; Transport; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..811
FT /note="Zinc finger CCCH domain-containing protein 11A"
FT /id="PRO_0000213907"
FT ZN_FING 2..30
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 32..58
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 61..87
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 140..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..424
FT /evidence="ECO:0000255"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
SQ SEQUENCE 811 AA; 89320 MW; 75155ADFD9838076 CRC64;
MPNQGEDCYF FFFYSTCTKG DSCPFRHCEA ALGNETVCTL WQEGRCFRQV CRFRHMEIDK
KRSEIPCYWE NQPTGCQKLN CAFHHNRGRY VDGLFLPPSK TVLPTVPESP EEEVKASQLS
VQQNKLSVQS NPSPQLRSVM KVESSENVPS PTHPPVVINA ADDDEDDDDQ FSEEGDETKT
PTLQPTPEVH NGLRVTSVRK PAVNIKQGEC LNFGIKTLEE IKSKKMKEKS KKQGEGSSGV
SSLLLHPEPV PGPEKENVRT VVRTVTLSTK QGEEPLVRLS LTERLGKRKF SAGGDSDPPL
KRSLAQRLGK KVEAPEANID KTPKRAQVSK SLKERLGMSA DPNNEDATEK VNKVGEIHVK
TLEEILLERA SQKRGELQTK LKTEGPSKTD DSTSGARSSS TIRIKTFSEV LAEKKHRQQE
AERQKSKKDT TCIKLKTDSE IKKTVVLPPI VASKGQSEEP AGKTKSMQEV HIKTLEEIKL
EKALRVQQSS ESSTSSPSQH EATPGARRLL RIAKRTGMKE EKNLQEGNEV DSQSSIRTEA
KEASGETTGV DITNIQVKRC ETMREKHMQK QQEREKSVLT PLRGDVASCN TQVAEKPVLT
AVPGITRHLT KRLPTKSSQK VEVEISGIGD SVLNVKYAAQ TLEKRGKAKP KVNVKPSVVK
VVSSPKLAPK RKAVEMHPAV IAAVKPLSSS SVLQEPPAKK AAVAVVPLVS EDKSVTVPEA
ENPRDSLVLP PTQSSSDSSP PEVSGPSSSQ MSMKTRRLSS ASTGKPQLSV EDDFEKLIWE
ISGGKLEAEI DLDPGKDEDD LLLELSEMID S
