ZC11A_MOUSE
ID ZC11A_MOUSE Reviewed; 792 AA.
AC Q6NZF1; Q6NXW9; Q6PDR6; Q80TU7; Q8C5L5; Q99JN6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger CCCH domain-containing protein 11A;
GN Name=Zc3h11a; Synonyms=Kiaa0663;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, CD-1, and FVB/N-3;
RC TISSUE=Kidney, Mammary tumor, and Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-493.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-493.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-149 AND SER-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58552.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC37127.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65623.4; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC066163; AAH66163.1; -; mRNA.
DR EMBL; BC005786; AAH05786.1; -; mRNA.
DR EMBL; BC066848; AAH66848.1; -; mRNA.
DR EMBL; BC058552; AAH58552.1; ALT_SEQ; mRNA.
DR EMBL; AK122341; BAC65623.4; ALT_INIT; mRNA.
DR EMBL; AK078105; BAC37127.1; ALT_FRAME; mRNA.
DR CCDS; CCDS15297.1; -.
DR RefSeq; NP_001263696.1; NM_001276767.1.
DR RefSeq; NP_653113.4; NM_144530.6.
DR RefSeq; XP_011246375.1; XM_011248073.2.
DR RefSeq; XP_011246376.1; XM_011248074.2.
DR RefSeq; XP_011246377.1; XM_011248075.1.
DR RefSeq; XP_011246378.1; XM_011248076.1.
DR AlphaFoldDB; Q6NZF1; -.
DR BioGRID; 214147; 8.
DR iPTMnet; Q6NZF1; -.
DR PhosphoSitePlus; Q6NZF1; -.
DR SwissPalm; Q6NZF1; -.
DR EPD; Q6NZF1; -.
DR jPOST; Q6NZF1; -.
DR MaxQB; Q6NZF1; -.
DR PaxDb; Q6NZF1; -.
DR PRIDE; Q6NZF1; -.
DR ProteomicsDB; 302109; -.
DR DNASU; 70579; -.
DR Ensembl; ENSMUST00000027736; ENSMUSP00000027736; ENSMUSG00000116275.
DR Ensembl; ENSMUST00000191896; ENSMUSP00000141255; ENSMUSG00000102976.
DR GeneID; 70579; -.
DR KEGG; mmu:70579; -.
DR UCSC; uc007cqm.1; mouse.
DR CTD; 9877; -.
DR MGI; MGI:1917829; Zc3h11a.
DR VEuPathDB; HostDB:ENSMUSG00000102976; -.
DR VEuPathDB; HostDB:ENSMUSG00000116275; -.
DR GeneTree; ENSGT00920000149095; -.
DR HOGENOM; CLU_019514_1_0_1; -.
DR InParanoid; Q6NZF1; -.
DR OMA; VMKPAVQ; -.
DR OrthoDB; 265128at2759; -.
DR PhylomeDB; Q6NZF1; -.
DR TreeFam; TF335608; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 70579; 6 hits in 41 CRISPR screens.
DR ChiTaRS; Zc3h11a; mouse.
DR PRO; PR:Q6NZF1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6NZF1; protein.
DR Bgee; ENSMUSG00000102976; Expressed in undifferentiated genital tubercle and 189 other tissues.
DR ExpressionAtlas; Q6NZF1; baseline and differential.
DR Genevisible; Q6NZF1; MM.
DR GO; GO:0000346; C:transcription export complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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; 3.
PE 1: Evidence at protein 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..792
FT /note="Zinc finger CCCH domain-containing protein 11A"
FT /id="PRO_0000213906"
FT ZN_FING 2..29
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 31..57
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 60..87
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 103..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..360
FT /evidence="ECO:0000255"
FT COMPBIAS 103..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75152"
FT CONFLICT 37
FT /note="C -> F (in Ref. 1; AAH58552)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="T -> A (in Ref. 1; AAH66848)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="E -> G (in Ref. 1; AAH66848)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Missing (in Ref. 1; AAH58552)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="E -> G (in Ref. 1; AAH66848)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="N -> T (in Ref. 3; BAC37127)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="V -> I (in Ref. 1; AAH05786)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="P -> S (in Ref. 1; AAH05786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 86492 MW; AA9AC0B1095D1B87 CRC64;
MPNQGEDCYF YFYSTCAKGD SCPFRHCEAA LGNETVCTLW QEGRCFRQVC RFRHMEIDKK
RSEIPCYWEN QPVGCQKLNC AFHHTRSRYV DGLFLPPSKT VLPTVPESQE EEVKTSQLTV
QQSKLSVQSN PSPQLRSVMK VESSENVPSP THPPVVINAA DDDEDDDDQF SEEGDESKTP
ALQPSPDVHN GLRVASARKP GVSLKQGECL NFGIKTLEEI KSKKMKEKSK KQGEGSSGVS
SVLQQPQPNP GPEKENVRTV VRMVTLSSKP EEPLVRLSLS ERLGKRKLSV GGDSDPPLKR
SLAQRLGKKV ESPETNIDKA PKKERGHKAG EIHVKTLEEI LLERASQKRG ELQTKLKAEE
PSGADDSPSG TKSSSSVRIK TFSEVLAEKK HRQQEMERQK SKKDTSCLTL TDDTEMKKTV
SLPTVAVSKG QPEEPAGRAR SMQEVHIKTL EEIKLEKALR VQQSSESSGN SRPQAEAAPG
TKRLLRITKR AGVKEEKKCG LEDSGDPPQS SVTKMEANET SDETISDPTK LAVNRCDTVK
EKHTQRLQER GASQKEKAAL SSVRGDEASS YTRVAGKPVL TAVSGVTRHL AKRLPVESSQ
KGEVETSGIG DSILNVKCAA QTLEKRSKVK PKVNVKPSVV KVVSAPKLAP KRKAVEMHSA
VIAAVKPLSS SSVLQESPTK KAAVAVVPLL SEDKPVTMSE TENPKDSSVL SSAQAASEPL
LPEGSGPSSS QTATKPRRLS SASTGKPPLS VEDDFEKLIW EISGGKLEAE IDLDPGKDED
DLLLELSEMI DS
