ZCHC7_MOUSE
ID ZCHC7_MOUSE Reviewed; 541 AA.
AC B1AX39; Q3TZN5; Q8C915; Q9CYZ9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Zinc finger CCHC domain-containing protein 7;
DE AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC7;
GN Name=Zcchc7; Synonyms=D4Wsu132e;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
CC -!- SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AX39-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AX39-3; Sequence=VSP_036901, VSP_036902;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI17021.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI17023.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI44775.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAC31499.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAE34173.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK013175; BAB28692.1; -; mRNA.
DR EMBL; AK043238; BAC31499.1; ALT_SEQ; mRNA.
DR EMBL; AK050430; BAC34252.1; -; mRNA.
DR EMBL; AK157728; BAE34173.1; ALT_SEQ; mRNA.
DR EMBL; AL805896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02416.1; -; Genomic_DNA.
DR EMBL; CH466565; EDL02418.1; -; Genomic_DNA.
DR EMBL; BC054405; AAH54405.1; -; mRNA.
DR EMBL; BC117020; AAI17021.1; ALT_SEQ; mRNA.
DR EMBL; BC117022; AAI17023.1; ALT_SEQ; mRNA.
DR EMBL; BC144774; AAI44775.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18127.2; -. [B1AX39-1]
DR RefSeq; NP_613056.2; NM_138590.4. [B1AX39-1]
DR RefSeq; XP_006538047.1; XM_006537984.3. [B1AX39-1]
DR AlphaFoldDB; B1AX39; -.
DR BioGRID; 235596; 14.
DR STRING; 10090.ENSMUSP00000103454; -.
DR iPTMnet; B1AX39; -.
DR PhosphoSitePlus; B1AX39; -.
DR EPD; B1AX39; -.
DR MaxQB; B1AX39; -.
DR PaxDb; B1AX39; -.
DR PeptideAtlas; B1AX39; -.
DR PRIDE; B1AX39; -.
DR ProteomicsDB; 302116; -. [B1AX39-1]
DR ProteomicsDB; 302117; -. [B1AX39-3]
DR Antibodypedia; 11966; 96 antibodies from 17 providers.
DR DNASU; 319885; -.
DR Ensembl; ENSMUST00000107824; ENSMUSP00000103454; ENSMUSG00000035649. [B1AX39-1]
DR Ensembl; ENSMUST00000147272; ENSMUSP00000126678; ENSMUSG00000035649. [B1AX39-3]
DR GeneID; 319885; -.
DR KEGG; mmu:319885; -.
DR UCSC; uc008sry.2; mouse. [B1AX39-1]
DR UCSC; uc008ssa.2; mouse. [B1AX39-3]
DR CTD; 84186; -.
DR MGI; MGI:2442912; Zcchc7.
DR VEuPathDB; HostDB:ENSMUSG00000035649; -.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_029787_0_0_1; -.
DR InParanoid; B1AX39; -.
DR OMA; SHAYCYN; -.
DR OrthoDB; 1535084at2759; -.
DR PhylomeDB; B1AX39; -.
DR TreeFam; TF329448; -.
DR BioGRID-ORCS; 319885; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Zcchc7; mouse.
DR PRO; PR:B1AX39; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AX39; protein.
DR Bgee; ENSMUSG00000035649; Expressed in optic fissure and 271 other tissues.
DR ExpressionAtlas; B1AX39; baseline and differential.
DR Genevisible; B1AX39; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043629; P:ncRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IBA:GO_Central.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IBA:GO_Central.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 4.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..541
FT /note="Zinc finger CCHC domain-containing protein 7"
FT /id="PRO_0000370241"
FT ZN_FING 236..253
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 258..275
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 299..316
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 343..360
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 111..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 530
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT VAR_SEQ 1..321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036901"
FT VAR_SEQ 322..324
FT /note="HLT -> MLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036902"
SQ SEQUENCE 541 AA; 63000 MW; 13CA0805AC34E419 CRC64;
MFGGYETIEA FEDDLYRDDS SSELSVDSEV EFQLYSQVHY AQSIHNANKE EGYEEKNCEN
SETVSSQPNQ KNLIVLSDSE VIQLSDTSEV ITLSDEDSIY RCKRKNIEVQ AEEKTQSPAT
SHSNKVAQKC KRNNKKPKPE ERPGVIREVM IIEVSSNEEE ESTTSENENV ESWMLLGSEE
DGKDNDILLN LVGCETAGAE DDVNWFISDK DIEAKIDNNR SSGRWNNRYY SVNKNVTCRN
CDKRGHLSKN CPLPQKVRAC CLCSERGHLQ YGCPARYCLD CSLPMSSNHR CFERLSWRKR
CDRCDMIGHH ADACPEIWRQ YHLTTKPGPP KKPKTPSGQS ALVYCYNCAQ KGHYGHECTE
RRMFNQTFPT SPFIYCYDGK YDIQQRDRRI KRKVKDLKKN GDFPRQFKRP HVEETDKRRH
HDMRKSRSPR KYRRWPRENK ETQKEKTRSR EGKTHRRGHQ PRGEDEDFPR GSKPNASGCA
NNQKPSKSLH HASHYHRLRE ERLLRESKRS KPKKRKSTED GSHDDLFLIK QKKKKPKPSG
L
