ZXDC_MOUSE
ID ZXDC_MOUSE Reviewed; 858 AA.
AC Q8C8V1; Q3TEP2; Q3URC2; Q8C4U7; Q8C4Z9; Q8C8C2; Q8C8T1; Q99J65;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein ZXDC;
GN Name=Zxdc;
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hippocampus, Retina, and Thymus;
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 MRNA] (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 -!- FUNCTION: Cooperates with CIITA to promote transcription of MHC class I
CC and MHC class II genes. {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Interacts with ZXDB and CIITA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C8V1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C8V1-2; Sequence=VSP_026443, VSP_026444;
CC Name=3;
CC IsoId=Q8C8V1-3; Sequence=VSP_026441, VSP_026442;
CC Name=4;
CC IsoId=Q8C8V1-4; Sequence=VSP_026439, VSP_026440;
CC -!- PTM: Sumoylated at Lys-661 with SUMO1, SUMO2 and SUMO3; sumoylation
CC enhances the activity of the transcriptional activation domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZXD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03332.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC31967.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33082.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC38113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK044429; BAC31914.1; -; mRNA.
DR EMBL; AK044529; BAC31967.1; ALT_INIT; mRNA.
DR EMBL; AK047538; BAC33082.1; ALT_FRAME; mRNA.
DR EMBL; AK080307; BAC37873.1; -; mRNA.
DR EMBL; AK081005; BAC38113.1; ALT_INIT; mRNA.
DR EMBL; AK141613; BAE24766.1; -; mRNA.
DR EMBL; AK169517; BAE41206.1; -; mRNA.
DR EMBL; BC003332; AAH03332.1; ALT_FRAME; mRNA.
DR CCDS; CCDS20358.1; -. [Q8C8V1-1]
DR CCDS; CCDS51848.1; -. [Q8C8V1-2]
DR RefSeq; NP_084536.2; NM_030260.3. [Q8C8V1-2]
DR RefSeq; NP_766590.1; NM_173002.3. [Q8C8V1-1]
DR AlphaFoldDB; Q8C8V1; -.
DR SMR; Q8C8V1; -.
DR STRING; 10090.ENSMUSP00000074619; -.
DR iPTMnet; Q8C8V1; -.
DR PhosphoSitePlus; Q8C8V1; -.
DR MaxQB; Q8C8V1; -.
DR PaxDb; Q8C8V1; -.
DR PRIDE; Q8C8V1; -.
DR ProteomicsDB; 275250; -. [Q8C8V1-1]
DR ProteomicsDB; 275251; -. [Q8C8V1-2]
DR ProteomicsDB; 275252; -. [Q8C8V1-3]
DR ProteomicsDB; 275253; -. [Q8C8V1-4]
DR Antibodypedia; 33073; 111 antibodies from 20 providers.
DR DNASU; 80292; -.
DR Ensembl; ENSMUST00000045740; ENSMUSP00000036329; ENSMUSG00000034430. [Q8C8V1-3]
DR Ensembl; ENSMUST00000075117; ENSMUSP00000074619; ENSMUSG00000034430. [Q8C8V1-1]
DR Ensembl; ENSMUST00000113539; ENSMUSP00000109167; ENSMUSG00000034430. [Q8C8V1-2]
DR GeneID; 80292; -.
DR KEGG; mmu:80292; -.
DR UCSC; uc009cxf.2; mouse. [Q8C8V1-1]
DR UCSC; uc012eoy.1; mouse. [Q8C8V1-2]
DR CTD; 79364; -.
DR MGI; MGI:1933108; Zxdc.
DR VEuPathDB; HostDB:ENSMUSG00000034430; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162216; -.
DR HOGENOM; CLU_007312_0_0_1; -.
DR InParanoid; Q8C8V1; -.
DR OMA; QCIQIPV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8C8V1; -.
DR TreeFam; TF330996; -.
DR BioGRID-ORCS; 80292; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8C8V1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C8V1; protein.
DR Bgee; ENSMUSG00000034430; Expressed in ascending aorta and 244 other tissues.
DR ExpressionAtlas; Q8C8V1; baseline and differential.
DR Genevisible; Q8C8V1; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
DR GO; GO:0030275; F:LRR domain binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..858
FT /note="Zinc finger protein ZXDC"
FT /id="PRO_0000292804"
FT ZN_FING 176..200
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 209..233
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 239..263
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 269..291
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..322
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 329..353
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 359..383
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..413
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 419..443
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..477
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 356..363
FT /note="ERPFICDS -> MSCSVHLM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026439"
FT VAR_SEQ 364..858
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026440"
FT VAR_SEQ 505..512
FT /note="SELTNIDL -> RKWGLSKN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026441"
FT VAR_SEQ 513..858
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026442"
FT VAR_SEQ 712
FT /note="E -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026443"
FT VAR_SEQ 713..858
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026444"
FT CONFLICT 154
FT /note="L -> Q (in Ref. 1; BAE24766)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="P -> R (in Ref. 1; BAC38113)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="G -> V (in Ref. 1; BAC37873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 90755 MW; A7B31AFE64907C3B CRC64;
MDLPAVLAAP ATRGDQHGGG PSRLRRGAGP SLGAGPGRRR LLLLRGPEDG GPGPRPEEAP
GPSPPPPEDG GDSFVVLLEV PRAADTHGQE EAEPDSGASP TEQVPAAAPG AALAGTVTIH
NQDLLVRFDR GVFTLAAAPA PAAPSLHPAT TPGLEPSSAA ASRRGPVAAS AGSPAYRCPE
PQCALSFAKK HQLKVHLLTH GSLQGRRPFK CPLDGCGWAF TTSYKLKRHL QSHDKLRPFS
CPVGGCGKKF TTVYNLKAHM KGHEQESLFK CEVCAERFPT HAKLNSHQRS HFEPERPYKC
DFPGCEKTFI TVSALFSHNR AHFREQELFS CSFPGCNKQY DKACRLKIHL RSHTGERPFI
CDSDSCGWTF TSMSKLLRHK RKHDDDRRFT CPVEGCGKSF TRAEHLKGHS ITHLGTKPFE
CPVEGCCARF SARSSLYIHS KKHLQDVGTP KSRCPVSSCN RLFTSKHSMK AHVVRQHSRR
QDLVPQLEAP SSLTPSSELS SPGQSELTNI DLAALFSDTP ANSSSSTAGS DEALNSGILT
IDVTSVSSSL GGNLPTNNNS LGPMDPLVLV AHGDMPPSLD SPLVLGTSAT VLQPGSFSAD
DSQAMSTGAV GCLVALPVRN LNQDSPALTP SNNLTAPGTT PTSSDTTQET GSVPDLLVPI
KVEQDLSPVP DVVQGQKESH GPSQSVLSSS TERPGAQKDS ELSAGTGSLY LESGGSARTD
YRAIQLVKKK KQKGTGSDEG ASDSAHRKVK GGTINPPHVH SGQHSCFCGT LMVPSGGLTV
PAPAAGLQCV QIPVLQDDPS GEGGLPLGLS PQRSAFHPYF TVDLPVYVLQ EVLPAPGGFA
GLETAQVPGS TINLRDLE
