ZN473_MOUSE
ID ZN473_MOUSE Reviewed; 892 AA.
AC Q8BI67; Q8BI98; Q8BIB7;
DT 31-AUG-2004, 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 473 homolog;
DE AltName: Full=Zinc finger protein 100;
DE Short=Zfp-100;
GN Name=Znf473; Synonyms=Zfp100, Zfp473;
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; TISSUE=Bone, and Testis;
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).
CC -!- FUNCTION: Involved in histone 3'-end pre-mRNA processing by associating
CC with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases
CC histone 3'-end pre-mRNA processing but has no effect on U7 snRNP
CC levels, when overexpressed. Required for cell cycle progression from G1
CC to S phases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SLBP/pre-mRNA complex but not with SLBP
CC alone. Interacts with LSM11 in a U7 snRNP-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Stable component of
CC Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The C2H2-type zinc fingers are involved in discrete Cajal
CC bodies localization, interaction with LSM11 and the SLBP/RNA complex
CC and histone pre-mRNA processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK030093; BAC26780.1; -; mRNA.
DR EMBL; AK036453; BAC29437.1; -; mRNA.
DR EMBL; AK050747; BAC34403.1; -; mRNA.
DR CCDS; CCDS21213.1; -.
DR RefSeq; NP_001276765.1; NM_001289836.1.
DR RefSeq; NP_001276766.1; NM_001289837.1.
DR RefSeq; NP_001276767.1; NM_001289838.1.
DR RefSeq; NP_001276768.1; NM_001289839.1.
DR RefSeq; NP_848849.2; NM_178734.4.
DR RefSeq; XP_006540941.1; XM_006540878.1.
DR RefSeq; XP_006540942.1; XM_006540879.1.
DR RefSeq; XP_006540944.1; XM_006540881.3.
DR RefSeq; XP_006540945.1; XM_006540882.1.
DR AlphaFoldDB; Q8BI67; -.
DR SMR; Q8BI67; -.
DR BioGRID; 232592; 32.
DR IntAct; Q8BI67; 7.
DR STRING; 10090.ENSMUSP00000051069; -.
DR iPTMnet; Q8BI67; -.
DR PhosphoSitePlus; Q8BI67; -.
DR jPOST; Q8BI67; -.
DR PaxDb; Q8BI67; -.
DR PRIDE; Q8BI67; -.
DR Antibodypedia; 32254; 125 antibodies from 20 providers.
DR DNASU; 243963; -.
DR Ensembl; ENSMUST00000060270; ENSMUSP00000051069; ENSMUSG00000048012.
DR Ensembl; ENSMUST00000120074; ENSMUSP00000113774; ENSMUSG00000048012.
DR GeneID; 243963; -.
DR KEGG; mmu:243963; -.
DR UCSC; uc009gqn.2; mouse.
DR CTD; 243963; -.
DR MGI; MGI:2442697; Zfp473.
DR VEuPathDB; HostDB:ENSMUSG00000048012; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00840000130048; -.
DR InParanoid; Q8BI67; -.
DR OMA; YSCAKCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BI67; -.
DR TreeFam; TF350932; -.
DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 243963; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Zbtb17; mouse.
DR PRO; PR:Q8BI67; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BI67; protein.
DR Bgee; ENSMUSG00000048012; Expressed in primary oocyte and 78 other tissues.
DR ExpressionAtlas; Q8BI67; baseline and differential.
DR Genevisible; Q8BI67; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..892
FT /note="Zinc finger protein 473 homolog"
FT /id="PRO_0000047605"
FT DOMAIN 23..101
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 209..231
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 265..287
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..399
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 488..510
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 516..538
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..719
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 725..747
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..775
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 781..803
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 809..831
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 837..859
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 865..887
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 66..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WTR7"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WTR7"
FT CONFLICT 65..66
FT /note="TD -> N (in Ref. 1; BAC29437)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="Q -> K (in Ref. 1; BAC26780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 892 AA; 101741 MW; 91A31C2BA0F07FE0 CRC64;
MERKEDDLKG GCWNQPAVAE EFETLKDLAM DFTVEDWKDL ESEWDQRDLF WDVTLNHYQD
MFSFTDTSQP SLTSQPDVRE ELEATSTEVP ETKSSPLQSG FVEEDFSQIM EIFSNGQLNF
EACIGEDWLN SFLGDPESLP RPDISDKESP ADHQSPESKS GLSPGPPLCT REDAVMSASP
EKTLTPVILK ESRSDLSQED SVQGHEKPYK CSECGESFSQ SHHLIQHWVL HTSGEPPIWR
EQQRGLSQGA HFPMCPGTPA SYESYTCQEC GKRFSQNVYL QWHQKIHTGE KLCKTQSDSN
LEGLSRSPSV EPGKQRLSKD TDSAKPSTIH GQDQEKPPTG ESRDQENLHE SQPGDRPSVL
HPKPLRHQKT PTNAKCFRCK KCGETFSGAF HLAKHQRAHA QRLYKCASCP AVFNLSKHCF
QHRKSHFPSA ACECQGCRKS FNWRSSLIKH QAIHKGEKPY KCDECGKAFN HSSTLKIHQR
IHSGQKPHKC SECGKAFCRR TDLTEHQRVH SGFRPHQCPV CARTFNRPSH LVRHRLRHAE
ERHFGCAKCK ETFIYKEQLE RHNKIHTIEG LYECKQCGEH FICRSTLNCH LSIHIRENTS
EKVVGQNSQH TEKCFKNTKC RKAPNHSRYL GQHEKIHAQV TSGECDPCGE TYDQSVQPIC
HQSICAGVKP SECAEPEKCT RNTSASEHHP SQREPSFKCD IYNRAFKQRA HLSKHQLIHI
TEKPFKCNEC DRAFKQSNYL IQHQKTHTAE KHFECSECGK TFHQRSCLSK HQKIHSGEKP
FKCGDCGKAF ISGAQLIRHQ RIHTGEKPYV CQECGKTFSQ SSCLTLHLRI HTGEKPYTCG
TCGKAFAQRA NQRKHERIHT GEKPYACGLC GKAFGLRTHL QQHQRIHTKA KP
