Entry euk: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   10-MAY-2017, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
CC       associating with U7 snRNP and interacting with SLBP/pre-mRNA
CC       complex. Increases histone 3'-end pre-mRNA processing but has no
CC       effect on U7 snRNP levels, when overexpressed. Required for cell
CC       cycle progression from G1 to S phases (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the SLBP/pre-mRNA complex but not with
CC       SLBP alone. Interacts with LSM11 in a U7 snRNP-dependent manner
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Stable component
CC       of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA
CC       (By 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
CC       complex and histone pre-mRNA processing. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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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   UniGene; Mm.382935; -.
DR   ProteinModelPortal; Q8BI67; -.
DR   SMR; Q8BI67; -.
DR   BioGrid; 232592; 7.
DR   STRING; 10090.ENSMUSP00000051069; -.
DR   PhosphoSitePlus; Q8BI67; -.
DR   PaxDb; Q8BI67; -.
DR   PRIDE; Q8BI67; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00840000130048; -.
DR   HOGENOM; HOG000234617; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q8BI67; -.
DR   KO; K09228; -.
DR   OMA; HIRENTS; -.
DR   OrthoDB; EOG091G02KC; -.
DR   PhylomeDB; Q8BI67; -.
DR   TreeFam; TF350932; -.
DR   Reactome; R-MMU-109688; Cleavage of Growing Transcript in the Termination Region.
DR   Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR   Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR   PRO; PR:Q8BI67; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000048012; -.
DR   CleanEx; MM_ZFP473; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01352; KRAB; 1.
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   Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    892       Zinc finger protein 473 homolog.
FT                                /FTId=PRO_0000047605.
FT   DOMAIN       23    101       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     209    231       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     265    287       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     377    399       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     404    426       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     432    454       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     460    482       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     488    510       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     516    538       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     544    566       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     572    594       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     697    719       C2H2-type 11; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     725    747       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     753    775       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     781    803       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     809    831       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     837    859       C2H2-type 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     865    887       C2H2-type 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CONFLICT     65     66       TD -> N (in Ref. 1; BAC29437).
FT                                {ECO:0000305}.
FT   CONFLICT    396    396       Q -> K (in Ref. 1; BAC26780).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       865    892       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       839    859       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       404    426       ismart:ZnF_C2H2 [T]
FT   MYHIT       209    236       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       837    864       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       781    803       ismart:ZnF_C2H2 [T]
FT   MYHIT       406    426       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       265    287       ismart:ZnF_C2H2 [T]
FT   MYHIT       460    482       ismart:ZnF_C2H2 [T]
FT   MYHIT       697    724       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       432    459       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       753    775       ismart:ZnF_C2H2 [T]
FT   MYHIT       377    400       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       753    780       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       811    831       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       546    566       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       572    599       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       432    454       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       460    487       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       516    543       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       488    510       ismart:ZnF_C2H2 [T]
FT   MYHIT       265    292       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        24     63       ipfam:KRAB [T]
FT   MYHIT       837    859       ismart:ZnF_C2H2 [T]
FT   MYHIT       725    747       ismart:ZnF_C2H2 [T]
FT   MYHIT       865    887       ismart:ZnF_C2H2 [T]
FT   MYHIT       574    594       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       404    431       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       209    231       ismart:ZnF_C2H2 [T]
FT   MYHIT       516    538       ismart:ZnF_C2H2 [T]
FT   MYHIT       488    515       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT        23    101       iprf:KRAB [T]
FT   MYHIT       432    454       ismart:ZnF_C2H2 [T]
FT   MYHIT       809    836       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       755    775       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       462    482       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       377    399       ismart:ZnF_C2H2 [T]
FT   MYHIT       572    594       ismart:ZnF_C2H2 [T]
FT   MYHIT       490    510       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       783    803       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       697    719       ismart:ZnF_C2H2 [T]
FT   MYHIT       518    538       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       867    887       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       379    399       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       809    831       ismart:ZnF_C2H2 [T]
FT   MYHIT       267    287       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       544    571       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       727    747       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       781    808       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       544    566       ismart:ZnF_C2H2 [T]
FT   MYHIT       725    752       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       211    231       ipat:ZINC_FINGER_C2H2_1 [T]
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
//