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Zinc finger and SCAN domain-containing protein 10 (Zinc finger protein 206)

 ZSC10_MOUSE             Reviewed;         782 AA.
Q3URR7; B7ZP53; Q20D61; Q20D62; Q20D63;
18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 112.
RecName: Full=Zinc finger and SCAN domain-containing protein 10;
AltName: Full=Zinc finger protein 206;
Name=Zscan10; Synonyms=Zfp206;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=129S1/Sv;
PubMed=16971461; DOI=10.1093/nar/gkl631;
Zhang W., Walker E., Tamplin O.J., Rossant J., Stanford W.L.,
Hughes T.R.;
"Zfp206 regulates ES cell gene expression and differentiation.";
Nucleic Acids Res. 34:4780-4790(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=129P2;
PubMed=17628018; DOI=10.1634/stemcells.2007-0085;
Wang Z.X., Kueh J.L., Teh C.H., Rossbach M., Lim L., Li P., Wong K.Y.,
Lufkin T., Robson P., Stanton L.W.;
"Zfp206 is a transcription factor that controls pluripotency of
embryonic stem cells.";
Stem Cells 25:2173-2182(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INDUCTION.
PubMed=17344211; DOI=10.1074/jbc.M611814200;
Wang Z.X., Teh C.H., Kueh J.L., Lufkin T., Robson P., Stanton L.W.;
"Oct4 and Sox2 directly regulate expression of another pluripotency
transcription factor, Zfp206, in embryonic stem cells.";
J. Biol. Chem. 282:12822-12830(2007).
[7]
FUNCTION, DNA-BINDING, AND INTERACTION WITH POU5F1 AND SOX2.
PubMed=19740739; DOI=10.1074/jbc.M109.016162;
Yu H.B., Kunarso G., Hong F.H., Stanton L.W.;
"Zfp206, Oct4, and Sox2 are integrated components of a transcriptional
regulatory network in embryonic stem cells.";
J. Biol. Chem. 284:31327-31335(2009).
-!- FUNCTION: Embryonic stem (ES) cell-specific transcription factor
required to maintain ES cell pluripotency. Can both activate and
/or repress expression of target genes, depending on the context.
Specifically binds the 5'-[GA]CGCNNGCG[CT]-3' DNA consensus
sequence. Regulates expression of POU5F1/OCT4, ZSCAN4 and
ALYREF/THOC4. {ECO:0000269|PubMed:16971461,
ECO:0000269|PubMed:17628018, ECO:0000269|PubMed:19740739}.
-!- SUBUNIT: Interacts with POU5F1/OCT4 and SOX2.
{ECO:0000269|PubMed:19740739}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00187, ECO:0000269|PubMed:16971461,
ECO:0000269|PubMed:17628018}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q3URR7-1; Sequence=Displayed;
Name=2;
IsoId=Q3URR7-2; Sequence=VSP_039228;
Name=3;
IsoId=Q3URR7-3; Sequence=VSP_039227;
-!- TISSUE SPECIFICITY: Embryonic stem (ES) cell-specific. Not
expressed in adult, except in testis.
{ECO:0000269|PubMed:16971461, ECO:0000269|PubMed:17628018}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
{ECO:0000269|PubMed:16971461}.
-!- INDUCTION: Transcriptionally regulated by POU5F1/OCT4 and SOX2.
{ECO:0000269|PubMed:17344211}.
-----------------------------------------------------------------------
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EMBL; DQ323929; ABC54589.1; -; mRNA.
EMBL; DQ323930; ABC54590.1; -; mRNA.
EMBL; DQ323931; ABC54591.1; -; mRNA.
EMBL; EF152498; ABM45916.1; -; mRNA.
EMBL; AK141259; BAE24621.1; -; mRNA.
EMBL; CH466606; EDL22251.1; -; Genomic_DNA.
EMBL; BC145638; AAI45639.1; -; mRNA.
CCDS; CCDS28451.1; -. [Q3URR7-1]
CCDS; CCDS70766.1; -. [Q3URR7-2]
CCDS; CCDS79510.1; -. [Q3URR7-3]
RefSeq; NP_001028597.2; NM_001033425.4. [Q3URR7-1]
RefSeq; NP_001276410.1; NM_001289481.1. [Q3URR7-2]
RefSeq; NP_001276411.1; NM_001289482.1. [Q3URR7-3]
RefSeq; NP_001276412.1; NM_001289483.1.
RefSeq; NP_001276413.1; NM_001289484.1.
UniGene; Mm.270315; -.
PDB; 4E6S; X-ray; 1.85 A; A=36-128.
PDBsum; 4E6S; -.
ProteinModelPortal; Q3URR7; -.
SMR; Q3URR7; -.
BioGrid; 237126; 1.
STRING; 10090.ENSMUSP00000093255; -.
iPTMnet; Q3URR7; -.
PhosphoSitePlus; Q3URR7; -.
PaxDb; Q3URR7; -.
PeptideAtlas; Q3URR7; -.
PRIDE; Q3URR7; -.
DNASU; 332221; -.
Ensembl; ENSMUST00000095595; ENSMUSP00000093255; ENSMUSG00000023902. [Q3URR7-1]
Ensembl; ENSMUST00000115509; ENSMUSP00000111171; ENSMUSG00000023902. [Q3URR7-3]
Ensembl; ENSMUST00000120967; ENSMUSP00000113386; ENSMUSG00000023902. [Q3URR7-2]
GeneID; 332221; -.
KEGG; mmu:332221; -.
UCSC; uc008ask.3; mouse. [Q3URR7-2]
UCSC; uc008asl.2; mouse. [Q3URR7-1]
UCSC; uc008asm.2; mouse. [Q3URR7-3]
CTD; 84891; -.
MGI; MGI:3040700; Zscan10.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00730000111047; -.
HOGENOM; HOG000234619; -.
HOVERGEN; HBG018163; -.
InParanoid; Q3URR7; -.
KO; K09230; -.
OMA; SHSPKKE; -.
OrthoDB; EOG091G02KC; -.
PhylomeDB; Q3URR7; -.
TreeFam; TF338010; -.
PRO; PR:Q3URR7; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023902; -.
ExpressionAtlas; Q3URR7; baseline and differential.
Genevisible; Q3URR7; MM.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR003309; SCAN_dom.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF02023; SCAN; 1.
SMART; SM00431; SCAN; 1.
SMART; SM00355; ZnF_C2H2; 14.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF57667; SSF57667; 8.
PROSITE; PS50804; SCAN_BOX; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 782 Zinc finger and SCAN domain-containing
protein 10.
/FTId=PRO_0000394248.
DOMAIN 1 71 SCAN box. {ECO:0000255|PROSITE-
ProRule:PRU00187}.
ZN_FING 292 315 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 321 343 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 349 371 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 377 399 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 421 443 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 467 489 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 495 517 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 523 545 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 551 573 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 579 601 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 607 629 C2H2-type 11. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 635 657 C2H2-type 12. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 669 691 C2H2-type 13. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 697 719 C2H2-type 14. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 104 175 Pro-rich.
MOD_RES 160 160 Phosphoserine.
{ECO:0000250|UniProtKB:Q96SZ4}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:Q96SZ4}.
VAR_SEQ 131 240 Missing (in isoform 3).
{ECO:0000303|PubMed:16971461}.
/FTId=VSP_039227.
VAR_SEQ 328 359 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16971461}.
/FTId=VSP_039228.
CONFLICT 306 306 V -> E (in Ref. 1; ABC54589/ABC54590/
ABC54591, 2; ABM45916 and 4; EDL22251).
{ECO:0000305}.
CONFLICT 546 546 V -> L (in Ref. 3; BAE24621).
{ECO:0000305}.
HELIX 39 47 {ECO:0000244|PDB:4E6S}.
TURN 53 55 {ECO:0000244|PDB:4E6S}.
HELIX 57 72 {ECO:0000244|PDB:4E6S}.
TURN 74 76 {ECO:0000244|PDB:4E6S}.
HELIX 79 93 {ECO:0000244|PDB:4E6S}.
HELIX 97 100 {ECO:0000244|PDB:4E6S}.
HELIX 101 103 {ECO:0000244|PDB:4E6S}.
HELIX 111 116 {ECO:0000244|PDB:4E6S}.
SEQUENCE 782 AA; 88355 MW; B521507A5C617AED CRC64;
MLAEPVPDAL EQEHPGAVKL EEDEVGEEDP RLAESRPRPE VAHQLFRCFQ YQEDMGPRAS
LGRLRELCNH WLRPALHTKK QILELLVLEQ FLSVLPPHVL SRLHGQPLRD GEEVVQLLEG
VPRDISHMGP LDFSFSAGKN APADIISEEQ NSPSQVPSHS PQTELPSEEI PALHPLNELP
PPQPAPIRPA EPEEWRLAPS SNWPMSPEPQ EILQDPRESN PSQGPSWLEE NSRDQELAAV
LESLTFEDTS EKRAWPANPL GFGSRMPDNE ELKVEEPKVT TWPVVIGAES QTEKPEVAGE
PLTQTVGQET SSTGWGGTPA DGSEVVKVRG ASDAPEPQGE MQFICTYCGV NFPEMSHLQA
HQLQSHPNLQ PHPSSRSFRC LWCGKTFGRS SILKLHMRTH TDERPHACHL CNRRFRQSSH
LTKHLLTHSS EPAFRCAECN QGFQRRSSLM QHLLAHAQGK NLTPNPEGKT KVPEMAAVLC
SHCGQTFKRR SSLKRHLRNH AKDKDHLSSE DPGSLSSSQE SNPYVCSDCG KAFRQSEQLM
IHTRRVHTRE RPFSCQVCGR CFTQNSQLIS HQQIHTGEKP HACPQCSKRF VRRAGLARHL
LTHGSLRPYH CAQCGKSFRQ MRDLTRHVRC HTGEKPCRCN ECGEGFTQNA HLARHQRIHT
GEKPHACDIC GHRFRNSSNL ARHRRSHTGE RPYSCPTCGR SFRRNAHLQR HLITHTGSKQ
EKEVPQECPE CGKSFNRSCN LLRHLLVHTG ARPYSCALCG RSFSRNSHLL RHLRTHARES
LY


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