
AC   T02332
XX
ID   T02332
XX
DT   21.01.1998 (created); ili.
CO   Copyright (C), QIAGEN.
XX
FA   Shn
XX
SY   schnurri; Shn.
XX
OS   fruit fly, Drosophila melanogaster
OC   eukaryota; animalia; metazoa; arthropoda; insecta; diptera; drosophiloidea; drosophilidae
XX
CL   C0001; CH.
XX
SZ   2578 AA; 277.6 kDa (cDNA) (calc.).
XX
SQ   MYQLALLFKLNYAKHIELISVFSLPLPLSSRFGIDEPTANTSQDNKFDNNMENATITTAK
SQ   HYKTAGKQYKTNKVNNTRRATAAAAAAAAAAATTTVTTAATPTKKRTYRETATATTVTQR
SQ   STNKANIAAAIALAAATEATASASASATATATDATLTASKAAATAAATTDAASGNSNSSS
SQ   KPSTSTRDKLGEVPLPTVDSNHIISNNNNNNNNNNTSNNNNNNHHSDNSISENNYEFKSR
SQ   DKASLSDSKMTLQQMAAVSSNQEPVAPNVANTMSNSSIINSQQTTVNATPATDEAPLGDR
SQ   SNISRYLHKKFKRLASTTEVDSWSATNGGGALQASGDAVRTTSLSSNSSLSPPPTTPLAN
SQ   GHHLMTQQQSHQQVQQQQQQQTPPPSVAIHEFSANFVNSNHVNAIGHEESIISNSGYKAA
SQ   GRTRTPLANSNSNTNSTSNSNSNHAANATLSPASFAQHQQLTQPTTVSPGIPGGAAAPNP
SQ   ACEKSGRYVCQYQNLICAKPSVLEKHIRAHTNERPYPCDTCGIAFKTKSNLYKHCRSRSH
SQ   AARARGLEVPADADDGLSDQDAELSNSSSELPSRAGSPYEEPINSPTPSPSTLSAAKSAY
SQ   IQQPPLPTYMQQLPLGSPAAGTLPPTTADNHHSATAQHRQSIDYKPYKPKFHNASLYSCS
SQ   SKELQQQQQQLQIQQQQQQHQLAQQKLSIQLPLVQQPSLAHPTLSPSTQMKMKHHINSHQ
SQ   IQLQLQQQQSLLAQQSLLAAMPPGGVYYLGQPSYYNQDTAAAIHQHALAIQQFQIHLAQQ
SQ   QQQQQQQQQHPPLVKAPPPMQQPPSLPPQQLVRANSQISSVATAPATPTPAANLSTFASS
SQ   SGGKQVNVAKVQEHISKLISQNEAIVENKEILLQKKYPKQLSRSRSFNNANSNNASQHGS
SQ   NASRLHANNSHNNTNAQMPERETKVNLAQAIFQKQQHQLQQQQQQQITQQQQQQLEQQNY
SQ   YTYIQQQQECQQQQLEPPNGVVKRNAYKPGVVMTTPVKQQQQLPPPPSPLPMQTMQYRQD
SQ   PATPVTKIEQPTTAVPVMSAKPKPTLVTVPVSSLSTSSLAPTPTTSTNPTSSSKTAPPPA
SQ   QVNNSIIKNLLLNARGLAVRLAKAMMLFIRVLSVQANSAVRRSEAAQQHLLSGCELKCPN
SQ   ESSIFAIPLQLDLAESTGTEEPHGQLEESLISGQEGWSQLKTKRSSLVLSRLSAAQTPAR
SQ   TSTVTAPTVTASAPAPAVATVTAPSSAPAPQIEALRFVDAPLPSPGPLLGKTPLVDYAQQ
SQ   STPRKAQDSVVITKMHEDRQFVIEAQPAKRIKTSDLVVASSSQQPTSFNFSFNNQNSSNS
SQ   VPELQSSKEERLRRFTSSGGSMIPISECPDLDNSPKMIRTPLLSGGSFQDVSVKVNNETG
SQ   SSSKERKLMALVSGSGLLGVSSGPQHFQFPPINSITAFNPLTLPPMSGGDKTTPVTPIPH
SQ   VPGMPGPGSLTPQMPLLPPPPQQLQLPIPSSRGRSPMRKQPSPLLLGGGSGELKALSPFG
SQ   GVQNVPSEFSRQPPTPAQRQALQWNSKETPKKAPFNFLRMADNVKTTEPEVRHFNLENVI
SQ   SGKQQELPLTPLHVDTPNGNAPEETSPVASASASAKSKFLRPTSLPLKPGTFTPKRHHGI
SQ   TPTANTLPLISPETPRPSKSCVQLYLNGHAYTYLGLKCSTKMFYCTVNCPQPSYVAGMHK
SQ   LSMYSVWQVCEENQPHPLGFKLKQVMALYDSRQRMLGNGSSTAMAGSGKLSYNLVASQQI
SQ   VSSPSTSSTSSAFYQGPLKTPPTVTIAALSEANVAAKANEEVQAKKLETSPSGQPLVGGY
SQ   ESHEDYTYIRGRGRGRYVCSECGIRCKKPSMLKKHIRTHTDVRPFTCSHCNFSFKTKGNL
SQ   TKHMQSKTHFKKCIELGINPGPMPPDSEFLDVDMDFDQQSSTSAGGRTSSMAGESDSDDY
SQ   SDNESESSDTDESKSRQKEHEAARGLLSLSMTPPIPQSVSPYPQLQDTPLPAASPANSIG
SQ   SSGSQPKRLVCSFTSPKPPFDYQKQEQYYSNPEESKPKRSVANEESAPMDLTKPRGSILL
SQ   ISPSPVSVPAHDLPKSQAQQMHDVIFGTSGNESGFMKTLISVSDKVRISAEMEEQAKHEA
SQ   EGEDVQLQTYIKEHALHQAKIKQSQFSRSYLINTLYTAASPVMSSSSTLFTANSRPVMSV
SQ   NEVPSIEVHEVKTPEAIESPRSAPEQAPVILAQIAQEENEEPNIAEPHNANLPAAVQQPD
SQ   VNEFTGVLGNPTAPPTSSVTATSVSTTTAAPVAPSSTANSTQPAQRTVIVGEDGFKSSTP
SQ   TSKIGDLQHVSYGRGVPPAPIAGDARPTCTMCSKTFQRQHQLTLHMNIHYMERKFKCEPC
SQ   SISFRTQGHLQKHERSEAHKNKVMMTSTFGVPTTSNPRPFECTDCKIAFRIHGHLAKHLR
SQ   SKTHVQKLECLQKLPFGTYAEIERAGISLTEIDTSDCENSLISLKLLAQKLQEKDPGKLS
SQ   SYTTPSGMMQLAQDAAGPVSQDSASEDGFSAAIASAIASLDNDSAGNTPKRASSMSEDET
SQ   VANGLNHSLKRRLPGSFSSTGEESDNPPESSGEKRARSGQELPLPVAVPVAASAAASN
XX
SC   Pir #56922
XX
FT       91   1792    PF00478; IMP dehydrogenase / GMP reductase domain.
FT      250    250
   PF00478; IMP dehydrogenase / GMP reductase domain.
FT      250    250    putative alternative start site [1].
FT      488    510
   putative alternative start site [1].
FT      488    510    SM00355; c2h2final6.
FT      488    515
   SM00355; c2h2final6.
FT      488    515    PS50157; ZINC_FINGER_C2H2_2.
FT      490    510
   PS50157; ZINC_FINGER_C2H2_2.
FT      490    510    zinc finger-like motif [3].
FT      513    547
   zinc finger-like motif [3].
FT      513    547    SM00451; ZnF_U1_5.
FT      516    540
   SM00451; ZnF_U1_5.
FT      516    540    PF00096; zf-C2H2.
FT      516    540
   PF00096; zf-C2H2.
FT      516    540    SM00355; c2h2final6.
FT      516    545
   SM00355; c2h2final6.
FT      516    545    PS50157; ZINC_FINGER_C2H2_2.
FT      664    673
   PS50157; ZINC_FINGER_C2H2_2.
FT      664    673    PF00904; Involucrin repeat.
FT      948    957
   PF00904; Involucrin repeat.
FT      948    957    PF00904; Involucrin repeat.
FT     1817   1839
   PF00904; Involucrin repeat.
FT     1817   1839    PF00096; zf-C2H2.
FT     1817   1839
   PF00096; zf-C2H2.
FT     1817   1839    SM00355; c2h2final6.
FT     1817   1844
   SM00355; c2h2final6.
FT     1817   1844    PS50157; ZINC_FINGER_C2H2_2.
FT     1842   1876
   PS50157; ZINC_FINGER_C2H2_2.
FT     1842   1876    SM00451; ZnF_U1_5.
FT     1845   1869
   SM00451; ZnF_U1_5.
FT     1845   1869    PF00096; zf-C2H2.
FT     1845   1869
   PF00096; zf-C2H2.
FT     1845   1869    PS50157; ZINC_FINGER_C2H2_2.
FT     1845   1869
   PS50157; ZINC_FINGER_C2H2_2.
FT     1845   1869    SM00355; c2h2final6.
FT     2307   2329
   SM00355; c2h2final6.
FT     2307   2329    PF00096; zf-C2H2.
FT     2307   2329
   PF00096; zf-C2H2.
FT     2307   2329    SM00355; c2h2final6.
FT     2307   2334
   SM00355; c2h2final6.
FT     2307   2334    PS50157; ZINC_FINGER_C2H2_2.
FT     2332   2366
   PS50157; ZINC_FINGER_C2H2_2.
FT     2332   2366    SM00451; ZnF_U1_5.
FT     2335   2359
   SM00451; ZnF_U1_5.
FT     2335   2359    PF00096; zf-C2H2.
FT     2335   2359
   PF00096; zf-C2H2.
FT     2335   2359    SM00355; c2h2final6.
FT     2335   2364
   SM00355; c2h2final6.
FT     2335   2364    PS50157; ZINC_FINGER_C2H2_2.
FT     2377   2411
   PS50157; ZINC_FINGER_C2H2_2.
FT     2377   2411    SM00451; ZnF_U1_5.
FT     2380   2404
   SM00451; ZnF_U1_5.
FT     2380   2404    PF00096; zf-C2H2.
FT     2380   2404
   PF00096; zf-C2H2.
FT     2380   2404    SM00355; c2h2final6.
FT     2380   2409
   SM00355; c2h2final6.
FT     2380   2409    PS50157; ZINC_FINGER_C2H2_2.
   PS50157; ZINC_FINGER_C2H2_2.
 XX
SF   similarity to human factors MBP-1(1) T00497 and HIV-EP2 T00939 is restricted to the zinc finger regions;
XX
FF   may be a transcription factor because of similarity to MBP-1(1) and HIV-EP2 [1] [2];
FF   involved in multiple patterning events that require dpp activity [1];
FF   might be a target of the dpp signaling pathway and respond to its stimulation by activating or repressing dpp-responsive genes [2];
FF   interaction with Mad T04378 in the presence of TkvA (Dpp Type-1 receptor) [4];
FF   Shn 1441-1635, preceding the 2nd set of paired zinc finger, is the strong Mad interaction domain (MID), whereas Shn 341-1069 and Shn 1776-2529 are the weak MIDs [4];
XX
BS   R10100.
XX
DR   TRANSPATH: MO000026329.
DR   EMBL: L42311;
DR   EMBL: U31368;
DR   UniProtKB: Q24107;
DR   UniProtKB: Q24605;
DR   FLYBASE: FBgn0003396; shn.
XX
RN   [1]; RE0006524.
RX   PUBMED: 7774017.
RA   Arora K., Dai H., Kazuko S. G., Jamal J., O'Connor M. B., Letsou A., Warrior R.
RT   The Drosophila schnurri gene acts in the Dpp/TGFbeta signaling pathway and encodes a transcription factor homologous to the human MBP family
RL   Cell 81:781-790 (1995).
RN   [2]; RE0006525.
RX   PUBMED: 7774018.
RA   Grieder N. C., Nellen D., Burke R., Basler K., Affolter M.
RT   Schnurri is required for Drosophila dpp signaling and encodes a zinc finger protein similar to the mammalian transcription factor PRDII-BF1
RL   Cell 81:791-800 (1995).
RN   [3]; RE0006655.
RA   TRANSFAC_Team.
RT   Revisions of transcription factor domains
RL   TRANSFAC Reports 1:0002 (1998).
RN   [4]; RE0016241.
RX   PUBMED: 11071761.
RA   Dai H., Hogan C., Gopalakrishnan B., Torres-Vazquez J., Nguyen M., Park S., Raftery L. A., Warrior R., Arora K.
RT   The zinc finger protein schnurri acts as a Smad partner in mediating the transcriptional response to decapentaplegic.
RL   Dev. Biol. 227:373-387 (2000).
XX
//
XX
SF   similarity to human factors MBP-1(1) T00497 and HIV-EP2 T00939 is restricted to the zinc finger regions;
XX
FF   may be a transcription factor because of similarity to MBP-1(1) and HIV-EP2 [1] [2];
FF   involved in multiple patterning events that require dpp activity [1];
FF   might be a target of the dpp signaling pathway and respond to its stimulation by activating or repressing dpp-responsive genes [2];
FF   interaction with Mad T04378 in the presence of TkvA (Dpp Type-1 receptor) [4];
FF   Shn 1441-1635, preceding the 2nd set of paired zinc finger, is the strong Mad interaction domain (MID), whereas Shn 341-1069 and Shn 1776-2529 are the weak MIDs [4];
XX
BS   R10100.
XX
DR   TRANSPATH: MO000026329.
DR   EMBL: L42311;
DR   EMBL: U31368;
DR   UniProtKB: Q24107;
DR   UniProtKB: Q24605;
DR   FLYBASE: FBgn0003396; shn.
XX
RN   [1]; RE0006524.
RX   PUBMED: 7774017.
RA   Arora K., Dai H., Kazuko S. G., Jamal J., O'Connor M. B., Letsou A., Warrior R.
RT   The Drosophila schnurri gene acts in the Dpp/TGFbeta signaling pathway and encodes a transcription factor homologous to the human MBP family
RL   Cell 81:781-790 (1995).
RN   [2]; RE0006525.
RX   PUBMED: 7774018.
RA   Grieder N. C., Nellen D., Burke R., Basler K., Affolter M.
RT   Schnurri is required for Drosophila dpp signaling and encodes a zinc finger protein similar to the mammalian transcription factor PRDII-BF1
RL   Cell 81:791-800 (1995).
RN   [3]; RE0006655.
RA   TRANSFAC_Team.
RT   Revisions of transcription factor domains
RL   TRANSFAC Reports 1:0002 (1998).
RN   [4]; RE0016241.
RX   PUBMED: 11071761.
RA   Dai H., Hogan C., Gopalakrishnan B., Torres-Vazquez J., Nguyen M., Park S., Raftery L. A., Warrior R., Arora K.
RT   The zinc finger protein schnurri acts as a Smad partner in mediating the transcriptional response to decapentaplegic.
RL   Dev. Biol. 227:373-387 (2000).
XX
//