ADN3_SCHPO
ID ADN3_SCHPO Reviewed; 964 AA.
AC O74522; Q9UTW9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Adhesion defective protein 3;
DE AltName: Full=LisH domain-containing protein adn3;
GN Name=adn3; ORFNames=SPCC1494.10, SPCC70.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 420-596, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION.
RX PubMed=19542312; DOI=10.1128/ec.00078-09;
RA Dodgson J., Avula H., Hoe K.L., Kim D.U., Park H.O., Hayles J.,
RA Armstrong J.;
RT "Functional genomics of adhesion, invasion, and mycelial formation in
RT Schizosaccharomyces pombe.";
RL Eukaryot. Cell 8:1298-1306(2009).
CC -!- FUNCTION: Probable transcriptional regulator involved in cell adhesion.
CC {ECO:0000269|PubMed:19542312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus
CC {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the FLO8 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19308.1; -; Genomic_DNA.
DR EMBL; AB027952; BAA87256.1; -; Genomic_DNA.
DR PIR; T41011; T41011.
DR PIR; T41547; T41547.
DR RefSeq; NP_588535.2; NM_001023523.2.
DR AlphaFoldDB; O74522; -.
DR SMR; O74522; -.
DR BioGRID; 275305; 38.
DR STRING; 4896.SPCC1494.10.1; -.
DR iPTMnet; O74522; -.
DR MaxQB; O74522; -.
DR PaxDb; O74522; -.
DR PRIDE; O74522; -.
DR EnsemblFungi; SPCC1494.10.1; SPCC1494.10.1:pep; SPCC1494.10.
DR GeneID; 2538721; -.
DR KEGG; spo:SPCC1494.10; -.
DR PomBase; SPCC1494.10; adn3.
DR VEuPathDB; FungiDB:SPCC1494.10; -.
DR eggNOG; ENOG502R28W; Eukaryota.
DR HOGENOM; CLU_306979_0_0_1; -.
DR InParanoid; O74522; -.
DR OMA; VHANEDI; -.
DR PRO; PR:O74522; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:PomBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:PomBase.
DR InterPro; IPR006594; LisH.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..964
FT /note="Adhesion defective protein 3"
FT /id="PRO_0000116893"
FT DOMAIN 34..66
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 104592 MW; B8CC13AD417D66F4 CRC64;
MADFMDIEPS SHSAKASQYE SSAPASSSLG NSHPNESLDY YIYDYFVKHN FEEAAQAFLR
ESKIQIPKSS SSTAFSPSNN NAPSPFPPKN SSLASPSKIS ESISGDRLYN HMSSAPSPNK
KEETNVVHAN EDISLDKRQS FGSSSLPPSE VSINVPEGFL VEWFNIFWDV FSARVSRVNS
TPIQLYDPST QRQMARPMSN LQASQPVPSS TFSRSAVVPN PSLPLNPSVL QGQVMNNPTI
PKGTPSTSIE GAKTSIPPSH AMQNPHNSFP ASADRLQKNH PVQSSNFNPY TPAPSITVPP
NYIPNTAMMG PSYSSFGDTD PRTYPAGMGP NPTAARNGFY PPTPAQIHQL KAQQQHLQRQ
SKQMSEPAPI NMKSNKDQQL QYVDFRGVGS GADLQKQQWN KSTSAEGLQP NGLVMRNFGD
VRHQKLPTSS PPSQHPPVGQ IPSQYLPYQA GLKVPGNTPI PVKQVGGMPL QSPLPVSMKP
SADDHSRATP TRSVEAPTLP SYAPRHPTQA NGSRYMNPST SRMTPQSPYM QNYYRPHAQM
QDQNNMMSYM LSQQKAMEIA KSREMAIQRN TQTLSSGNQP PQQSGPNPNE FSMSMDPANM
QQGNHALSDY HMQLMLLEEQ NKKRLMMARQ EQGTGSLSPQ SYMNSRYSVD VGKEHMSMIP
NQTAPMIQPN VPVSANSPAQ ANTPAADSTK SGTIQPTNRN GEGLSYSPHQ QFSPSAPQAE
KLSRSMSPFV SQQQQLNQPV SNKPDGLTQN KEVTGMPLNK EELTNPAFPQ SRTSWMMPQS
FDTSSLNAPG AKDSSSFSSL HAQPGKSGIA TMGVADNTIR TTERSTFSEI MKDSPSAHAS
PGAKTSPNAS RAPEPTGGTN SISQDTTQSL QMQSNSVNSS SMVDASKSKE KSGGDTSALD
SNAKNEPTAA KPISKLEDDA LFNDSAGNAF GFSSKTDSNV EMLNDFDFES FLNDAGADSA
SVYY
