ID   SGF3_BOMMO              Reviewed;         351 AA.
AC   Q17237;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Silk gland factor 3;
DE            Short=SGF-3;
DE   AltName: Full=POU domain protein M1;
GN   Name=SGF3; Synonyms=POU-M1;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Kinshu X Showa; TISSUE=Silk gland;
RX   PubMed=7690034; DOI=10.1016/s0021-9258(19)36539-1;
RA   Fukuta M., Matsuno K., Hui C.-C., Nagata T., Takiya S., Xu P.-X., Ueno K.,
RA   Suzuki Y.;
RT   "Molecular cloning of a POU domain-containing factor involved in the
RT   regulation of the Bombyx sericin-1 gene.";
RL   J. Biol. Chem. 268:19471-19475(1993).
CC   -!- FUNCTION: Involved in the transcriptional regulation of sericin-1 gene.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Restricted to the middle silk gland.
CC   -!- DEVELOPMENTAL STAGE: Expression differentially regulated in the
CC       posterior and middle silk glands during the fourth molt/fifth
CC       intermolt.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M64781; AAA27841.1; -; mRNA.
DR   PIR; A48763; A48763.
DR   AlphaFoldDB; Q17237; -.
DR   SMR; Q17237; -.
DR   STRING; 7091.Q17237; -.
DR   PaxDb; 7091-BGIBMGA010868-TA; -.
DR   eggNOG; KOG3802; Eukaryota.
DR   InParanoid; Q17237; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0048699; P:generation of neurons; IEA:UniProt.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR013847; POU.
DR   InterPro; IPR000327; POU_dom.
DR   PANTHER; PTHR11636; POU DOMAIN; 1.
DR   PANTHER; PTHR11636:SF89; POU DOMAIN PROTEIN 2, ISOFORM B-RELATED; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00157; Pou; 1.
DR   PRINTS; PR00028; POUDOMAIN.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00352; POU; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00035; POU_1; 1.
DR   PROSITE; PS00465; POU_2; 1.
DR   PROSITE; PS51179; POU_3; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; Differentiation; DNA-binding; Homeobox;
KW   Neurogenesis; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..351
FT                   /note="Silk gland factor 3"
FT                   /id="PRO_0000100776"
FT   DOMAIN          149..223
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        241..300
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          61..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  38591 MW;  A6DFA4A59E9322B6 CRC64;
     MAATTYMPAE MELGNIGGYH AASPRSAEPA DMKYQHPLHS GGSPSPGAPV IGNPWTSLPP
     ADPWAMHQHH AHAHQPDVKP PPAPHDHRHL QHAAHGWHAP VVSPHYGAAR PSHCMEDTQC
     PCTNTICSET SSPRDPLHHH AMERDQPEED TPTSDDLEAF AKQFKQRRIK LGFTQADVGL
     ALGTLYGNVF SQTTICRFEA LQLSFKNMCK LKPLLQKWLE EADSTTGSPT SIDKIAAQGR
     KRKKRTSIEV SVKGALEQHF HKQPKPSAQE ITSLADSLQL EKEVVRVWFC NRRQKEKRMT
     PPNTLGGEMM EGMGHAHYGH GDVHGSPLQH SPPGLSPQHG LPQGAHTLAA H
//