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Database: UniProt
Entry: A0A1S3JPS8_LINUN
LinkDB: A0A1S3JPS8_LINUN
Original site: A0A1S3JPS8_LINUN 
ID   A0A1S3JPS8_LINUN        Unreviewed;       451 AA.
AC   A0A1S3JPS8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=HMG box-containing protein 1 {ECO:0000256|ARBA:ARBA00017229};
DE   AltName: Full=HMG box transcription factor 1 {ECO:0000256|ARBA:ARBA00030708};
DE   AltName: Full=High mobility group box transcription factor 1 {ECO:0000256|ARBA:ARBA00030026};
GN   Name=LOC106175083 {ECO:0000313|RefSeq:XP_013412362.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013412362.1};
RN   [1] {ECO:0000313|RefSeq:XP_013412362.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013412362.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Transcriptional repressor that binds to the promoter region
CC       of target genes. Plays a role in the regulation of the cell cycle and
CC       of the Wnt pathway. Binds preferentially to the sequence 5'-
CC       TTCATTCATTCA-3'. Binding to the histone H1.0 promoter is enhanced by
CC       interaction with RB1. Disrupts the interaction between DNA and TCF4.
CC       {ECO:0000256|ARBA:ARBA00025095}.
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DR   RefSeq; XP_013412362.1; XM_013556908.1.
DR   AlphaFoldDB; A0A1S3JPS8; -.
DR   EnsemblMetazoa; XM_013556908.1; XP_013412362.1; LOC106175083.
DR   GeneID; 106175083; -.
DR   OrthoDB; 2882425at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd21988; HMG-box_HBP1; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   InterPro; IPR003652; Ataxin_AXH_dom.
DR   InterPro; IPR036096; Ataxin_AXH_dom_sf.
DR   InterPro; IPR039655; HBP1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   PANTHER; PTHR15499; HMG BOX-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR15499:SF3; HMG BOX-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF08517; AXH; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00536; AXH; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF102031; AXH domain; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS51148; AXH; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00267};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          165..311
FT                   /note="AXH"
FT                   /evidence="ECO:0000259|PROSITE:PS51148"
FT   DOMAIN          371..439
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        371..439
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  50486 MW;  75AA7868955ABCCB CRC64;
     MGRHKVDDDE DDDMLEVVTT TRSAKHTPPS LRLDSSDSSP IDVVSTTDGE DSNANHVTVQ
     PVSTSNWLEQ LAEIATGPKS PLIQKQSTAE RSPTKSFLEC SLHSYARPPR TRSPSPVRGN
     TRSLSSSASE SHFKYNCDES ESRVSSSSPF PSSPLDDSYG SSGSWSHSWP SAVWQCFIQG
     TRIRFTTGNK TEWQLAEDLA NTSYLTAQAS QDNLPKDSNY APNGLTLLHI EECKATEQRP
     VPFLRLRFSS DIPTQSEIIA ECALDHPFFV REKGWSSFHP SMTVEHYGIP CSELEVGDIT
     LPPSHPEATF TVDVFESFKS YDFTPMDSSA VFTLSTMAKK SKESDSWSPK SSPTTSPNRK
     RLSKPESPSK AKRPMNAFML FAKKYRVEYT QMYPGKDNRA ISCLLGERWK KLKSEERKAF
     SLEAKMLADQ HKKIHPDCWK RKRSTSTGSL E
//
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