HMGB3_CHICK
ID HMGB3_CHICK Reviewed; 202 AA.
AC P40618; F1NGP8; P36194;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=High mobility group protein B3;
DE AltName: Full=High mobility group protein 2a;
DE Short=HMG-2a;
DE AltName: Full=High mobility group protein 4;
DE Short=HMG-4;
GN Name=HMGB3; Synonyms=HMG2A, HMG4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=1562600; DOI=10.1016/0167-4781(92)90534-7;
RA Oka T., Endo Y., Ito M., Miyamoto K., Sasakawa T., Suzuki I., Natori Y.;
RT "Molecular cloning of chick liver HMG 2a cDNA and developmental expression
RT of HMG 2a mRNA.";
RL Biochim. Biophys. Acta 1130:224-226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7904558; DOI=10.1242/dev.119.2.433;
RA Funahashi J., Sekido R., Murai K., Kamachi Y., Kondoh H.;
RT "Delta-crystallin enhancer binding protein delta EF1 is a zinc finger-
RT homeodomain protein implicated in postgastrulation embryogenesis.";
RL Development 119:433-446(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Multifunctional protein with various roles in different
CC cellular compartments. May act in a redox sensitive manner. Associates
CC with chromatin and binds DNA with a preference to non-canonical DNA
CC structures such as single-stranded DNA. Can bent DNA and enhance DNA
CC flexibility by looping thus providing a mechanism to promote activities
CC on various gene promoters (By similarity). Binds to the delta-1
CC crystallin/ASL1 enhancer (PubMed:7904558). Proposed to be involved in
CC the innate immune response to nucleic acids by acting as a cytoplasmic
CC promiscuous immunogenic DNA/RNA sensor (By similarity).
CC {ECO:0000250|UniProtKB:O54879, ECO:0000250|UniProtKB:P09429,
CC ECO:0000269|PubMed:7904558}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:7904558}. Chromosome
CC {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O54879}.
CC -!- DEVELOPMENTAL STAGE: Found in newly hatched chick liver and decreases
CC during postnatal development.
CC -!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-
CC 104 and a possible intramolecular disulfide bond involving Cys-23 and
CC Cys-45 give rise to different redox forms with specific functional
CC activities in various cellular compartments: 1- fully reduced HMGB3
CC (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and
CC 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63463; CAA45065.1; -; mRNA.
DR EMBL; AADN03004033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03004127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D14314; BAA03260.1; -; mRNA.
DR PIR; S22359; S22359.
DR RefSeq; NP_990626.2; NM_205295.1.
DR AlphaFoldDB; P40618; -.
DR SMR; P40618; -.
DR STRING; 9031.ENSGALP00000014747; -.
DR PaxDb; P40618; -.
DR Ensembl; ENSGALT00000014763; ENSGALP00000014747; ENSGALG00000009071.
DR GeneID; 396232; -.
DR KEGG; gga:396232; -.
DR CTD; 3149; -.
DR VEuPathDB; HostDB:geneid_396232; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000153299; -.
DR HOGENOM; CLU_082854_0_0_1; -.
DR InParanoid; P40618; -.
DR OMA; DMKNTEL; -.
DR OrthoDB; 1641977at2759; -.
DR TreeFam; TF105371; -.
DR PRO; PR:P40618; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000009071; Expressed in spermatid and 13 other tissues.
DR ExpressionAtlas; P40618; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008301; F:DNA binding, bending; IDA:AgBase.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:AgBase.
DR GO; GO:0032392; P:DNA geometric change; IDA:AgBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017967; HMG_boxA_CS.
DR InterPro; IPR031077; HMGB3.
DR PANTHER; PTHR48112:SF14; PTHR48112:SF14; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS00353; HMG_BOX_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 2: Evidence at transcript level;
KW Chromosome; Cytoplasm; Disulfide bond; DNA-binding; Immunity;
KW Innate immunity; Nucleus; Oxidation; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..202
FT /note="High mobility group protein B3"
FT /id="PRO_0000048541"
FT DNA_BIND 9..79
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 93..161
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 71..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 45
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 104
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT DISULFID 23..45
FT /note="In disulfide HMGB3"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT CONFLICT 30
FT /note="Missing (in Ref. 2; BAA03260)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="G -> A (in Ref. 1; CAA45065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 23057 MW; 24222C692BC5C903 CRC64;
MAKGDPKKPK GKMSAYAFFV QTCREEHKKK NPEVPVNFAE FSKKCSERWK TMSSKEKAKF
DEMAKADKVR YDREMKDYGP AKGGKKKKDP NAPKRPPSGF FLFCSEFRPK IKSTNPGISI
GDVAKKLGEM WNNLSDGEKQ PYNNKAAKLK EKYEKDVADY KSKGKFDGAK GAATKAARKK
VEEEDEEEEE DEEEEDEDDD DE
