SPB10_CHICK
ID SPB10_CHICK Reviewed; 410 AA.
AC O73790;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Heterochromatin-associated protein MENT;
DE AltName: Full=Myeloid and erythroid nuclear termination stage-specific protein;
DE AltName: Full=Serpin B10;
GN Name=SERPINB10; Synonyms=MENT;
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], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RC STRAIN=White leghorn; TISSUE=Blood;
RX PubMed=10026180; DOI=10.1074/jbc.274.9.5626;
RA Grigoryev S.A., Bednar J., Woodcock C.L.;
RT "MENT, a heterochromatin protein that mediates higher order chromatin
RT folding, is a new serpin family member.";
RL J. Biol. Chem. 274:5626-5636(1999).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9446625; DOI=10.1074/jbc.273.5.3082;
RA Grigoryev S.A., Woodcock C.L.;
RT "Chromatin structure in granulocytes. A link between tight compaction and
RT accumulation of a heterochromatin-associated protein (MENT).";
RL J. Biol. Chem. 273:3082-3089(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 73-ARG--PRO-79 AND THR-358,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11821386; DOI=10.1074/jbc.m108460200;
RA Irving J.A., Shushanov S.S., Pike R.N., Popova E.Y., Broemme D.,
RA Coetzer T.H.T., Bottomley S.P., Boulynko I.A., Grigoryev S.A.,
RA Whisstock J.C.;
RT "Inhibitory activity of a heterochromatin-associated serpin (MENT) against
RT papain-like cysteine proteinases affects chromatin structure and blocks
RT cell proliferation.";
RL J. Biol. Chem. 277:13192-13201(2002).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=12930828; DOI=10.1074/jbc.m307635200;
RA Springhetti E.M., Istomina N.E., Whisstock J.C., Nikitina T.,
RA Woodcock C.L., Grigoryev S.A.;
RT "Role of the M-loop and reactive center loop domains in the folding and
RT bridging of nucleosome arrays by MENT.";
RL J. Biol. Chem. 278:43384-43393(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, SUBUNIT, AND MUTAGENESIS
RP OF ARG-78; LYS-99; LYS-107; ARG-109; LYS-138; ARG-214; ARG-332 AND LYS-338.
RX PubMed=16810322; DOI=10.1038/sj.emboj.7601201;
RA McGowan S., Buckle A.M., Irving J.A., Ong P.C., Bashtannyk-Puhalovich T.A.,
RA Kan W.-T., Henderson K.N., Bulynko Y.A., Popova E.Y., Smith A.I.,
RA Bottomley S.P., Rossjohn J., Grigoryev S.A., Pike R.N., Whisstock J.C.;
RT "X-ray crystal structure of MENT: evidence for functional loop-sheet
RT polymers in chromatin condensation.";
RL EMBO J. 25:3144-3155(2006).
CC -!- FUNCTION: DNA-binding protein that promotes DNA condensation into
CC transcriptionally inactive heterochromatin in terminally differentiated
CC avian blood cells. Promotes tight packing of nucleosomes into spherical
CC clusters by binding to linker DNA and subsequent oligomerization. Acts
CC as a cysteine protease inhibitor towards CTSL (cathepsin L1) and CTSV
CC (cathepsin L2), but does not inhibit serine proteases.
CC {ECO:0000269|PubMed:10026180, ECO:0000269|PubMed:11821386,
CC ECO:0000269|PubMed:12930828, ECO:0000269|PubMed:16810322,
CC ECO:0000269|PubMed:9446625}.
CC -!- SUBUNIT: Homodimer and homooligomer. Interaction with DNA promotes
CC oligomerization. {ECO:0000269|PubMed:12930828,
CC ECO:0000269|PubMed:16810322}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with
CC chromatin.
CC -!- TISSUE SPECIFICITY: Detected in all major blood cell types. Highly
CC expressed in granulocytes (at protein level).
CC {ECO:0000269|PubMed:9446625}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF053401; AAC15710.1; -; mRNA.
DR RefSeq; NP_990228.1; NM_204897.1.
DR RefSeq; XP_015137649.1; XM_015282163.1.
DR RefSeq; XP_015137651.1; XM_015282165.1.
DR PDB; 2DUT; X-ray; 3.00 A; A/B/C/D=1-410.
DR PDB; 2H4P; X-ray; 1.70 A; A=1-369, B=377-410.
DR PDB; 2H4Q; X-ray; 2.10 A; A=1-369, B=377-410.
DR PDB; 2H4R; X-ray; 2.70 A; A=1-410.
DR PDBsum; 2DUT; -.
DR PDBsum; 2H4P; -.
DR PDBsum; 2H4Q; -.
DR PDBsum; 2H4R; -.
DR AlphaFoldDB; O73790; -.
DR SMR; O73790; -.
DR STRING; 9031.ENSGALP00000020960; -.
DR MEROPS; I04.033; -.
DR PaxDb; O73790; -.
DR Ensembl; ENSGALT00000020990; ENSGALP00000020960; ENSGALG00000019553.
DR Ensembl; ENSGALT00000107055; ENSGALP00000069238; ENSGALG00000019553.
DR GeneID; 395715; -.
DR KEGG; gga:395715; -.
DR CTD; 395715; -.
DR VEuPathDB; HostDB:geneid_395715; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000165915; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; O73790; -.
DR OMA; MGMHSAF; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; O73790; -.
DR TreeFam; TF352619; -.
DR EvolutionaryTrace; O73790; -.
DR PRO; PR:O73790; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000019553; Expressed in granulocyte and 8 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:AgBase.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:AgBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IDA:AgBase.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043362; P:nucleate erythrocyte maturation; IDA:AgBase.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Direct protein sequencing;
KW DNA condensation; DNA-binding; Nucleus; Protease inhibitor;
KW Reference proteome.
FT CHAIN 1..410
FT /note="Heterochromatin-associated protein MENT"
FT /id="PRO_0000355551"
FT REGION 61..69
FT /note="M-loop required for interaction with nucleosome
FT linker DNA"
FT REGION 68..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..372
FT /note="Required for oligomerization and DNA condensation"
FT MOTIF 80..84
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MUTAGEN 73..79
FT /note="RPSRGRP->KGAKAKG: Reduced nuclear localization."
FT /evidence="ECO:0000269|PubMed:11821386"
FT MUTAGEN 78
FT /note="R->Q: Reduced interaction with DNA."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 99
FT /note="K->Q: Reduced interaction with DNA; when associated
FT with Q-107 and Q-109."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 107
FT /note="K->Q: Reduced interaction with DNA; when associated
FT with Q-99 and Q-109."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 109
FT /note="R->Q: Reduced interaction with DNA; when associated
FT with Q-99 and Q-107."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 138
FT /note="K->Q: Reduced interaction with DNA."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 214
FT /note="R->A: Reduced interaction with DNA."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 332
FT /note="R->A: Reduced interaction with DNA."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 338
FT /note="K->A: Reduced interaction with DNA."
FT /evidence="ECO:0000269|PubMed:16810322"
FT MUTAGEN 358
FT /note="T->R: Strongly reduced inhibition of cysteine
FT proteases."
FT /evidence="ECO:0000269|PubMed:11821386"
FT HELIX 1..22
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2H4R"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 110..123
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2H4P"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2H4P"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2H4Q"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 187..201
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 219..237
FT /evidence="ECO:0007829|PDB:2H4P"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:2H4P"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2H4P"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:2H4Q"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 341..353
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 355..369
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:2H4P"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:2H4P"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:2H4P"
SQ SEQUENCE 410 AA; 47384 MW; 24FC06D9C4F4F0BA CRC64;
MEQVSASIGN FTVDLFNKLN ETNRDKNIFF SPWSISSALA LTYLAAKGST AREMAEVLHF
TEAVRAESSS VARPSRGRPK RRRMDPEHEQ AENIHSGFKE LLTAFNKPRN NYSLRSANRI
YVEKTYALLP TYLQLSKKYY KAEPQKVNFK TAPEQSRKEI NTWVEKQTES KIKNLLSSDD
VKATTRLILV NAIYFKAEWE VKFQAEKTSI QPFRLSKNKS KPVKMMYMRD TFPVLIMEKM
NFKMIELPYV KRELSMFILL PDDIKDGTTG LEQLERELTY ERLSEWADSK MMTETLVDLH
LPKFSLEDRI DLRDTLRNMG MTTAFTTNAD FRGMTDKKDL AISKVIHQSF VAVDEKGTEA
AAATAVIISF TTSVINHVLK FKVDHPFHFF IRHNKSKTIL FFGRFCCPVE
