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Heterochromatin-associated protein MENT (Myeloid and erythroid nuclear termination stage-specific protein) (Serpin B10)

 SPB10_CHICK             Reviewed;         410 AA.
O73790;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
07-NOV-2018, entry version 112.
RecName: Full=Heterochromatin-associated protein MENT;
AltName: Full=Myeloid and erythroid nuclear termination stage-specific protein;
AltName: Full=Serpin B10;
Name=SERPINB10; Synonyms=MENT;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
LOCATION, AND FUNCTION.
STRAIN=White leghorn; TISSUE=Blood;
PubMed=10026180; DOI=10.1074/jbc.274.9.5626;
Grigoryev S.A., Bednar J., Woodcock C.L.;
"MENT, a heterochromatin protein that mediates higher order chromatin
folding, is a new serpin family member.";
J. Biol. Chem. 274:5626-5636(1999).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9446625; DOI=10.1074/jbc.273.5.3082;
Grigoryev S.A., Woodcock C.L.;
"Chromatin structure in granulocytes. A link between tight compaction
and accumulation of a heterochromatin-associated protein (MENT).";
J. Biol. Chem. 273:3082-3089(1998).
[3]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 73-ARG--PRO-79 AND
THR-358, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11821386; DOI=10.1074/jbc.M108460200;
Irving J.A., Shushanov S.S., Pike R.N., Popova E.Y., Broemme D.,
Coetzer T.H.T., Bottomley S.P., Boulynko I.A., Grigoryev S.A.,
Whisstock J.C.;
"Inhibitory activity of a heterochromatin-associated serpin (MENT)
against papain-like cysteine proteinases affects chromatin structure
and blocks cell proliferation.";
J. Biol. Chem. 277:13192-13201(2002).
[4]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
PubMed=12930828; DOI=10.1074/jbc.M307635200;
Springhetti E.M., Istomina N.E., Whisstock J.C., Nikitina T.,
Woodcock C.L., Grigoryev S.A.;
"Role of the M-loop and reactive center loop domains in the folding
and bridging of nucleosome arrays by MENT.";
J. Biol. Chem. 278:43384-43393(2003).
[5]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, SUBUNIT, AND
MUTAGENESIS OF ARG-78; LYS-99; LYS-107; ARG-109; LYS-138; ARG-214;
ARG-332 AND LYS-338.
PubMed=16810322; DOI=10.1038/sj.emboj.7601201;
McGowan S., Buckle A.M., Irving J.A., Ong P.C.,
Bashtannyk-Puhalovich T.A., Kan W.-T., Henderson K.N., Bulynko Y.A.,
Popova E.Y., Smith A.I., Bottomley S.P., Rossjohn J., Grigoryev S.A.,
Pike R.N., Whisstock J.C.;
"X-ray crystal structure of MENT: evidence for functional loop-sheet
polymers in chromatin condensation.";
EMBO J. 25:3144-3155(2006).
-!- FUNCTION: DNA-binding protein that promotes DNA condensation into
transcriptionally inactive heterochromatin in terminally
differentiated avian blood cells. Promotes tight packing of
nucleosomes into spherical clusters by binding to linker DNA and
subsequent oligomerization. Acts as a cysteine protease inhibitor
towards CTSL (cathepsin L1) and CTSV (cathepsin L2), but does not
inhibit serine proteases. {ECO:0000269|PubMed:10026180,
ECO:0000269|PubMed:11821386, ECO:0000269|PubMed:12930828,
ECO:0000269|PubMed:16810322, ECO:0000269|PubMed:9446625}.
-!- SUBUNIT: Homodimer and homooligomer. Interaction with DNA promotes
oligomerization. {ECO:0000269|PubMed:12930828,
ECO:0000269|PubMed:16810322}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with
chromatin.
-!- TISSUE SPECIFICITY: Detected in all major blood cell types. Highly
expressed in granulocytes (at protein level).
{ECO:0000269|PubMed:9446625}.
-!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
{ECO:0000305}.
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EMBL; AF053401; AAC15710.1; -; mRNA.
RefSeq; NP_990228.1; NM_204897.1.
RefSeq; XP_015137649.1; XM_015282163.1.
RefSeq; XP_015137651.1; XM_015282165.1.
UniGene; Gga.415; -.
PDB; 2DUT; X-ray; 3.00 A; A/B/C/D=1-410.
PDB; 2H4P; X-ray; 1.70 A; A=1-369, B=377-410.
PDB; 2H4Q; X-ray; 2.10 A; A=1-369, B=377-410.
PDB; 2H4R; X-ray; 2.70 A; A=1-410.
PDBsum; 2DUT; -.
PDBsum; 2H4P; -.
PDBsum; 2H4Q; -.
PDBsum; 2H4R; -.
ProteinModelPortal; O73790; -.
SMR; O73790; -.
STRING; 9031.ENSGALP00000020960; -.
MEROPS; I04.033; -.
PaxDb; O73790; -.
PRIDE; O73790; -.
Ensembl; ENSGALT00000020990; ENSGALP00000020960; ENSGALG00000019553.
GeneID; 395715; -.
KEGG; gga:395715; -.
CTD; 395715; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118789; -.
HOGENOM; HOG000238519; -.
HOVERGEN; HBG005957; -.
InParanoid; O73790; -.
KO; K13963; -.
OMA; ITHLIRF; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; O73790; -.
TreeFam; TF352619; -.
Reactome; R-GGA-6798695; Neutrophil degranulation.
EvolutionaryTrace; O73790; -.
PRO; PR:O73790; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000019553; Expressed in 7 organ(s), highest expression level in spleen.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0005654; C:nucleoplasm; IDA:AgBase.
GO; GO:0031490; F:chromatin DNA binding; IDA:AgBase.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0030261; P:chromosome condensation; IDA:AgBase.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
GO; GO:0043362; P:nucleate erythrocyte maturation; IDA:AgBase.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosome; Complete proteome;
Direct protein sequencing; DNA condensation; DNA-binding; Nucleus;
Protease inhibitor; Reference proteome.
CHAIN 1 410 Heterochromatin-associated protein MENT.
/FTId=PRO_0000355551.
REGION 61 69 M-loop required for interaction with
nucleosome linker DNA.
REGION 356 372 Required for oligomerization and DNA
condensation.
MOTIF 80 84 Nuclear localization signal.
{ECO:0000250}.
MUTAGEN 73 79 RPSRGRP->KGAKAKG: Reduced nuclear
localization.
{ECO:0000269|PubMed:11821386}.
MUTAGEN 78 78 R->Q: Reduced interaction with DNA.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 99 99 K->Q: Reduced interaction with DNA; when
associated with Q-107 and Q-109.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 107 107 K->Q: Reduced interaction with DNA; when
associated with Q-99 and Q-109.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 109 109 R->Q: Reduced interaction with DNA; when
associated with Q-99 and Q-107.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 138 138 K->Q: Reduced interaction with DNA.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 214 214 R->A: Reduced interaction with DNA.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 332 332 R->A: Reduced interaction with DNA.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 338 338 K->A: Reduced interaction with DNA.
{ECO:0000269|PubMed:16810322}.
MUTAGEN 358 358 T->R: Strongly reduced inhibition of
cysteine proteases.
{ECO:0000269|PubMed:11821386}.
HELIX 1 22 {ECO:0000244|PDB:2H4P}.
STRAND 24 26 {ECO:0000244|PDB:2H4R}.
STRAND 28 30 {ECO:0000244|PDB:2H4P}.
HELIX 32 43 {ECO:0000244|PDB:2H4P}.
HELIX 48 57 {ECO:0000244|PDB:2H4P}.
HELIX 92 105 {ECO:0000244|PDB:2H4P}.
STRAND 110 123 {ECO:0000244|PDB:2H4P}.
HELIX 130 140 {ECO:0000244|PDB:2H4P}.
STRAND 143 147 {ECO:0000244|PDB:2H4P}.
TURN 149 151 {ECO:0000244|PDB:2H4P}.
HELIX 153 167 {ECO:0000244|PDB:2H4P}.
TURN 168 170 {ECO:0000244|PDB:2H4P}.
STRAND 171 173 {ECO:0000244|PDB:2H4Q}.
TURN 178 180 {ECO:0000244|PDB:2H4P}.
STRAND 187 201 {ECO:0000244|PDB:2H4P}.
HELIX 205 207 {ECO:0000244|PDB:2H4P}.
STRAND 209 216 {ECO:0000244|PDB:2H4P}.
STRAND 219 237 {ECO:0000244|PDB:2H4P}.
TURN 238 241 {ECO:0000244|PDB:2H4P}.
STRAND 242 249 {ECO:0000244|PDB:2H4P}.
HELIX 250 252 {ECO:0000244|PDB:2H4P}.
STRAND 253 263 {ECO:0000244|PDB:2H4P}.
STRAND 266 270 {ECO:0000244|PDB:2H4P}.
HELIX 272 276 {ECO:0000244|PDB:2H4P}.
HELIX 280 287 {ECO:0000244|PDB:2H4P}.
STRAND 293 302 {ECO:0000244|PDB:2H4P}.
STRAND 304 311 {ECO:0000244|PDB:2H4P}.
HELIX 313 319 {ECO:0000244|PDB:2H4P}.
HELIX 323 325 {ECO:0000244|PDB:2H4P}.
TURN 332 334 {ECO:0000244|PDB:2H4Q}.
STRAND 336 338 {ECO:0000244|PDB:2H4P}.
STRAND 341 353 {ECO:0000244|PDB:2H4P}.
STRAND 355 369 {ECO:0000244|PDB:2H4P}.
STRAND 379 382 {ECO:0000244|PDB:2H4P}.
STRAND 387 393 {ECO:0000244|PDB:2H4P}.
TURN 394 397 {ECO:0000244|PDB:2H4P}.
STRAND 398 405 {ECO:0000244|PDB:2H4P}.
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


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