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Database: UniProt
Entry: E9Q2X6_MOUSE
LinkDB: E9Q2X6_MOUSE
Original site: E9Q2X6_MOUSE 
ID   E9Q2X6_MOUSE            Unreviewed;      1261 AA.
AC   E9Q2X6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=Smc4 {ECO:0000313|Ensembl:ENSMUSP00000103433.2,
GN   ECO:0000313|MGI:MGI:1917349};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000103433.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000103433.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103433.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000103433.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103433.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   AlphaFoldDB; E9Q2X6; -.
DR   SMR; E9Q2X6; -.
DR   jPOST; E9Q2X6; -.
DR   MaxQB; E9Q2X6; -.
DR   PeptideAtlas; E9Q2X6; -.
DR   ProteomicsDB; 324371; -.
DR   Antibodypedia; 18504; 281 antibodies from 35 providers.
DR   Ensembl; ENSMUST00000107803.7; ENSMUSP00000103433.2; ENSMUSG00000034349.15.
DR   AGR; MGI:1917349; -.
DR   MGI; MGI:1917349; Smc4.
DR   VEuPathDB; HostDB:ENSMUSG00000034349; -.
DR   GeneTree; ENSGT00900000141094; -.
DR   HOGENOM; CLU_001042_4_1_1; -.
DR   ChiTaRS; Smc4; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000034349; Expressed in late embryo and 283 other cell types or tissues.
DR   ExpressionAtlas; E9Q2X6; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProt.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   1: Evidence at protein level;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Proteomics identification {ECO:0007829|EPD:E9Q2X6,
KW   ECO:0007829|MaxQB:E9Q2X6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          586..701
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          370..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          514..548
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          749..776
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          865..983
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1261 AA;  144207 MW;  4FCA6E17A573852B CRC64;
     MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPATMASEA GAPRLMITHI
     VNQNFKSYAG EKVLGPFHKR FSCIIGPNGS GKSNVIDSML FVFGYRAQKI RSKKLSVLIH
     NSDEHKDIQS CTVEVHFQKI IDKEGDDYEV LPNSNFYVSR TAYRDSTSVY HISGKKKTFK
     DVGNLLRSHG IDLDHNRFLI LQGEVEQIAM MKPKGQTEHD EGMLEYLEDI IGCGRLNEPI
     KVLCRRVEIL NEHRGEKLNR VKMVEKEKDA LEGEKNIAIE FLTLENEMFK KKNHICQYYI
     YDLQNRIAEI TTQKEKIHED TKEITEKSNV LSNEMKAKNS AVKDVEKKLN KVTKFIEQNK
     EKFTQLDLED VQVREKLKHA TSKAKKLEKQ LQKDKEKVEE LKSVPAKSKT VINETTTRNN
     SLEKEREKEE KKLKEVMDSL KQETQGLQKE KEIQEKELMG FNKSVNEARS KMEVAQSELD
     IYLSRHNTAV SQLSKAKEAL ITASETLKER KAAIKDINTK LPQTQQELKE KEKELQKLTQ
     EEINLKSLVH DLFQKVEEAK SSLAMNRSRG KVLDAIIQEK KSGRIPGIYG RLGDLGAIDE
     KYDIAISSCC HALDYIVVDS IDTAQECVNF LKKHNIGIAT FIGLDKMTVW AKKMSKIQTP
     ENTPRLFDLV KVKNEEIRQA FYFALRDTLV ANNLDQATRV AYQRDRRWRV VTLQGQIIEQ
     SGTMSGGGSK VMRGRMGSSV IDEISVEEVN KMESQLERHS KQAMQIQEQK VQHEEAVVKL
     RHSERDMRNT LEKFAASIQG LSEQEEYLCV QIKELEANVL TTAPDRKQQK LLEENVSVFK
     KEYDAVAEKA GKVEAEIKRL HNTIIDINNR KLKAQQNKLD TINKQLDECA SAITKAQVAI
     KTADRNLKKA QDSVCRTEKE IKDTEKEIND LKTELKNIED KAEEVINNTK TAETSLPEIQ
     KEHRNLLQEL KVIQENEHAL QKDALSIKLK LEQIDGHISE HNSKIKYWQK EISKIKLHPV
     EDNPVETVAV LSQEELEAIK NPESITNEIA LLEAQCREMK PNLGAIAEYK KKEDLYLQRV
     AELDKITSER DNFRQAYEDL RKQRLNEFMA GFYVITNKLK ENYQMLTLGG DAELELVDSL
     DPFSEGIMFS VRPPKKSWKK IFNLSGGEKT LSSLALVFAL HHYKPTPLYF MDEIDAALDF
     KNVSIVAFYI YEQTKNAQFI IISLRNNMFE ISDRLIGIYK TYNSTKSVAV NPKQIASKGL
     C
//
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