SMC5_MOUSE
ID SMC5_MOUSE Reviewed; 1101 AA.
AC Q8CG46; Q80TW7; Q8CHX5; Q922K3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE Short=SMC protein 5;
DE Short=SMC-5;
DE Short=mSMC5;
DE AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 453;
DE Short=MLZ-453;
GN Name=Smc5; Synonyms=Kiaa0594, Smc5l1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-1101 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11408570; DOI=10.1091/mbc.12.6.1583;
RA Taylor E.M., Moghraby J.S., Lees J.H., Smit B., Moens P.B., Lehmann A.R.;
RT "Characterization of a novel human SMC heterodimer homologous to the
RT Schizosaccharomyces pombe Rad18/Spr18 complex.";
RL Mol. Biol. Cell 12:1583-1594(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT "Screening of genes involved in chromosome segregation during meiosis I:
RT toward the identification of genes responsible for infertility in humans.";
RL J. Hum. Genet. 55:293-299(2010).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC in repair of DNA double-strand breaks by homologous recombination. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC complex is required for telomere maintenance via recombination and
CC mediates sumoylation of shelterin complex (telosome) components.
CC Required for sister chromatid cohesion during prometaphase and mitotic
CC progression; the function seems to be independent of SMC6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC6. Component of the SMC5-SMC6
CC complex which consists at least of SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A
CC or EID3 and NSMCE3. Interacts with NSMCE2. Interacts with SLF2; this
CC interaction induces an association of the SLF1-SLF2 complex with the
CC SMC5-SMC6 complex. Interacts with RAD18; this interaction is increased
CC in a SLF1 or SLF2-dependent manner. {ECO:0000250|UniProtKB:Q8IY18}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570,
CC ECO:0000269|PubMed:20339383}. Chromosome {ECO:0000269|PubMed:11408570}.
CC Nucleus, PML body {ECO:0000250|UniProtKB:Q8IY18}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q8IY18}. Note=Colocalizes with SMC6 on the X-Y
CC chromosome pair within the sex vesicle during late pachytene/diplotene
CC (PubMed:11408570). Associates with chromatin. Localizes to PML nuclear
CC bodies in ALT cell lines. Accumulates with RAD18 and the SLF1-SLF2
CC complex at replication-coupled DNA interstrand repair and DNA double-
CC strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent
CC manner. {ECO:0000250|UniProtKB:Q8IY18, ECO:0000269|PubMed:11408570}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CG46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CG46-2; Sequence=VSP_022251, VSP_022252;
CC -!- TISSUE SPECIFICITY: Expressed in testis but not ovary.
CC {ECO:0000269|PubMed:20339383}.
CC -!- DEVELOPMENTAL STAGE: Expressed in ovary and testis at 15.5 dpc.
CC {ECO:0000269|PubMed:20339383}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ534941; CAD59184.1; -; mRNA.
DR EMBL; BC007174; AAH07174.1; ALT_INIT; mRNA.
DR EMBL; BC038345; AAH38345.1; -; mRNA.
DR EMBL; AK122321; BAC65603.3; -; Transcribed_RNA.
DR CCDS; CCDS37936.1; -. [Q8CG46-2]
DR CCDS; CCDS89364.1; -. [Q8CG46-1]
DR RefSeq; NP_001239613.1; NM_001252684.1. [Q8CG46-1]
DR RefSeq; NP_722503.1; NM_153808.2. [Q8CG46-2]
DR AlphaFoldDB; Q8CG46; -.
DR SMR; Q8CG46; -.
DR BioGRID; 230460; 7.
DR IntAct; Q8CG46; 2.
DR MINT; Q8CG46; -.
DR STRING; 10090.ENSMUSP00000084837; -.
DR iPTMnet; Q8CG46; -.
DR PhosphoSitePlus; Q8CG46; -.
DR EPD; Q8CG46; -.
DR jPOST; Q8CG46; -.
DR MaxQB; Q8CG46; -.
DR PaxDb; Q8CG46; -.
DR PeptideAtlas; Q8CG46; -.
DR PRIDE; Q8CG46; -.
DR ProteomicsDB; 261257; -. [Q8CG46-1]
DR ProteomicsDB; 261258; -. [Q8CG46-2]
DR Antibodypedia; 26866; 200 antibodies from 27 providers.
DR Ensembl; ENSMUST00000087556; ENSMUSP00000084837; ENSMUSG00000024943. [Q8CG46-1]
DR Ensembl; ENSMUST00000223934; ENSMUSP00000153364; ENSMUSG00000024943. [Q8CG46-2]
DR GeneID; 226026; -.
DR KEGG; mmu:226026; -.
DR UCSC; uc008haa.2; mouse. [Q8CG46-2]
DR UCSC; uc008hab.2; mouse. [Q8CG46-1]
DR CTD; 23137; -.
DR MGI; MGI:2385088; Smc5.
DR VEuPathDB; HostDB:ENSMUSG00000024943; -.
DR eggNOG; KOG0979; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_004969_1_0_1; -.
DR InParanoid; Q8CG46; -.
DR OMA; SAEFFPG; -.
DR OrthoDB; 100993at2759; -.
DR PhylomeDB; Q8CG46; -.
DR TreeFam; TF105708; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 226026; 23 hits in 109 CRISPR screens.
DR ChiTaRS; Smc5; mouse.
DR PRO; PR:Q8CG46; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8CG46; protein.
DR Bgee; ENSMUSG00000024943; Expressed in spermatid and 252 other tissues.
DR ExpressionAtlas; Q8CG46; baseline and differential.
DR Genevisible; Q8CG46; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0035061; C:interchromatin granule; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IMP:BHF-UCL.
DR GO; GO:0000803; C:sex chromosome; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IMP:MGI.
DR GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:MGI.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IMP:MGI.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; ISS:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; DNA damage; DNA recombination; DNA repair; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Ubl conjugation.
FT CHAIN 1..1101
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000270952"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..644
FT /note="Flexible hinge"
FT COILED 207..440
FT /evidence="ECO:0000255"
FT COILED 645..753
FT /evidence="ECO:0000255"
FT COILED 780..828
FT /evidence="ECO:0000255"
FT COILED 888..927
FT /evidence="ECO:0000255"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY18"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY18"
FT VAR_SEQ 842..856
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022251"
FT VAR_SEQ 888
FT /note="S -> SV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022252"
FT CONFLICT 545
FT /note="Y -> C (in Ref. 3; AAH07174)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="A -> T (in Ref. 3; AAH07174)"
FT /evidence="ECO:0000305"
FT CONFLICT 842..847
FT /note="QVPTIP -> VSIKIS (in Ref. 3; BAC65603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1101 AA; 128813 MW; 71F7D790EE28C427 CRC64;
MATPSGKAAP PNPQVSKRSL PRDASSEVPS KRKNSNPLPT LPRPSGTFVE GSIVRIAMEN
FLTYDICEVS PGPHLNMIIG ANGTGKSSIV CAICLGLAGK PAFMGRADKV GFFVKRGCSK
GLVEIELFRT SGNLIITREI DVIKNQSFWF INKKPVTQKI VEEQVAALNI QVGNLCQFLP
QDKVGEFAKL SKIELLEATE KSVGPPEMHR YHCELKNFRE KEKQLETSCK EKTEYLEKMV
QRNERYKQDV ERFYERKRHL DLIEMLEAKR PWVEYENVRQ EYEGVKLIRD RVKEEVRKLK
EGQIPMTRRI EEIDRQRHTL EVRIKEKSTD IKEASQKCKQ RQDLIERKDR QIKELQQALT
VKQNEELDRQ KRISNTRKMI EDLQSELKTA ENCENLQPQI DTVTNDLRRV QEEKALCEGE
IIDKQREKEM LEKQRRSVSD HITRFDNLMN QKEDKLRQRY RDTYDAVLWL RNNRDRFKQR
VCEPIMLTIN MKDNKNAKYV ENHISSNDLR AFVFESQEDM EIFLREVRDN KKLRVNAVIA
PKISYADKAP SRSLNDLKQY GFFSYLRELF DAPDPVMSYL CCQYHIHEVP VGTERTRERI
ERVIQETRLK QIYTAEEKYV LKTSVYSNKV ISSNTSLKVA QFLTVTVDLE QRRHLEEQLK
EMNRQLEAVD SGLAALRDTN RHLELKDNEL RLKKKELLER KTRKRQLEQK ISSKLASIRL
MEQDTCNLEE EERKASTKIK EINVQKAKLV TELTGLVKIC TSFQIQKVDL ILQNTTVISE
KNKLEADYMA SSSQLRVTEQ QFIELDDNRQ RLLQKCKELM KKARQVCNLS ADQAVPQEFQ
TQVPTIPNGH SSSPPMAFQD LPNTLDEIDA LLTEERSRAS CFTGLNPSVV EEYSKREVEI
QQLTEELQGK KVELDEYREN ISQVKERWLN PLKELVEKIN EKFSNFFSSM QCAGEVDLHT
ENEEDYDKYG IRIRVKFRSS TQLHELTPHH QSGGERSVST MLYLMALQEL NRCPFRVVDE
INQGMDPINE RRVFEMVVNT ACKENTSQYF FITPKLLQNL PYSEKMTVLF VYNGPHMLEP
NRWNLKAFQR RRRRITFTQP Q
