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MSH5_CAEEL
ID   MSH5_CAEEL              Reviewed;        1369 AA.
AC   Q19272; A0A061AKP2; Q9NB29;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=MutS protein homolog 5;
GN   Name=msh-5 {ECO:0000312|WormBase:F09E8.3a};
GN   ORFNames=F09E8.3 {ECO:0000312|WormBase:F09E8.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RC   STRAIN=Bristol N2;
RX   PubMed=11014811; DOI=10.1093/genetics/156.2.617;
RA   Kelly K.O., Dernburg A.F., Stanfield G.M., Villeneuve A.M.;
RT   "Caenorhabditis elegans msh-5 is required for both normal and radiation-
RT   induced meiotic crossing over but not for completion of meiosis.";
RL   Genetics 156:617-630(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-933.
RX   PubMed=9787078; DOI=10.1006/geno.1998.5447;
RA   Winand N.J., Panzer J.A., Kolodner R.D.;
RT   "Cloning and characterization of the human and Caenorhabditis elegans
RT   homologs of the Saccharomyces cerevisiae MSH5 gene.";
RL   Genomics 53:69-80(1998).
RN   [4]
RP   FUNCTION.
RX   PubMed=23832114; DOI=10.1038/cdd.2013.68;
RA   Silva N., Adamo A., Santonicola P., Martinez-Perez E., La Volpe A.;
RT   "Pro-crossover factors regulate damage-dependent apoptosis in the
RT   Caenorhabditis elegans germ line.";
RL   Cell Death Differ. 20:1209-1218(2013).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=29521627; DOI=10.7554/elife.30789;
RA   Zhang L., Koehler S., Rillo-Bohn R., Dernburg A.F.;
RT   "A compartmentalized signaling network mediates crossover control in
RT   meiosis.";
RL   Elife 7:0-0(2018).
RN   [6]
RP   INTERACTION WITH BRC-1 AND BRD-1, AND SUBCELLULAR LOCATION.
RX   PubMed=30383754; DOI=10.1371/journal.pgen.1007653;
RA   Janisiw E., Dello Stritto M.R., Jantsch V., Silva N.;
RT   "BRCA1-BARD1 associate with the synaptonemal complex and pro-crossover
RT   factors and influence RAD-51 dynamics during Caenorhabditis elegans
RT   meiosis.";
RL   PLoS Genet. 14:e1007653-e1007653(2018).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30379819; DOI=10.1371/journal.pgen.1007776;
RA   Nguyen H., Labella S., Silva N., Jantsch V., Zetka M.;
RT   "C. elegans ZHP-4 is required at multiple distinct steps in the formation
RT   of crossovers and their transition to segregation competent chiasmata.";
RL   PLoS Genet. 14:E1007776-E1007776(2018).
CC   -!- FUNCTION: Crucial component in meiotic recombination, functioning at
CC       some point after the initiation step of recombination. Plays a role in
CC       promoting the crossover outcome of meiotic recombination events.
CC       Required for formation of normal meiotic crossover, and crossover and
CC       chiasmata generated by artificially made DNA breaks. Together with him-
CC       14 and zhp-3 plays a role in the activation of DNA damage-dependent
CC       apoptosis at the DNA damage checkpoint in pachytene cells
CC       (PubMed:23832114). {ECO:0000269|PubMed:11014811,
CC       ECO:0000269|PubMed:23832114}.
CC   -!- SUBUNIT: Heterooligomer of him-14 and msh-5 (By similarity). Interacts
CC       with the brc-1-brd-1 heterodimer (PubMed:30383754).
CC       {ECO:0000250|UniProtKB:Q12175, ECO:0000269|PubMed:30383754}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29521627,
CC       ECO:0000269|PubMed:30379819}. Note=From mid-pachytene, co-localizes
CC       with cosa-1 and rmh-1 at crossover sites of early recombination
CC       intermediates (PubMed:29521627, PubMed:30379819). Co-localizes with
CC       brc-1 at crossover sites in mid-late pachytene nuclei
CC       (PubMed:30383754). {ECO:0000269|PubMed:29521627,
CC       ECO:0000269|PubMed:30379819, ECO:0000269|PubMed:30383754}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:F09E8.3a};
CC         IsoId=Q19272-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:F09E8.3b};
CC         IsoId=Q19272-2; Sequence=VSP_060676;
CC   -!- TISSUE SPECIFICITY: Expressed in the germline.
CC       {ECO:0000269|PubMed:29521627}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
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DR   EMBL; AF271389; AAF76200.1; -; mRNA.
DR   EMBL; AF070070; AAC70065.1; -; mRNA.
DR   EMBL; BX284604; CAA98059.2; -; Genomic_DNA.
DR   EMBL; BX284604; CDR32661.1; -; Genomic_DNA.
DR   PIR; T20659; T20659.
DR   PIR; T20660; T20660.
DR   PIR; T43201; T43201.
DR   RefSeq; NP_001293899.1; NM_001306970.1.
DR   RefSeq; NP_502531.1; NM_070130.6. [Q19272-1]
DR   AlphaFoldDB; Q19272; -.
DR   SMR; Q19272; -.
DR   BioGRID; 43359; 4.
DR   STRING; 6239.F09E8.3; -.
DR   PaxDb; Q19272; -.
DR   EnsemblMetazoa; F09E8.3a.1; F09E8.3a.1; WBGene00003421. [Q19272-1]
DR   EnsemblMetazoa; F09E8.3b.1; F09E8.3b.1; WBGene00003421. [Q19272-2]
DR   GeneID; 178268; -.
DR   KEGG; cel:CELE_F09E8.3; -.
DR   UCSC; F09E8.3; c. elegans. [Q19272-1]
DR   CTD; 178268; -.
DR   WormBase; F09E8.3a; CE26678; WBGene00003421; msh-5. [Q19272-1]
DR   WormBase; F09E8.3b; CE49987; WBGene00003421; msh-5. [Q19272-2]
DR   eggNOG; KOG0221; Eukaryota.
DR   GeneTree; ENSGT00550000074977; -.
DR   HOGENOM; CLU_004671_0_0_1; -.
DR   InParanoid; Q19272; -.
DR   OMA; ACRIYKA; -.
DR   OrthoDB; 138168at2759; -.
DR   PhylomeDB; Q19272; -.
DR   PRO; PR:Q19272; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00003421; Expressed in germ line (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q19272; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0051026; P:chiasma assembly; IMP:WormBase.
DR   GO; GO:0045143; P:homologous chromosome segregation; IMP:WormBase.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chromosome; DNA-binding; Meiosis;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1369
FT                   /note="MutS protein homolog 5"
FT                   /id="PRO_0000115205"
FT   REGION          138..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..915
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1042
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1050..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..446
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060676"
SQ   SEQUENCE   1369 AA;  153140 MW;  DDC5FDAB7DB86C4A CRC64;
     MSTRWRYYNS KRGNGFRGRG RGRGRGTSLT AVALPRDDNF HKGAQDGAYF KDMPMDPEQF
     RDETVLSLSF AQGMLGAAYY EQSSQLLKIM NDISEDLEFR FLKRLIDDVK PTLIIANRSQ
     DLEFIKFLTT RYDPQEKIYE DGTTEEGTSE DTVPTWDSSL AYSTDETTAE KEEKEEDEDD
     DDEGLPAKLN KLPNNFFRMS RAIERLKAMA GSHDSSMTEE DKYIIIKMRF DIEAVNMIRS
     FGALLLFLDE TRMGVTDDPL SVTSPIKSIK TFTLGNLVEI DFNTIQALDI LPKETENKKT
     FGQGRSLYQL MDKCRSTVGK KCLRKWFRNP TTDRDDLVSR QKCVHYFKQD WNAEVTAKLS
     SILGRVKALN SVFQKFQSGT AQLIHWECFV STVNALVEIL NIIRQTPISK EFPVESDLLR
     EVSEIAVIAG SIINFAESKI QGRVTVMNGI DEELDEIRDT YENMPMVLTA IAKQEEARLG
     LPPYSNVACV YIPLVGFVLS VPRDYGVESQ PDMTLLYSTH EDLRVRNATT SRLDDEFGDI
     LMRLIDSQTA IILTLKTRVM KKKRSIIKLL SIASRIDVLI SFGLIAAQNG WNCPALVDEP
     VIEAVELYHP ISVLVVKKSF VPNQVSSGRD GIKASIITGP NACGKSVYMK SIGIMVFLSH
     IGSFVPARHA KIGIVDRIVT RMFTVDSVLD GMSTFAKDVE QVALALRKAT GNSLVIIDEF
     GKGTMTEVGL SLLASVMTYW MNRGADRCPH IFLSSHFHAL PNYIPLETNI ATFLTFTVLR
     EAGGKIKYLF RMTPGLVDCS FALSVAKEEG IPPPVIGRAC RIYKALKAGT LLKEIKAEVS
     NDNEKQLVED MDVVLADEDG FMAAVESFVK RKKTSFCESS MRNVSEEIEK ERSEASTPAS
     KSRSTITARS NSVLSSRSMA SVDQLSVLDA LLPKKKKKKV TGSSMESSMS PDPFQEEDEG
     TEGEEDQISA PVSRPTLPSV QKYASEEEKQ QSINSRHSFS TRTAIHIPTP IQMGEAGGVK
     RPRSTSTSSP GPSASKSVRT EVFKKTPNVK ESQVLETPKQ LSISSFLEPK FPSSEKDVIS
     RVSERYLQSD PFKTPISDRR SQQSSRHSTP KNRSMNQSLI QSARDTPHET IRSSNEVNPE
     FFNIFNFPDD SILKSQDTYD PNVTPRSSSR RELRPDVSHS QNSQFGEVFS ELGTQFSIFN
     SQQSFPGNSM GTTNPDCSIF DDFFANSQDG EKKIDSTKTS MPIVNSDNFI FKTPEPRSSE
     KQRSLLKNKG QASNSSISPS SLILGQLAFG DVDQTPRPRG DNPIEFQYDV VDDDDPIFEE
     KNCSAPVFEF LKSNDDEEDD EFLKSFLETE GSLHIDTSAD ETIDRSKRS
 
 
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