ID G1T0Q6_RABIT Unreviewed; 1244 AA.
AC G1T0Q6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC3 {ECO:0000313|Ensembl:ENSOCUP00000009593.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000009593.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000009593.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000009593.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000009593.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000009593.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement. {ECO:0000256|ARBA:ARBA00034085}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Nucleus
CC {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; AAGW02051286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T0Q6; -.
DR SMR; G1T0Q6; -.
DR STRING; 9986.ENSOCUP00000009593; -.
DR PaxDb; 9986-ENSOCUP00000009593; -.
DR Ensembl; ENSOCUT00000011146.4; ENSOCUP00000009593.3; ENSOCUG00000011142.4.
DR eggNOG; KOG0964; Eukaryota.
DR GeneTree; ENSGT00580000081628; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; G1T0Q6; -.
DR TreeFam; TF105602; -.
DR Proteomes; UP000001811; Chromosome 18.
DR Bgee; ENSOCUG00000011142; Expressed in autopod skin and 15 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0030893; C:meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0030892; C:mitotic cohesin complex; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR GO; GO:0036033; F:mediator complex binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR CDD; cd03272; ABC_SMC3_euk; 1.
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; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 557..670
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 269..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..530
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 702..880
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 907..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 989..1016
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1094..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 144245 MW; 652D77E673D8BC1B CRC64;
MGVRMGSDFL LPAVQGSGLF PGLGRGTMYI KQVIIQGFRS YRDQTIVDPF SSKHNVIVGR
NGSGKSNFFY AIQFVLSDEF SHLRPEQRLA LLHEGTGPRV ISAFVEIIFD NSDNRLPIDK
EEVSLRRVIG AKKDQYFLDK KMVTKNDVMN LLESAGFSRS NPYYIVKQGK INQMATAPDS
QRLKLLREVA GTRVYDERKE ESISLMKETE GKREKINELL KYIEERLHTL EEEKEELAQY
QKWDKMRRAL EYTIYNQELN ETRAKLDELS AKRETSGEKS RQLRDAQQDA RDKMEDIERQ
VRELKTKISA MKEEKEQLSA ERQEQIKQRT KLELKAKDLQ DELAGNSEQR KRLLKERQKL
LEKIEEKQKE LAETEPKFNS VKEKEERGIA RLAQATQERT DLYAKQGRGS QFTSKEERDK
WIKKELKSLD QAINDKKRQI AAIHKDLEDT EANKEKNLEQ YNKLDQDLNE VKARVEELDR
KYYEVKNKKD ELQSERNYLW REENAEQQAL AAKREDLEKK QQLLRAATGK AILNGIDSIN
KVLDHFRRKG INQHVQNGYH GIVMNNFECE PAFYTCVEVT AGNRLFYHIV DSDEVSTKIL
MEFNKMNLPG EVTFLPLNKL DVRDTAYPET NDAIPMISKL RYNPRFDKAF KHVFGKTLIC
RSMEVSTQLA RAFTMDCITL EGDQVSHRGA LTGGYYDTRK SRLELQKDVR KAEEELGELE
AKLNENLRRN IERINNEIDQ LMNQMQQIET QQRKFKASRD SILSEMKMLK EKRQQSEKTF
MPKQRSLQSL EASLHAMEST RESLKAELGT DLLSQLSLED QKRVDALNDE IRQLQQENRQ
LLNERIKLEG IITRVETYLN ENLRKRLDQV EQELNELRET EGGTVLTATT SELEAINKRV
KDTMARSEDL DNSIDKTEAG IKELQKSMER WKNMEKEHMD AINHDTKELE KMTNRQGMLL
KKKEECMKKI RELGSLPQEA FEKYQTLSLK QLFRKLEQCN TELKKYSHVN KKALDQFVNF
SEQKEKLIKR QEELDRGYKS IMELMNVLEL RKYEAIQLTF KQVSKNFSEV FQKLVPGGKA
TLVMKKGDVE GSQSQDEGEG SGESERGSGS QSSVPSVDQF TGVGIRVSFT GKQGEMREMQ
QLSGGQKSLV ALALIFAIQK CDPAPFYLFD EIDQALDAQH RKAVSDMIME LAVHAQFITT
TFRPELLESA DKFYGVKFRN KVSHIDVITA EMAKDFVEDD TTHG
//
