ID F7F143_ORNAN Unreviewed; 1220 AA.
AC F7F143;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=SMC3 {ECO:0000313|Ensembl:ENSOANP00000002549.4};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000002549.4, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000002549.4}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000002549.4};
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 {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR AlphaFoldDB; F7F143; -.
DR STRING; 9258.ENSOANP00000002549; -.
DR Ensembl; ENSOANT00000002550.4; ENSOANP00000002549.4; ENSOANG00000001596.4.
DR eggNOG; KOG0964; Eukaryota.
DR GeneTree; ENSGT00580000081628; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR TreeFam; TF105602; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000001596; Expressed in fibroblast and 8 other cell types or tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd03272; ABC_SMC3_euk; 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 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:UP000002279}.
FT DOMAIN 533..646
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 245..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..506
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 678..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 890..917
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 965..992
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1070..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 141773 MW; E95373EBAF611B08 CRC64;
MGFGYLEQVI IQGFRSYRDQ TIVDPFSSKH NVIVGRNGSG KSNFFYAIQF VLSDEFSHLR
PEQRLALLHE GTGPRVISAF VEIIFDNSDN RLPIDKEEVS LRRVIGAKKD QYFLDKKMVT
KNDVMNLLES AGFSRSNPYY IVKQGKINQM ATAPDSQRLK LLREVAGTRV YDERKEESIS
LMKETEGKRE KINELLKYIE ERLHTLEEEK EELAQYQKWD KMRRALEYTI YNQELNETRA
KLDELSAKRE TSGEKSRQLR DAQQDARDKM EDIERQVREL KTKISAMKEE KEQLSAERQE
QIKQRTKLEL KAKDLQDELA GNSEQRKRLL KERQKLLEKI EEKQKELAET EPKFNSVKEK
EERGIARLAQ ATQERTDLYA KQGRGSQFTS KEERDKWIKK ELKSLDQAIN DKKRQIAAIH
KDLEDTEANK EKNLEQYSKL DQDLNEVKAR VEELDRKYYE VKNKKDELQS ERNYLWREEN
AEQQALAAKR EDLEKKQQLL RAATGKAILN GIDSINKVLE HFRRKGINQH VQNGYHGIVM
NNFECEPAFY TCVEVTAGNR LFYHIVDSDE VSTKILMEFN KMNLPGEVTF LPLNKLDVRD
TAYPETNDAI PMISKLRYNP RFDKAFKHVF GKTLICRSME VSTQLARAFT MDCITLEGDQ
VSHRGALTGG YYDTRKSRLE LQKDVRKAEE ELGELEAKLN ENLRRNIERI NNEIDQLMNQ
MQQIETQQRK FKASRDSILS EMKMLKEKRQ QSEKTFMPKQ RSLQSLEASL HAMESTRESL
KAELGTDLLS QLSLDDQKRV DALNDEIRQL QQENRQLLNE RIKLEGIITR VETYLNENLR
KRLDQVEQEL NELRETEGGT VLTATTSELE AINKRVKDTL ARSDDLDNSI DKTEVGIKDL
QKSMERWKNM EKEHMDAINH DTKELEKMTN RQGMLLKKKE ECMKKIRELG SLPQEAFEKY
QTLSLKQLFR KLEQCNTELK KYSHVNKKAL DQFVNFSEQK EKLIKRQEEL DRGYKSIMEL
MNVLELRKYE AIQLTFKQVS KNFSEVFQKL VPGGKATLVM KKGDVEGSQS QDEGEGSAES
ERGSGSQSSV PSVDQFTGVG IRVSFTGKQG EMREMQQLSG GQKSLVALAL IFAIQKCDPA
PFYLFDEIDQ ALDAQHRKAV SDMIMELAVH AQFITTTFRP ELLESADKFY GVKFRNKVSH
IDVITAEMAK DFVEDDTTHG
//
