SMC1A_RAT
ID SMC1A_RAT Reviewed; 1233 AA.
AC Q9Z1M9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Structural maintenance of chromosomes protein 1A;
DE Short=SMC protein 1A;
DE Short=SMC-1A;
GN Name=Smc1a; Synonyms=Smc1, Smc1l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Althoff B., Voelkl A., Fahimi D., Baumgart E.;
RT "Molecular characterization of a rat heterochromatin-associated SMC-
RT protein.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH SYCP2.
RX PubMed=10652260; DOI=10.1242/jcs.113.4.673;
RA Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes
RT and synaptonemal complexes.";
RL J. Cell Sci. 113:673-682(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair. Central component of cohesin complex. The cohesin complex is
CC required for the cohesion of sister chromatids after DNA replication.
CC The cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped. At anaphase, the complex is
CC cleaved and dissociates from chromatin, allowing sister chromatids to
CC segregate. The cohesin complex may also play a role in spindle pole
CC assembly during mitosis. Involved in DNA repair via its interaction
CC with BRCA1 and its related phosphorylation by ATM, or via its
CC phosphorylation by ATR. Works as a downstream effector both in the
CC ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
CC -!- SUBUNIT: Forms a heterodimer with SMC3 in cohesin complexes. Cohesin
CC complexes are composed of the SMC1 (SMC1A or meiosis-specific SMC1B)
CC and SMC3 heterodimer attached via their SMC hinge domain, RAD21 which
CC link them, and one STAG protein (STAG1, STAG2 or meiosis-specific
CC STAG3), which interacts with RAD21. In germ cell cohesin complexes,
CC SMC1A is mutually exclusive with SMC1B. Found in a complex with CDCA5,
CC SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Interacts with STAG3,
CC NDC80, BRAC1, BRAT1 and RPGR. Found in a complex containing POLE and
CC SMC3. Found in a cohesin complex with SMC3, STAG1 and RAD21. The SMC1A-
CC SMC3 heterodimer interacts with the NIPBL-MAU2 heterodimer (By
CC similarity). Interacts with SYCP2 (PubMed:10652260).
CC {ECO:0000250|UniProtKB:O97593, ECO:0000250|UniProtKB:Q14683,
CC ECO:0000250|UniProtKB:Q9CU62, ECO:0000269|PubMed:10652260}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Associates with chromatin. Before prophase it is scattered along
CC chromosome arms. During prophase, most of cohesin complexes dissociate
CC from chromatin probably because of phosphorylation by PLK, except at
CC centromeres, where cohesin complexes remain. At anaphase, the RAD21
CC subunit of the cohesin complex is cleaved, leading to the dissociation
CC of the complex from chromosomes, allowing chromosome separation. In
CC germ cells, cohesin complex dissociates from chromatin at prophase I,
CC and may be replaced by a meiosis-specific cohesin complex. The
CC phosphorylated form on Ser-957 and Ser-966 associates with chromatin
CC during G1/S/G2 phases but not during M phase, suggesting that
CC phosphorylation does not regulate cohesin function (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC3, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable RAD21 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated upon ionizing radiation or DNA methylation.
CC Phosphorylation of Ser-957 and Ser-966 activates it and is required for
CC S-phase checkpoint activation (By similarity).
CC {ECO:0000250|UniProtKB:Q14683}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q14683}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ005113; CAA06377.1; -; mRNA.
DR RefSeq; NP_113871.1; NM_031683.1.
DR AlphaFoldDB; Q9Z1M9; -.
DR SMR; Q9Z1M9; -.
DR BioGRID; 248928; 1.
DR IntAct; Q9Z1M9; 5.
DR STRING; 10116.ENSRNOP00000004364; -.
DR CarbonylDB; Q9Z1M9; -.
DR iPTMnet; Q9Z1M9; -.
DR PhosphoSitePlus; Q9Z1M9; -.
DR jPOST; Q9Z1M9; -.
DR PRIDE; Q9Z1M9; -.
DR GeneID; 63996; -.
DR KEGG; rno:63996; -.
DR CTD; 8243; -.
DR RGD; 61991; Smc1a.
DR eggNOG; KOG0018; Eukaryota.
DR InParanoid; Q9Z1M9; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q9Z1M9; -.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q9Z1M9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0008278; C:cohesin complex; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030893; C:meiotic cohesin complex; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0036033; F:mediator complex binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0072423; P:response to DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISO:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR CDD; cd03275; ABC_SMC1_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR029683; SMC1A_metazoan.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF170; PTHR18937:SF170; 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; DNA damage; DNA repair; Meiosis; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1233
FT /note="Structural maintenance of chromosomes protein 1A"
FT /id="PRO_0000118991"
FT DOMAIN 515..629
FT /note="SMC hinge"
FT REGION 284..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..124
FT /evidence="ECO:0000255"
FT COILED 163..503
FT /evidence="ECO:0000255"
FT COILED 660..935
FT /evidence="ECO:0000255"
FT COILED 991..1068
FT /evidence="ECO:0000255"
FT COMPBIAS 950..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 1037
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CU62"
SQ SEQUENCE 1233 AA; 143205 MW; A20C18C1E07E8F30 CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ ALKDEVVRAQ VQLQLFKLYH NEVEIEKLNK
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
AKENTSHKIK KLEAAKKSLQ NRQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGGSQGE
ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
