SMC1A_BOVIN
ID SMC1A_BOVIN Reviewed; 1233 AA.
AC O97593;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH SMC3.
RX PubMed=10072753; DOI=10.1016/s0378-1119(99)00021-9;
RA Stursberg S., Riwar B., Jessberger R.;
RT "Cloning and characterization of mammalian SMC1 and SMC3 genes and
RT proteins, components of the DNA recombination complexes RC-1.";
RL Gene 228:1-12(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, AND IDENTIFICATION IN A COMPLEX WITH SMC3 AND
RP POLE.
RX PubMed=8670910; DOI=10.1002/j.1460-2075.1996.tb00779.x;
RA Jessberger R., Riwar B., Baechtold H., Akhmedov A.T.;
RT "SMC proteins constitute two subunits of the mammalian recombination
RT complex RC-1.";
RL EMBO J. 15:4061-4068(1996).
RN [3]
RP INTERACTION WITH RPGR, AND MUTAGENESIS OF SER-957 AND SER-966.
RX PubMed=16043481; DOI=10.1074/jbc.m505827200;
RA Khanna H., Hurd T.W., Lillo C., Shu X., Parapuram S.K., He S., Akimoto M.,
RA Wright A.F., Margolis B., Williams D.S., Swaroop A.;
RT "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with
RT SMC1, SMC3, and microtubule transport proteins.";
RL J. Biol. Chem. 280:33580-33587(2005).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair. Involved in DNA repair via its interaction with BRCA1 and its
CC related phosphorylation by ATM, and works as a downstream effector in
CC the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central
CC component of cohesin complex. The cohesin complex is required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC The cohesin complex may also play a role in spindle pole assembly
CC during mitosis. Involved in DNA repair via its interaction with BRCA1
CC and its related phosphorylation by ATM, or via its phosphorylation by
CC ATR. Works as a downstream effector both in the ATM/NBS1 branch and in
CC the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC3 in cohesin complexes
CC (PubMed:10072753). Cohesin complexes are composed of the SMC1 (SMC1A or
CC meiosis-specific SMC1B) and SMC3 heterodimer attached via their SMC
CC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2
CC or meiosis-specific STAG3), which interacts with RAD21. In germ cell
CC cohesin complexes, SMC1A is mutually exclusive with SMC1B. Found in a
CC complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN.
CC Interacts with NDC80, SYCP2, STAG3, BRCA1 and BRAT1. Found in a cohesin
CC complex with SMC3, STAG1 and RAD21. The SMC1A-SMC3 heterodimer
CC interacts with the NIPBL-MAU2 heterodimer (By similarity). Interacts
CC with RPGR (PubMed:16043481). Found in a complex containing POLE and
CC SMC3 (PubMed:8670910). {ECO:0000250|UniProtKB:Q14683,
CC ECO:0000250|UniProtKB:Q9CU62, ECO:0000250|UniProtKB:Q9Z1M9,
CC ECO:0000269|PubMed:10072753, ECO:0000269|PubMed:16043481,
CC ECO:0000269|PubMed:8670910}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC Note=Associates with chromatin. The phosphorylated form on Ser-957 and
CC Ser-966 associates with chromatin during G1/S/G2 phases but not during
CC M phase, suggesting that phosphorylation does not regulate cohesin
CC function (By similarity). 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.
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}.
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DR EMBL; AF072712; AAD13141.1; -; mRNA.
DR PIR; S71602; S71602.
DR RefSeq; NP_777039.1; NM_174614.1.
DR AlphaFoldDB; O97593; -.
DR SMR; O97593; -.
DR BioGRID; 159631; 1.
DR CORUM; O97593; -.
DR STRING; 9913.ENSBTAP00000023619; -.
DR PaxDb; O97593; -.
DR PRIDE; O97593; -.
DR Ensembl; ENSBTAT00000023619; ENSBTAP00000023619; ENSBTAG00000017761.
DR GeneID; 282370; -.
DR KEGG; bta:282370; -.
DR CTD; 8243; -.
DR VEuPathDB; HostDB:ENSBTAG00000017761; -.
DR VGNC; VGNC:34997; SMC1A.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000155614; -.
DR HOGENOM; CLU_001042_0_2_1; -.
DR InParanoid; O97593; -.
DR OMA; YIRDHTT; -.
DR OrthoDB; 326079at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000017761; Expressed in ileum and 113 other tissues.
DR ExpressionAtlas; O97593; baseline and differential.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
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; Centromere;
KW Chromosome; Coiled coil; Direct protein sequencing; DNA damage; DNA repair;
KW Meiosis; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1233
FT /note="Structural maintenance of chromosomes protein 1A"
FT /id="PRO_0000118988"
FT DOMAIN 515..629
FT /note="SMC hinge"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..968
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 949..968
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:0000250|UniProtKB:Q14683"
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"
FT MUTAGEN 957
FT /note="S->A: No effect on interaction with RPGR."
FT /evidence="ECO:0000269|PubMed:16043481"
FT MUTAGEN 966
FT /note="S->A: Abolishes binding with RPGR."
FT /evidence="ECO:0000269|PubMed:16043481"
SQ SEQUENCE 1233 AA; 143248 MW; CB5C8E54789FBC8C CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK 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 SQEEGSSQGE
DSVSGSQRTS NIYAREALIE 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
