SMC1A_XENLA
ID SMC1A_XENLA Reviewed; 1232 AA.
AC O93308;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Structural maintenance of chromosomes protein 1A;
DE Short=SMC protein 1A;
DE Short=SMC-1A;
DE Short=xSMC1;
GN Name=smc1a; Synonyms=smc1, smc1l1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND IDENTIFICATION IN A
RP COHESIN COMPLEX WITH SMC3 AND RAD21.
RC TISSUE=Egg;
RX PubMed=9649503; DOI=10.1101/gad.12.13.1986;
RA Losada A., Hirano M., Hirano T.;
RT "Identification of Xenopus SMC protein complexes required for sister
RT chromatid cohesion.";
RL Genes Dev. 12:1986-1997(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN A COHESIN COMPLEX WITH
RP STAG1; SMC3 AND RAD21.
RC TISSUE=Egg;
RX PubMed=10931856; DOI=10.1083/jcb.150.3.405;
RA Losada A., Yokochi T., Kobayashi R., Hirano T.;
RT "Identification and characterization of SA/Scc3p subunits in the Xenopus
RT and human cohesin complexes.";
RL J. Cell Biol. 150:405-416(2000).
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.
CC -!- SUBUNIT: Forms a heterodimer with SMC3 in cohesin complex. The cohesin
CC complex is composed of the SMC1A and SMC3 heterodimer attached via
CC their SMC hinge domain, RAD21 which link them, and one STAG protein
CC (STAG1 or STAG2), which interacts with RAD21.
CC {ECO:0000269|PubMed:10931856, ECO:0000269|PubMed:9649503}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
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.
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 -!- 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; AF051784; AAC26807.1; -; mRNA.
DR RefSeq; NP_001165905.1; NM_001172434.1.
DR AlphaFoldDB; O93308; -.
DR SMR; O93308; -.
DR BioGRID; 1078967; 8.
DR IntAct; O93308; 8.
DR PRIDE; O93308; -.
DR GeneID; 100379087; -.
DR CTD; 100379087; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030893; C:meiotic cohesin complex; ISS:UniProtKB.
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: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:0072423; P:response to DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
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 ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; DNA damage; DNA repair; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1232
FT /note="Structural maintenance of chromosomes protein 1A"
FT /id="PRO_0000118992"
FT DOMAIN 515..629
FT /note="SMC hinge"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..503
FT /evidence="ECO:0000255"
FT COILED 660..935
FT /evidence="ECO:0000255"
FT COILED 997..1068
FT /evidence="ECO:0000255"
FT COMPBIAS 949..970
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"
SQ SEQUENCE 1232 AA; 142628 MW; 50920422ED113722 CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFHRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEDSGE EKVFSRVIVG GSSEYKINNK VVQLSEYSDS
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEAERYQ RLKDEVARAQ IQLQLFKLYH NESEIEKLNK
ELSVKNKGIE KDKKHMDKVE EELKDKKKEL GKMMREQQAI EKEIKEKDAE LNQKLPQYIK
AKENPSHKIK KFRAAKKSLQ NAQKQYKKRK ADMDELEKEM LSVEKARQEF EERMEEESQS
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK
IKQKLRELEE NQKRIEKLEE YIATSKQSLE EQKNLEETLT EEVEMAKRRI DEINSELNQV
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDERLRELKG AKLVIDVIRY
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE
QTKTRHLAMN MQEKSKLESE LANFSPRIND IKRIIQSRDR EMKDLKEKMN QVEDEVFEEF
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDYEKNQLKE DQGKVQTWEQ
SVKKDDNEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHL MEDIRKKLGS
ANKEVTHLQK EVTAIETKLE QKRSDRHNLL QACKMSDIKL PLSKGTMDDI SQEEGSSQGE
ESASSSQRSS TVYAKEALIE IDYSDLSEDL KDAVADDDIK QEMSALHQKI NEQQSILQRI
SAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QTKKERFDRF NACFESVATN
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL
LFAIHSYKPS PFFVLDEIDA ALDNTNIGKV ANYIKEQSMS NFQAIVISLK EEFYTKAESL
IGVYPEQGDC VISKVLTFDL TKYPDANPNP ND
