SMC1_CAEEL
ID SMC1_CAEEL Reviewed; 1262 AA.
AC O01789; Q2A957;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Structural maintenance of chromosomes protein 1 {ECO:0000312|WormBase:F28B3.7a};
DE AltName: Full=High incidence of males protein 1 {ECO:0000312|WormBase:F28B3.7a};
GN Name=him-1 {ECO:0000312|WormBase:F28B3.7a};
GN Synonyms=smc-1 {ECO:0000312|WormBase:F28B3.7a};
GN ORFNames=F28B3.7 {ECO:0000312|WormBase:F28B3.7a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=12808038; DOI=10.1091/mbc.e02-09-0603;
RA Mito Y., Sugimoto A., Yamamoto M.;
RT "Distinct developmental function of two Caenorhabditis elegans homologs of
RT the cohesin subunit Scc1/Rad21.";
RL Mol. Biol. Cell 14:2399-2409(2003).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP COHESIN COMPLEX, INTERACTION WITH SCC-1; SCC-3; SMC-3 AND TIM-1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12827206; DOI=10.1038/nature01697;
RA Chan R.C., Chan A., Jeon M., Wu T.F., Pasqualone D., Rougvie A.E.,
RA Meyer B.J.;
RT "Chromosome cohesion is regulated by a clock gene paralogue TIM-1.";
RL Nature 423:1002-1009(2003).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=21856158; DOI=10.1016/j.cub.2011.07.007;
RA Lightfoot J., Testori S., Barroso C., Martinez-Perez E.;
RT "Loading of meiotic cohesin by SCC-2 is required for early processing of
RT DSBs and for the DNA damage checkpoint.";
RL Curr. Biol. 21:1421-1430(2011).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair (By similarity). Required for chromosome segregation during
CC mitosis (PubMed:12808038, PubMed:12827206). Central component of
CC cohesin complex (PubMed:12827206). The cohesin complex is required for
CC the cohesion of sister chromatids after DNA replication
CC (PubMed:12827206). The cohesin complex apparently forms a large
CC proteinaceous ring within which sister chromatids can be trapped (By
CC similarity). At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate (By similarity).
CC {ECO:0000250|UniProtKB:Q14683, ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206}.
CC -!- SUBUNIT: Component of the cohesin complex, composed of the smc-1 and
CC smc-3 heterodimer attached via their SMC hinge domain, scc-1 which
CC links them, and scc-3. Interacts with smc-3, scc-1, scc-3 and tim-1.
CC {ECO:0000269|PubMed:12827206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:21856158}. Chromosome {ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:21856158}. Note=Has diffuse nuclear appearance at
CC interphase during mitosis in somatic and germline tissues
CC (PubMed:12827206). Colocalizes with rec-8 along synapsed chromosomes
CC during meiotic pachytene and diakinesis (PubMed:12827206). Diffuse
CC nuclear accumulation in meiotic pachytene (PubMed:21856158).
CC {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F28B3.7a};
CC IsoId=O01789-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F28B3.7b};
CC IsoId=O01789-2; Sequence=VSP_057589;
CC -!- DISRUPTION PHENOTYPE: Defective chromosome segregation during germline
CC mitosis, resulting in aneuploidy (PubMed:12827206). RNAi-mediated
CC knock-down is embryonic lethal and results in aberrant chromosome
CC segregation in mitosis (PubMed:12827206, PubMed:12808038).
CC {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
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DR EMBL; FO081198; CCD69832.1; -; Genomic_DNA.
DR EMBL; FO081198; CCD69826.1; -; Genomic_DNA.
DR RefSeq; NP_001040658.2; NM_001047193.4. [O01789-1]
DR RefSeq; NP_001040659.1; NM_001047194.1. [O01789-2]
DR AlphaFoldDB; O01789; -.
DR SMR; O01789; -.
DR ComplexPortal; CPX-967; Nuclear mitotic cohesin complex.
DR STRING; 6239.F28B3.7a; -.
DR EPD; O01789; -.
DR PaxDb; O01789; -.
DR PeptideAtlas; O01789; -.
DR EnsemblMetazoa; F28B3.7a.1; F28B3.7a.1; WBGene00001860. [O01789-1]
DR EnsemblMetazoa; F28B3.7b.1; F28B3.7b.1; WBGene00001860. [O01789-2]
DR GeneID; 172116; -.
DR KEGG; cel:CELE_F28B3.7; -.
DR UCSC; F28B3.7a.1; c. elegans.
DR CTD; 172116; -.
DR WormBase; F28B3.7a; CE42002; WBGene00001860; him-1. [O01789-1]
DR WormBase; F28B3.7b; CE39925; WBGene00001860; him-1. [O01789-2]
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00940000171089; -.
DR HOGENOM; CLU_001042_0_2_1; -.
DR InParanoid; O01789; -.
DR OMA; GIDNHEG; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; O01789; -.
DR Reactome; R-CEL-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-CEL-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:O01789; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001860; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0008278; C:cohesin complex; IPI:WormBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:WormBase.
DR GO; GO:0009411; P:response to UV; IMP:WormBase.
DR GO; GO:0010165; P:response to X-ray; IMP:WormBase.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
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 Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA repair; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1262
FT /note="Structural maintenance of chromosomes protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432834"
FT DOMAIN 524..642
FT /note="SMC hinge"
FT REGION 965..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..497
FT /evidence="ECO:0000255"
FT COILED 680..937
FT /evidence="ECO:0000255"
FT COILED 1017..1086
FT /evidence="ECO:0000255"
FT MOTIF 1148..1183
FT /note="DA-box"
FT /evidence="ECO:0000250|UniProtKB:P32908"
FT COMPBIAS 975..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1122
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057589"
SQ SEQUENCE 1262 AA; 144217 MW; 8473653CC05DB70A CRC64;
MRGGSSLDSF PGKGTLHTLE IENFKSYKGK HTIGPFTRFT AIIGPNGSGK SNLMDAISFV
LGEKPSSLRV RKYADLIHGA PINKPVAKKC RVTMNYKYSD GKVKAFTRGV NNGTSEHLLD
GQTVTSAAYS QEMESINIFI KARNFLVYQG AIENIAMKTP KERTQLFEEL SRSHEFQAEY
ERLKVEMTKA EDDTQHNMNK RRGIAQEKRE AKMEKDEAEK YQTMKNELAA KSTMLFLHQL
FHCERTIDES KEEINAQKKT IASLEATRSK EEAKIAAVHQ EHRKALREVQ KMTRKLDQKE
TDLAEKQQNM LTLKVSVAHE HKKLEIAKKM LAAAESKAEN NSTQLADLKK SKKELEKKKA
AYEAEIQDMM QRGELNLSDE QVREYGQLKD QAQRESAMVQ RELLMAEQVF EGDKSSLNHE
LRRQKEHQER VKAKEGDVRR IETQIATLAQ RIKETEEETK ILKADLKKIE NDVVIDKSAA
AEYNKELVAV VRQLSEASGD SAEGERNQRR TEALEGLKKN FPESVYGRLV DLCQPSHKRF
NIATTKILQK HMNSIVCDTE ETAAKAIVYL KDHRYPPETF LPNDALVVNP LNEKLREIKK
PAGVKLVFDV INPQHQAARK ALQFVCGNAL VCESQEDAKQ LAYGGGELKD RFKAVSMDGT
LFQQSGVMSG GSADLRQKSK KWDEKVVKQL REKRNQLNEK IADLQKHRRR ELEVESVRSK
INGNEQRLAM MKRDLKNMRE MQLERLQNEL EGMTAEMNML PPRISNCQEK LERSESTLKS
LQTKSNEVAD RIFADFCTRV GIASIRDYEN REMRIKQEME DKLRSFDDDI QKLAYEIDFV
TEQDGNRKVE VEKEKVSQID RQYKDMKKKE KTAAAALKEH TESMEQDKEV LEEKKALSHK
LETEWNEVKK IAQVAMKDFT KAEKELLRLE SLLTKKQYER HSLLHSVKLG QIALPLKSGS
MADVEYEEDD GDDTASQSSQ SATDGPSVSE EQIQREQHIK INYDSLPREY KDVDDDDGVR
QMSNRLNVEI DELQKNVSKM NAPNLKANQR MAEVKEREAE STEELENARK KAKRIRQQFE
KVKTDRYRRF QDFFDPVANT IDDIYKQLSR NTSAQAFLGA DNMEEPYLDG IQYNCVAPGK
RFRPMDNLSG GEKTIAALAL LFAVHGRNPA PFFVLDEIDA ALDNTNIGKV ASYICESARE
HMQIIVISLK EEFYNKADSL IGIFPYPAAC TTSGVLTFDL TRFKQIGLNE MTENPPTPSI
AT
