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Structural maintenance of chromosomes protein 1 (High incidence of males protein 1)

 SMC1_CAEEL              Reviewed;        1262 AA.
O01789; Q2A957;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 4.
23-MAY-2018, entry version 147.
RecName: Full=Structural maintenance of chromosomes protein 1 {ECO:0000312|WormBase:F28B3.7a};
AltName: Full=High incidence of males protein 1 {ECO:0000312|WormBase:F28B3.7a};
Name=him-1 {ECO:0000312|WormBase:F28B3.7a};
Synonyms=smc-1 {ECO:0000312|WormBase:F28B3.7a};
ORFNames=F28B3.7 {ECO:0000312|WormBase:F28B3.7a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION.
PubMed=12808038; DOI=10.1091/mbc.E02-09-0603;
Mito Y., Sugimoto A., Yamamoto M.;
"Distinct developmental function of two Caenorhabditis elegans
homologs of the cohesin subunit Scc1/Rad21.";
Mol. Biol. Cell 14:2399-2409(2003).
[3] {ECO:0000305}
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
COHESIN COMPLEX, INTERACTION WITH SCC-1; SCC-3; SMC-3 AND TIM-1,
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=12827206; DOI=10.1038/nature01697;
Chan R.C., Chan A., Jeon M., Wu T.F., Pasqualone D., Rougvie A.E.,
Meyer B.J.;
"Chromosome cohesion is regulated by a clock gene paralogue TIM-1.";
Nature 423:1002-1009(2003).
[4] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=21856158; DOI=10.1016/j.cub.2011.07.007;
Lightfoot J., Testori S., Barroso C., Martinez-Perez E.;
"Loading of meiotic cohesin by SCC-2 is required for early processing
of DSBs and for the DNA damage checkpoint.";
Curr. Biol. 21:1421-1430(2011).
-!- FUNCTION: Involved in chromosome cohesion during cell cycle and in
DNA repair (By similarity). Required for chromosome segregation
during mitosis (PubMed:12808038, PubMed:12827206). Central
component of cohesin complex (PubMed:12827206). The cohesin
complex is required for the cohesion of sister chromatids after
DNA replication (PubMed:12827206). The cohesin complex apparently
forms a large proteinaceous ring within which sister chromatids
can be trapped (By similarity). At anaphase, the complex is
cleaved and dissociates from chromatin, allowing sister chromatids
to segregate (By similarity). {ECO:0000250|UniProtKB:Q14683,
ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}.
-!- SUBUNIT: Component of the cohesin complex, composed of the smc-1
and smc-3 heterodimer attached via their hinge domain, scc-1 which
links them, and scc-3. Interacts with smc-3, scc-1, scc-3 and tim-
1. {ECO:0000269|PubMed:12827206}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206,
ECO:0000269|PubMed:21856158}. Chromosome
{ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}.
Note=Has diffuse nuclear appearance at interphase during mitosis
in somatic and germline tissues (PubMed:12827206). Colocalizes
with rec-8 along synapsed chromosomes during meiotic pachytene and
diakinesis (PubMed:12827206). Diffuse nuclear accumulation in
meiotic pachytene (PubMed:21856158). {ECO:0000269|PubMed:12827206,
ECO:0000269|PubMed:21856158}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a {ECO:0000312|WormBase:F28B3.7a};
IsoId=O01789-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:F28B3.7b};
IsoId=O01789-2; Sequence=VSP_057589;
Note=No experimental confirmation available. {ECO:0000305};
-!- DISRUPTION PHENOTYPE: Defective chromosome segregation during
germline mitosis, resulting in aneuploidy (PubMed:12827206). RNAi-
mediated knock-down is embryonic lethal and results in aberrant
chromosome segregation in mitosis (PubMed:12827206,
PubMed:12808038). {ECO:0000269|PubMed:12808038,
ECO:0000269|PubMed:12827206}.
-!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
{ECO:0000305}.
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EMBL; FO081198; CCD69832.1; -; Genomic_DNA.
EMBL; FO081198; CCD69826.1; -; Genomic_DNA.
RefSeq; NP_001040658.2; NM_001047193.4. [O01789-1]
RefSeq; NP_001040659.1; NM_001047194.1. [O01789-2]
UniGene; Cel.5375; -.
ProteinModelPortal; O01789; -.
SMR; O01789; -.
STRING; 6239.F28B3.7a.1; -.
EPD; O01789; -.
PaxDb; O01789; -.
PeptideAtlas; O01789; -.
EnsemblMetazoa; F28B3.7a; F28B3.7a; WBGene00001860. [O01789-1]
GeneID; 172116; -.
KEGG; cel:CELE_F28B3.7; -.
UCSC; F28B3.7a.1; c. elegans.
CTD; 172116; -.
WormBase; F28B3.7a; CE42002; WBGene00001860; him-1. [O01789-1]
WormBase; F28B3.7b; CE39925; WBGene00001860; him-1. [O01789-2]
eggNOG; KOG0018; Eukaryota.
eggNOG; COG1196; LUCA.
GeneTree; ENSGT00580000081569; -.
HOGENOM; HOG000195481; -.
InParanoid; O01789; -.
KO; K06636; -.
OMA; FNFKSYK; -.
OrthoDB; EOG091G00R5; -.
PhylomeDB; O01789; -.
PRO; PR:O01789; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00001860; -.
GO; GO:0008278; C:cohesin complex; IPI:WormBase.
GO; GO:0000790; C:nuclear chromatin; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:WormBase.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:WormBase.
GO; GO:0009411; P:response to UV; IMP:WormBase.
GO; GO:0010165; P:response to X-ray; IMP:WormBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003395; RecF/RecN/SMC_N.
InterPro; IPR024704; SMC.
InterPro; IPR010935; SMC_hinge.
InterPro; IPR036277; SMC_hinge_sf.
Pfam; PF06470; SMC_hinge; 1.
Pfam; PF02463; SMC_N; 1.
PIRSF; PIRSF005719; SMC; 1.
SMART; SM00968; SMC_hinge; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF75553; SSF75553; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Chromosome;
Coiled coil; Complete proteome; DNA damage; DNA repair; Mitosis;
Nucleus; Reference proteome.
CHAIN 1 1262 Structural maintenance of chromosomes
protein 1. {ECO:0000305}.
/FTId=PRO_0000432834.
COILED 171 497 {ECO:0000255}.
COILED 680 937 {ECO:0000255}.
COILED 1017 1086 {ECO:0000255}.
MOTIF 1148 1183 DA-box. {ECO:0000250|UniProtKB:P32908}.
VAR_SEQ 1 1122 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_057589.
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


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