Q9Z1M9 (SMC1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Structural maintenance of chromosomes protein 1A
Short name=SMC protein 1A
Short name=SMC-1A

Gene names

Name:	Smc1a
Synonyms:	Smc1, Smc1l1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.
Subunit structure	Interacts with POLE. Forms a heterodimer with SMC3 in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or meiosis-specific SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or meiosis-specific STAG3), which interacts with RAD21. In germ cell cohesin complexes, SMC1A is mutually exclusive with SMC1B. Interacts with BRCA1. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/APRIN and PDS5B/SCC-112. Interacts with NDC80 By similarity. Interacts with RPGR By similarity. Interacts with SYCP2. Ref.2
Subcellular location	Nucleus By similarity. Chromosome By similarity. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function By similarity.
Domain	The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure By similarity.
Post-translational modification	Phosphorylated upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation By similarity.
Sequence similarities	Belongs to the SMC family. SMC1 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA repair Meiosis Mitosis
Cellular component	Chromosome Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle checkpoint Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome condensation Inferred from electronic annotation. Source: InterPro meiosis Inferred from direct assay Ref.2. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW response to radiation Inferred from sequence or structural similarity. Source: UniProtKB signal transduction in response to DNA damage Inferred from sequence or structural similarity. Source: UniProtKB sister chromatid cohesion Inferred from electronic annotation. Source: InterPro
Cellular_component	kinetochore Inferred from sequence or structural similarity. Source: UniProtKB meiotic cohesin complex Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1233	1233	Structural maintenance of chromosomes protein 1A		PRO_0000118991
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	504 – 659	156	Flexible hinge
	Coiled coil	104 – 124	21	Potential
	Coiled coil	163 – 503	341	Potential
	Coiled coil	660 – 935	276	Potential
	Coiled coil	991 – 1068	78	Potential
	Compositional bias	1128 – 1163	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	358	1	Phosphoserine By similarity
	Modified residue	360	1	Phosphoserine By similarity
	Modified residue	648	1	N6-acetyllysine By similarity
	Modified residue	713	1	N6-acetyllysine By similarity
	Modified residue	957	1	Phosphoserine By similarity
	Modified residue	966	1	Phosphoserine By similarity
	Modified residue	970	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z1M9 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A20C18C1E07E8F30	FASTA	1,233	143,205
	10 20 30 40 50 60 MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 70 80 90 100 110 120 LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 130 140 150 160 170 180 LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE 190 200 210 220 230 240 DTQFNYHRKK NIAAERKEAK QEKEEADRYQ ALKDEVVRAQ VQLQLFKLYH NEVEIEKLNK 250 260 270 280 290 300 ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 310 320 330 340 350 360 AKENTSHKIK KLEAAKKSLQ NRQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS 370 380 390 400 410 420 QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK 430 440 450 460 470 480 IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV 490 500 510 520 530 540 MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK 550 560 570 580 590 600 NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 610 620 630 640 650 660 EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK 670 680 690 700 710 720 AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE 730 740 750 760 770 780 QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF 790 800 810 820 830 840 CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ 850 860 870 880 890 900 TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 910 920 930 940 950 960 ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGGSQGE 970 980 990 1000 1010 1020 ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI 1030 1040 1050 1060 1070 1080 AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN 1090 1100 1110 1120 1130 1140 IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL 1150 1160 1170 1180 1190 1200 LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 1210 1220 1230 IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ

References

[1]	"Molecular characterization of a rat heterochromatin-associated SMC-protein." Althoff B., Voelkl A., Fahimi D., Baumgart E. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes and synaptonemal complexes." Eijpe M., Heyting C., Gross B., Jessberger R. J. Cell Sci. 113:673-682(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYCP2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ005113 mRNA. Translation: CAA06377.1.
IPI	IPI00209018.
RefSeq	NP_113871.1. NM_031683.1.
UniGene	Rn.11763.
3D structure databases
ProteinModelPortal	Q9Z1M9.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000004364.
PTM databases
PhosphoSite	Q9Z1M9.
Proteomic databases
PaxDb	Q9Z1M9.
PRIDE	Q9Z1M9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	63996.
KEGG	rno:63996.
Organism-specific databases
CTD	8243.
RGD	61991. Smc1a.
Phylogenomic databases
eggNOG	COG1196.
HOGENOM	HOG000195481.
HOVERGEN	HBG039593.
KO	K06636.
OrthoDB	EOG4HX507.
Gene expression databases
ArrayExpress	Q9Z1M9.
Genevestigator	Q9Z1M9.
Family and domain databases
InterPro	IPR003395. RecF/RecN/SMC. IPR024704. SMC. IPR010935. SMC_hinge. [Graphical view]
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view]
PIRSF	PIRSF005719. SMC. 1 hit.
SMART	SM00968. SMC_hinge. 1 hit. [Graphical view]
SUPFAM	SSF75553. SMC_hinge. 1 hit.
ProtoNet	Search...
Other
NextBio	612558.

Entry information

Entry name

SMC1A_RAT

Accession

Primary (citable) accession number: Q9Z1M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program