NSE1_RAT
ID NSE1_RAT Reviewed; 266 AA.
AC Q499U6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog;
DE Short=Non-SMC element 1 homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN Name=Nsmce1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: RING-type zinc finger-containing E3 ubiquitin ligase that
CC assembles with melanoma antigen protein (MAGE) to catalyze the direct
CC transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a
CC specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE
CC stimulates and specifies ubiquitin ligase activity likely through
CC recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme
CC at the E3:substrate complex. Involved in maintenance of genome
CC integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1
CC ubiquitin ligase are components of SMC5-SMC6 complex and may positively
CC regulate homologous recombination-mediated DNA repair.
CC {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WV22};
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC domains of the SMC5-SMC6 heterodimer. Interacts with NSMCE3.
CC {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WV22}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q8WV22}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH99757.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC099757; AAH99757.1; ALT_INIT; mRNA.
DR RefSeq; NP_001034700.1; NM_001039611.1.
DR RefSeq; XP_006230353.1; XM_006230291.3.
DR RefSeq; XP_006230354.1; XM_006230292.3.
DR RefSeq; XP_006230355.1; XM_006230293.3.
DR AlphaFoldDB; Q499U6; -.
DR SMR; Q499U6; -.
DR STRING; 10116.ENSRNOP00000051912; -.
DR PaxDb; Q499U6; -.
DR GeneID; 361645; -.
DR KEGG; rno:361645; -.
DR UCSC; RGD:1307760; rat.
DR CTD; 197370; -.
DR RGD; 1307760; Nsmce1.
DR VEuPathDB; HostDB:ENSRNOG00000015218; -.
DR eggNOG; KOG4718; Eukaryota.
DR HOGENOM; CLU_045153_3_1_1; -.
DR InParanoid; Q499U6; -.
DR OrthoDB; 1159451at2759; -.
DR PhylomeDB; Q499U6; -.
DR TreeFam; TF314721; -.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q499U6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015218; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q499U6; baseline and differential.
DR Genevisible; Q499U6; RN.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR014857; Znf_RING-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; PTHR20973; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA recombination; DNA repair; Metal-binding;
KW Nucleus; Reference proteome; Telomere; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..266
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000270947"
FT ZN_FING 191..232
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..102
FT /note="Interaction with NSMCE3"
FT /evidence="ECO:0000250|UniProtKB:Q8WV22"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 30702 MW; AF60161836798E6E CRC64;
MQGSTRRAGA MTDVHRRFLQ LLMTHGVLEE WEVRRLQNHC YKVHDRNATV DKLEDFINNI
NSVLESLYIE IKKGITEDDG RPIYALVNLA TTSVSKMATD FAENELDLFR KALELIVDSE
TGFASSTNIL NLVDQLKGKK MRKKEAEQVL QKFVQSKWLI EKEGEFTLHG RAILEMEQFI
RESYPDAVKM CNICHSLLIQ GQSCETCGIR MHLPCVAKYF QSTAEPRCPH CNDYWPHDIP
EVFDPEKERE AGISKSSRKS LRTRQH
