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Database: UniProt
Entry: I3L8X3_PIG
LinkDB: I3L8X3_PIG
Original site: I3L8X3_PIG 
ID   I3L8X3_PIG              Unreviewed;       661 AA.
AC   I3L8X3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=RAD17 checkpoint clamp loader component {ECO:0000313|Ensembl:ENSSSCP00000020484.2};
GN   Name=RAD17 {ECO:0000313|Ensembl:ENSSSCP00000020484.2,
GN   ECO:0000313|VGNC:VGNC:92052};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000020484.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000020484.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000020484.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000020484.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the rad17/RAD24 family.
CC       {ECO:0000256|ARBA:ARBA00006168}.
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DR   AlphaFoldDB; I3L8X3; -.
DR   Ensembl; ENSSSCT00000023550.2; ENSSSCP00000020484.2; ENSSSCG00000016960.5.
DR   VGNC; VGNC:92052; RAD17.
DR   GeneTree; ENSGT00440000039046; -.
DR   HOGENOM; CLU_1932420_0_0_1; -.
DR   Proteomes; UP000008227; Chromosome 16.
DR   Bgee; ENSSSCG00000016960; Expressed in testis and 44 other cell types or tissues.
DR   ExpressionAtlas; I3L8X3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031389; C:Rad17 RFC-like complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018324; Rad17/Rad24_fun/met.
DR   NCBIfam; TIGR00602; rad24; 1.
DR   PANTHER; PTHR12172; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR   PANTHER; PTHR12172:SF0; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR   Pfam; PF03215; Rad17; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   REGION          77..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..661
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  74930 MW;  F06CC6751C446EA1 CRC64;
     MLLPEGELYF NVLQVVYSGW ELSKFIMSKT FLRPKVSSTK VTDWVDPSFD DFSETTNIST
     INATSLSVNN SSLRRKKVPS TLESRRSPTR KRGNLSSSKQ IYSLENSKEY VSENEPWVDK
     YKPETQHELA VHKKKIEEVE TWLKVEVLER QPTQGGSILL ITGPPGCGKT ATIKILSKEH
     GIQVQEWINP VLPEFQKDDF KEIFNPESSF HIFPYQSQIA VFKEFLLRAT KYNKLQMLGD
     DLTTDKKIIL VEDLPNQFYR DPHILHEVLR RYVQVGRCPL IFIISDSLSG DNNHRLLFPK
     EIQEECAISN ISFNPVAPTI MMKFLNRIVT KEANKNGGKI IVPDKTSLEL LCQGCSGDIR
     SAINSLQFSS STGKNNLWPR KKGTSSLKSD AALSKSKRRQ KPDRVFENQE VQAIGGKDVS
     LFLFRALGKI LYCKRASVTE LDSPRLPSHL SEYERDTLLI HPEEVVEMSH MPGDLFNLYL
     HQNYVDFFMD VDDLVRASEF LSFADILSGD WNYRENCLAA KALFSDFCLS PVCLQTQLLP
     YLALLTIPMR NQAQISFIQD IGRLPLKRHF GRLKMEALTD REHGMMDLDS GDEAQLGGGQ
     PTEEALGEPT PSTEPEPELL SLPLSQNSGS ELPASQPRPF SAQGDMEEED MIIEDYESDG
     T
//
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