INT3_PONAB
ID INT3_PONAB Reviewed; 1043 AA.
AC Q5RE70;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Integrator complex subunit 3;
DE Short=Int3;
DE AltName: Full=SOSS complex subunit A;
DE AltName: Full=Sensor of single-strand DNA complex subunit A;
DE Short=SOSS-A;
DE Short=Sensor of ssDNA subunit A;
GN Name=INTS3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Integrator (INT) complex. The Integrator
CC complex is involved in the small nuclear RNAs (snRNA) U1 and U2
CC transcription and in their 3'-box-dependent processing. The Integrator
CC complex is associated with the C-terminal domain (CTD) of RNA
CC polymerase II largest subunit (POLR2A) and is recruited to the U1 and
CC U2 snRNAs genes. Mediates recruitment of cytoplasmic dynein to the
CC nuclear envelope, probably as component of the INT complex.
CC {ECO:0000250|UniProtKB:Q68E01}.
CC -!- FUNCTION: Component of the SOSS complex, a multiprotein complex that
CC functions downstream of the MRN complex to promote DNA repair and G2/M
CC checkpoint. The SOSS complex associates with single-stranded DNA at DNA
CC lesions and influences diverse endpoints in the cellular DNA damage
CC response including cell-cycle checkpoint activation, recombinational
CC repair and maintenance of genomic stability. The SOSS complex is
CC required for efficient homologous recombination-dependent repair of
CC double-strand breaks (DSBs) and ATM-dependent signaling pathways. In
CC the SOSS complex, it is required for the assembly of the complex and
CC for stabilization of the complex at DNA damage sites.
CC {ECO:0000250|UniProtKB:Q68E01}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Component of the SOSS
CC complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-
CC A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are
CC more abundant than complexes containing SOSS-B2/NABP1. Interacts with
CC SOSS-B1/NABP2, SOSS-B2/NABP1 and SOSS-C/INIP; the interaction is
CC direct. Interacts with NBN/NBS1. {ECO:0000250|UniProtKB:Q68E01}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q68E01}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q68E01}. Note=Localizes to nuclear foci
CC following DNA damage. {ECO:0000250|UniProtKB:Q68E01}.
CC -!- SIMILARITY: Belongs to the Integrator subunit 3 family. {ECO:0000305}.
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DR EMBL; CR857667; CAH89937.1; -; mRNA.
DR RefSeq; NP_001124909.1; NM_001131437.1.
DR AlphaFoldDB; Q5RE70; -.
DR SMR; Q5RE70; -.
DR STRING; 9601.ENSPPYP00000000932; -.
DR GeneID; 100171777; -.
DR KEGG; pon:100171777; -.
DR CTD; 65123; -.
DR eggNOG; KOG4262; Eukaryota.
DR InParanoid; Q5RE70; -.
DR OrthoDB; 644334at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070876; C:SOSS complex; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR045334; INTS3.
DR InterPro; IPR019333; INTS3_N.
DR PANTHER; PTHR13587; PTHR13587; 1.
DR Pfam; PF10189; Ints3_N; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1043
FT /note="Integrator complex subunit 3"
FT /id="PRO_0000259536"
FT REGION 977..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q68E01"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68E01"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68E01"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68E01"
SQ SEQUENCE 1043 AA; 118101 MW; 862AA878E32B6DA7 CRC64;
MELQKGKGAA AAAAAASGAA GGGGGGAGAG APGGGRLLLS TSLDAKDELE ERLERCMSIV
TSMTAGVSER EANDALNAYV CKGLPQHEEI CLGLFTLILT EPAQAQKCYR DLALVSRDGM
NIVLNKINQI LMEKYLKLQD TCRTQLVWLV RELVKSGVLG ADGVCMTFMK QIAGGDVTAK
NIWLAESVLD ILTEQREWVL KSSILIAMAV YTYLRLIVDH HGTAQLQALR QKEVDFCISL
LRERFMECLM IGRDLVRLLQ NVARIPEFEL LWKDIIHNPQ ALSPQFTGIL QLLQSRTSRK
FLACRLTPDM ETKLLFMTSR VRFGQQKRYQ DWFQRQYLST PDSQSLRCDL IRYICGVVHP
SNEVLSSDIL PRWAIIGWLL TACTSNVAAS NAKLALFYDW LFFSPDKDSI MNIEPAILVM
HHSMKPHPAI TATLLDFMCR IIPNFYPPLE GHVRQGVFSS LNHIVEKRVL AHLAPLFDNP
KLDKELRAML REKFPEFCSS PSPPVEVKIE EPVSMEMDNH MSDKDESCYD NAEAAFSDDE
EDLNSKGKKR EFRFHPIKET VVEEPVDITP YLDQLDESLR DKVLQLQKGS DTEAQCEVMQ
EIVDQVLEED FDSEQLSVLA SCLQELFKAH FRGEVLPEEI TEESLEESVG KPLYLIFRNL
CQMQEDNSSF SLLLDLLSEL YQKQPKIGYH LLYYLRASKA AAGKMNLYES FAQATQLGDL
HTCLMMDMKA CQEDDVRLLC HLTPSIYTEF PDETLRSGEL LNMIVAVIDS AQLQELVCHV
MMGNLVMFRK DSVLNILIQS LDWETFEQYC AWQLFLAHNI PLETIIPILQ HLKYKEHPEA
LSCLLLQLRR EKPSEEMVKM VLSRPCHPDD QFTTSILRHW CMKHDELLAE RIKSLLIKNN
SLPRKRQSLR SSSSKLAQLT LEQILEHLDN LRLNLTNTKQ NFFSQTPILQ ALQHVQASCD
EAHKMKFSDL FSLAEEYEDS STKPPKSRRK AALSSPRSRK NATQPPNAEE ESGSSSASEE
EDTKPKPTKR KRRGSSAVGS DSD