SHLD3_MOUSE
ID SHLD3_MOUSE Reviewed; 255 AA.
AC Q9CZV2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Shieldin complex subunit 3 {ECO:0000250|UniProtKB:Q6ZNX1};
DE AltName: Full=REV7-interacting novel NHEJ regulator 1 {ECO:0000250|UniProtKB:Q6ZNX1};
GN Name=Shld3 {ECO:0000250|UniProtKB:Q6ZNX1};
GN Synonyms=Rinn1 {ECO:0000250|UniProtKB:Q6ZNX1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Component of the shieldin complex, which plays an important
CC role in repair of DNA double-stranded breaks (DSBs). During G1 and S
CC phase of the cell cycle, the complex functions downstream of TP53BP1 to
CC promote non-homologous end joining (NHEJ) and suppress DNA end
CC resection. Mediates various NHEJ-dependent processes including
CC immunoglobulin class-switch recombination, and fusion of unprotected
CC telomeres. {ECO:0000250|UniProtKB:Q6ZNX1}.
CC -!- SUBUNIT: Component of the shieldin complex, consisting of SHLD1, SHLD2,
CC SHLD3 and MAD2L2/REV7. Within the complex, SHLD2 forms a scaffold which
CC interacts with a SHLD3-MAD2L2 subcomplex via its N-terminus, and with
CC SHLD1 via its C-terminus. {ECO:0000250|UniProtKB:Q6ZNX1}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q6ZNX1}.
CC Note=Recruited to sites of chromosomal double-stranded breaks during G1
CC and S phase of the cell cycle. {ECO:0000250|UniProtKB:Q6ZNX1}.
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DR EMBL; AK012141; BAB28057.1; -; mRNA.
DR EMBL; GL456167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS88514.1; -.
DR AlphaFoldDB; Q9CZV2; -.
DR SMR; Q9CZV2; -.
DR ComplexPortal; CPX-3483; Shieldin complex.
DR PRIDE; Q9CZV2; -.
DR Antibodypedia; 76730; 2 antibodies from 1 providers.
DR Ensembl; ENSMUST00000133280; ENSMUSP00000159139; ENSMUSG00000118537.
DR UCSC; uc007rsw.1; mouse.
DR MGI; MGI:6194609; Shld3.
DR VEuPathDB; HostDB:ENSMUSG00000118537; -.
DR GeneTree; ENSGT00530000065159; -.
DR OMA; CNATIQR; -.
DR PRO; PR:Q9CZV2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CZV2; protein.
DR Bgee; ENSMUSG00000118537; Expressed in cleaving embryo and 173 other tissues.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0035861; C:site of double-strand break; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0045830; P:positive regulation of isotype switching; IBA:GO_Central.
DR GO; GO:0002208; P:somatic diversification of immunoglobulins involved in immune response; IC:ComplexPortal.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; IC:ComplexPortal.
DR InterPro; IPR039996; Shieldin_RINN1.
DR PANTHER; PTHR41404; PTHR41404; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..255
FT /note="Shieldin complex subunit 3"
FT /id="PRO_0000439347"
FT REGION 33..88
FT /note="Sufficient for interaction with MAD2L2"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNX1"
FT REGION 116..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 58
FT /note="P -> A (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Y -> F (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="F -> C (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..127
FT /note="KNSG -> IISE (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> R (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="L -> V (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="L -> I (in Ref. 1; BAB28057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29675 MW; FD9BA89D6158103D CRC64;
MDSCRMTTEV ILHYRPYEND PKQLAKIAEN VIQDFPTHPL PRFIPWFPYD ESKLPLKPER
LPPVISEEAA ESVKQYLAIS EPGVKSQSYD CTVDLLEFQP SSKLQHFIQS HTVKEQTNAA
HLDKNSGKEK QHKQRSWSVS LASSHCPEKI FPLSRKLQAS LRTLHLHSFH RARWTLEYSV
CNNQTLEDIW TKLNRLIRRD ELPSCNATIQ RQLGQIWVFC DIKCCEYVGN LLKERLSLIG
KIDLFVHKYG VIFSM
