SPIDR_MOUSE
ID SPIDR_MOUSE Reviewed; 933 AA.
AC Q8BGX7; Q3TCD0; Q5U457; Q6A0B6; Q6IS60; Q811E1; Q8BWD6; Q8R305;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DNA repair-scaffolding protein;
DE AltName: Full=Scaffolding protein involved in DNA repair;
GN Name=Spidr; Synonyms=Kiaa0146;
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] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Mammary gland, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Eye, Mammary tumor, and Olfactory epithelium;
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: Plays a role in DNA double-strand break (DBS) repair via
CC homologous recombination (HR). Serves as a scaffolding protein that
CC helps to promote the recruitment of DNA-processing enzymes like the
CC helicase BLM and recombinase RAD51 to site of DNA damage, and hence
CC contributes to maintain genomic integrity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex, at least composed of BLM, RAD51 and SPIDR;
CC the complex formation is mediated by SPIDR. Interacts (via C-terminal
CC region) with BLM; the interaction is direct. Interacts with RAD51; the
CC interaction is direct. Interacts (via the C-terminal region) with
CC FIGNL1 (via N-terminal one-half region); the interaction is direct (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Together with BLM, is
CC redistributed in discrete nuclear DNA damage-induced foci following
CC hydroxyurea (HU) or camptothecin (CPT) treatment. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BGX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGX7-2; Sequence=VSP_020769;
CC Name=3;
CC IsoId=Q8BGX7-3; Sequence=VSP_020767, VSP_020768;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26877.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35167.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172902; BAD32180.1; ALT_INIT; mRNA.
DR EMBL; AK044836; BAC32113.1; -; mRNA.
DR EMBL; AK052832; BAC35167.1; ALT_FRAME; mRNA.
DR EMBL; AK075871; BAC36018.1; -; mRNA.
DR EMBL; AK170784; BAE42027.1; -; mRNA.
DR EMBL; BC026877; AAH26877.1; ALT_FRAME; mRNA.
DR EMBL; BC046558; AAH46558.1; -; mRNA.
DR EMBL; BC069859; AAH69859.1; -; mRNA.
DR EMBL; BC085258; AAH85258.1; -; mRNA.
DR EMBL; BC089026; AAH89026.1; -; mRNA.
DR CCDS; CCDS27980.1; -. [Q8BGX7-1]
DR RefSeq; NP_666180.2; NM_146068.4. [Q8BGX7-1]
DR AlphaFoldDB; Q8BGX7; -.
DR BioGRID; 230222; 1.
DR STRING; 10090.ENSMUSP00000038820; -.
DR iPTMnet; Q8BGX7; -.
DR PhosphoSitePlus; Q8BGX7; -.
DR EPD; Q8BGX7; -.
DR PaxDb; Q8BGX7; -.
DR PeptideAtlas; Q8BGX7; -.
DR PRIDE; Q8BGX7; -.
DR ProteomicsDB; 258588; -. [Q8BGX7-1]
DR ProteomicsDB; 258589; -. [Q8BGX7-2]
DR ProteomicsDB; 258590; -. [Q8BGX7-3]
DR Antibodypedia; 24233; 35 antibodies from 9 providers.
DR DNASU; 224008; -.
DR Ensembl; ENSMUST00000040248; ENSMUSP00000038820; ENSMUSG00000041974. [Q8BGX7-1]
DR GeneID; 224008; -.
DR KEGG; mmu:224008; -.
DR UCSC; uc007yhy.2; mouse. [Q8BGX7-3]
DR UCSC; uc007yhz.2; mouse. [Q8BGX7-1]
DR CTD; 23514; -.
DR MGI; MGI:1924834; Spidr.
DR VEuPathDB; HostDB:ENSMUSG00000041974; -.
DR eggNOG; ENOG502S0BG; Eukaryota.
DR GeneTree; ENSGT00390000014654; -.
DR HOGENOM; CLU_013509_0_0_1; -.
DR InParanoid; Q8BGX7; -.
DR OMA; WRHQSIS; -.
DR OrthoDB; 326023at2759; -.
DR PhylomeDB; Q8BGX7; -.
DR TreeFam; TF333292; -.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR BioGRID-ORCS; 224008; 5 hits in 107 CRISPR screens.
DR ChiTaRS; Spidr; mouse.
DR PRO; PR:Q8BGX7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BGX7; protein.
DR Bgee; ENSMUSG00000041974; Expressed in granulocyte and 175 other tissues.
DR Genevisible; Q8BGX7; MM.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0070202; P:regulation of establishment of protein localization to chromosome; ISS:UniProtKB.
DR InterPro; IPR028026; DUF4502.
DR InterPro; IPR028032; DUF4503.
DR Pfam; PF14950; DUF4502; 1.
DR Pfam; PF14951; DUF4503; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..933
FT /note="DNA repair-scaffolding protein"
FT /id="PRO_0000251721"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..469
FT /note="Necessary for interaction with RAD51"
FT /evidence="ECO:0000250"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020767"
FT VAR_SEQ 174..196
FT /note="LDISDCDSCASLTSDDRLCEPSE -> MIASVAPHCPSEVPPGLLKPEEK
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020768"
FT VAR_SEQ 827..933
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_020769"
FT CONFLICT 60
FT /note="S -> F (in Ref. 1; BAD32180)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="K -> E (in Ref. 2; BAE42027)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="F -> V (in Ref. 3; AAH85258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 933 AA; 103297 MW; 64EC6762D3332474 CRC64;
MSGARRPGTS KRKRNWHIEH PSFREERSQQ LRRGNFKTVE AADSLSKAWL KCGEGFQDTS
EILSLASEKT GITEKHLELS PKPKTETTSK NASELPNIIW SSSESDFSDE DKTLPALQRD
GRHGPRADRL GDRTISCPED EDIEDELQVI DWEVNSDKED PGGPSECEDD KGTLDISDCD
SCASLTSDDR LCEPSEPIST EILEYSSDSE KEEDPEHSLF IDSESPHKYQ ADFKSDARWC
LVSQTDSEAN SAEPTLTPQK YTVKFPKTPE YSVTKKKLLR GGLAERLQEL QNRKRSAISL
WRHRCVSYQM TPLGRKSGVL TVKILELHEE CSMQVAVCEQ LAGPPITSPP GGLAPRPGAY
LKVLFTRETA DHLMGHPQDI IYIFPPWQKL LIPNGSCSII LNTYFCQKAI AKETVREDLY
SPDISLSRRN ITLAQTFRIK DITDNSSINQ TTYDSLATPG TGWTHGHEKA EQHLIVAAPL
RNSLLDIVES QRAGLWSGVR VQVVVQRVYS LLSRDGARSQ QGHTVGHADA SGAWSCLLVQ
DACGMFGEVF LNSTLWKSRQ LEGKSCSMSG VKVLQKATRG RTPGLFSLID SLWPPVISLT
EPSCGQPSGE TKTYLPPPIF CYIFSAHPTL GQIDAIEDHI SKLYQPPVVR CLKEILQTNE
CSTRCSFYAR VIYQKPQLKN LLAQKEIWLL VTDITLQTQD ERDHSLPKTL PVYIAPSCVL
GPEVVEELAL LVSYNLLFRD AFKDNGQIVC IERTVILPQK PLLCVPSASC DLPSPVTLDE
LSALTPVNSI CSVQGTVVDV DESTAFSWPV CDRCGNGRLE QKPEDGGTFS CGDCSQLVLS
PLQERHLHVF LDCPTRPEST VKVKLLESSI SLLLMSAASE DGSYEVESVL GKEMGPLLCF
VQSITTQQSS CVVTLEEIEL LSTEGATAAQ PPP
