ID   PALB2_MOUSE             Reviewed;        1104 AA.
AC   Q3U0P1; Q6NZG9; Q7TMQ4; Q8CEA9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Partner and localizer of BRCA2;
GN   Name=Palb2;
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 4), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-1086 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
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 MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and FVB/N-3;
RC   TISSUE=Embryonic germ cell, and Mammary tumor;
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 critical role in homologous recombination repair
CC       (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks.
CC       Strongly stimulates the DNA strand-invasion activity of RAD51,
CC       stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4
CC       polypeptide and helps RAD51 to overcome the suppressive effect of
CC       replication protein A (RPA). Functionally cooperates with RAD51AP1 in
CC       promoting of D-loop formation by RAD51. Serves as the molecular
CC       scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is
CC       essential for homologous recombination. Via its WD repeats is proposed
CC       to scaffold a HR complex containing RAD51C and BRCA2 which is thought
CC       to play a role in HR-mediated DNA repair. Essential partner of BRCA2
CC       that promotes the localization and stability of BRCA2. Also enables its
CC       recombinational repair and checkpoint functions of BRCA2. May act by
CC       promoting stable association of BRCA2 with nuclear structures, allowing
CC       BRCA2 to escape the effects of proteasome-mediated degradation. Binds
CC       DNA with high affinity for D loop, which comprises single-stranded,
CC       double-stranded and branched DNA structures. May play a role in the
CC       extension step after strand invasion at replication-dependent DNA
CC       double-strand breaks; together with BRCA2 is involved in both POLH
CC       localization at collapsed replication forks and DNA polymerization
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer; dissociated upon DNA damage thus allowing
CC       association with BRCA1. Oligomerization is essential for its focal
CC       accumulation at DNA breaks. Part of a BRCA complex containing BRCA1,
CC       BRCA2 and PALB2. Interacts with BRCA1 and this interaction is essential
CC       for its function in HRR. Interacts with RAD51AP1 and MORF4L1/MRG15.
CC       Component of the homologous recombination repair (HR) complex composed
CC       of ERCC5/XPG, BRCA2, PALB2, DSS1 and RAD51 (By similarity). Within the
CC       complex, interacts with ERCC5/XPG and BRCA2 (By similarity). Interacts
CC       with BRCA2, RAD51C, RAD51 and XRCC3; the interactions are direct and it
CC       may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC       RAD51C, RAD51 and XRCC3. Interacts with POLH; the interaction is direct
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86YC2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86YC2}.
CC       Note=Colocalizes with BRCA2 in nuclear foci.
CC       {ECO:0000250|UniProtKB:Q86YC2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3U0P1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U0P1-2; Sequence=VSP_020929;
CC       Name=3;
CC         IsoId=Q3U0P1-3; Sequence=VSP_020928;
CC       Name=4;
CC         IsoId=Q3U0P1-4; Sequence=VSP_020930, VSP_020931;
CC   -!- DOMAIN: Interaction with BRCA2 occurs through a hydrophobic pocket at
CC       the crossover between WD repeats 4 and 5. {ECO:0000250}.
CC   -!- DOMAIN: The coiled coil domain mediates self-association.
CC   -!- DOMAIN: The chromatin-association motif (ChAM) mediates association
CC       with chromatin, probably through nucleosome core particles,
CC       independently from binding to D loop, ssDNA or dsDNA structures.
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DR   EMBL; AK028653; BAC26048.1; -; mRNA.
DR   EMBL; AK156701; BAE33811.1; -; mRNA.
DR   EMBL; BC055302; AAH55302.1; -; mRNA.
DR   EMBL; BC066140; AAH66140.1; -; mRNA.
DR   CCDS; CCDS40117.1; -. [Q3U0P1-1]
DR   CCDS; CCDS72035.1; -. [Q3U0P1-2]
DR   CCDS; CCDS80796.1; -. [Q3U0P1-3]
DR   RefSeq; NP_001074707.1; NM_001081238.2. [Q3U0P1-1]
DR   RefSeq; NP_001276771.1; NM_001289842.1.
DR   RefSeq; NP_001276772.1; NM_001289843.1.
DR   RefSeq; NP_001276773.1; NM_001289844.1. [Q3U0P1-2]
DR   RefSeq; NP_001276774.1; NM_001289845.1. [Q3U0P1-3]
DR   PDB; 6E4H; NMR; -; A/B=1-60.
DR   PDB; 7K3S; NMR; -; B=1-60.
DR   PDBsum; 6E4H; -.
DR   PDBsum; 7K3S; -.
DR   AlphaFoldDB; Q3U0P1; -.
DR   SMR; Q3U0P1; -.
DR   BioGRID; 231454; 13.
DR   IntAct; Q3U0P1; 1.
DR   MINT; Q3U0P1; -.
DR   STRING; 10090.ENSMUSP00000095675; -.
DR   iPTMnet; Q3U0P1; -.
DR   PhosphoSitePlus; Q3U0P1; -.
DR   EPD; Q3U0P1; -.
DR   MaxQB; Q3U0P1; -.
DR   PaxDb; 10090-ENSMUSP00000095675; -.
DR   ProteomicsDB; 295454; -. [Q3U0P1-1]
DR   ProteomicsDB; 295455; -. [Q3U0P1-2]
DR   ProteomicsDB; 295456; -. [Q3U0P1-3]
DR   ProteomicsDB; 295457; -. [Q3U0P1-4]
DR   Antibodypedia; 26008; 327 antibodies from 35 providers.
DR   DNASU; 233826; -.
DR   Ensembl; ENSMUST00000063587.13; ENSMUSP00000063514.7; ENSMUSG00000044702.14. [Q3U0P1-3]
DR   Ensembl; ENSMUST00000098068.10; ENSMUSP00000095675.4; ENSMUSG00000044702.14. [Q3U0P1-1]
DR   Ensembl; ENSMUST00000106469.8; ENSMUSP00000102077.2; ENSMUSG00000044702.14. [Q3U0P1-2]
DR   GeneID; 233826; -.
DR   KEGG; mmu:233826; -.
DR   UCSC; uc009joj.2; mouse. [Q3U0P1-1]
DR   UCSC; uc009jom.1; mouse. [Q3U0P1-4]
DR   UCSC; uc012ftg.2; mouse. [Q3U0P1-2]
DR   UCSC; uc012fth.2; mouse. [Q3U0P1-3]
DR   AGR; MGI:3040695; -.
DR   CTD; 79728; -.
DR   MGI; MGI:3040695; Palb2.
DR   VEuPathDB; HostDB:ENSMUSG00000044702; -.
DR   eggNOG; ENOG502QRAP; Eukaryota.
DR   GeneTree; ENSGT00390000014423; -.
DR   HOGENOM; CLU_008217_1_0_1; -.
DR   InParanoid; Q3U0P1; -.
DR   OMA; GHCQKED; -.
DR   OrthoDB; 5404130at2759; -.
DR   PhylomeDB; Q3U0P1; -.
DR   TreeFam; TF351544; -.
DR   Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR   BioGRID-ORCS; 233826; 28 hits in 117 CRISPR screens.
DR   ChiTaRS; Palb2; mouse.
DR   PRO; PR:Q3U0P1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3U0P1; Protein.
DR   Bgee; ENSMUSG00000044702; Expressed in animal zygote and 151 other cell types or tissues.
DR   ExpressionAtlas; Q3U0P1; baseline and differential.
DR   GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR042417; PALB2.
DR   InterPro; IPR031920; PALB2_WD40.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR14662; PARTNER AND LOCALIZER OF BRCA2; 1.
DR   PANTHER; PTHR14662:SF2; PARTNER AND LOCALIZER OF BRCA2; 1.
DR   Pfam; PF16756; PALB2_WD40; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   Genevisible; Q3U0P1; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Tumor suppressor; WD repeat.
FT   CHAIN           1..1104
FT                   /note="Partner and localizer of BRCA2"
FT                   /id="PRO_0000252392"
FT   REPEAT          772..833
FT                   /note="WD 1"
FT   REPEAT          835..879
FT                   /note="WD 2"
FT   REPEAT          880..927
FT                   /note="WD 3"
FT   REPEAT          928..970
FT                   /note="WD 4"
FT   REPEAT          976..1027
FT                   /note="WD 5"
FT   REPEAT          1033..1071
FT                   /note="WD 6"
FT   REPEAT          1073..1104
FT                   /note="WD 7"
FT   REGION          1..308
FT                   /note="Interaction with BRCA1"
FT                   /evidence="ECO:0000250"
FT   REGION          1..195
FT                   /note="Interaction with RAD51"
FT                   /evidence="ECO:0000250"
FT   REGION          1..157
FT                   /note="Required for its oligomerization and is important
FT                   for its focal concentration at DNA damage sites"
FT                   /evidence="ECO:0000250"
FT   REGION          39..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..424
FT                   /note="ChAM (Chromatin-association motif); required for
FT                   chromatin association, mediates nucleosome association"
FT                   /evidence="ECO:0000250"
FT   REGION          417..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..1104
FT                   /note="Required for interaction with POLH and POLH DNA
FT                   synthesis stimulation"
FT                   /evidence="ECO:0000250"
FT   REGION          771..1104
FT                   /note="Interaction with RAD51 and BRCA2"
FT                   /evidence="ECO:0000250"
FT   REGION          771..1104
FT                   /note="Interaction with RAD51, BRCA2 and POLH"
FT                   /evidence="ECO:0000250"
FT   COILED          9..48
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        58..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YC2"
FT   VAR_SEQ         36..755
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020928"
FT   VAR_SEQ         170..532
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020929"
FT   VAR_SEQ         533..544
FT                   /note="DFELPDEDFGLL -> GKSRRRVRLRLM (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020930"
FT   VAR_SEQ         545..1104
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020931"
FT   HELIX           11..39
FT                   /evidence="ECO:0007829|PDB:6E4H"
SQ   SEQUENCE   1104 AA;  119097 MW;  D8E027609707D03D CRC64;
     MEELSGKPLS YAEKEKLKEK LAFLKKEYSR TLARLQRAKR AEKAKNSKKA IEDGVPQPEA
     SSQLSHSESI NKGFPCDTLQ SNHLDEETGE NISQILDVEP QSFNCKQGKE VLHTPRAGDI
     QGQLLHSTSS PDGKKEQNTL PGTTKTPWEK SSVSQEKEDY FDTNSLALLG KHRKGQESIS
     RKNSRTPVSE KTHLLSLRSQ IPDPPALVTG IGEGILIPPS GKSERGIDTL VRGNTVSAEA
     AVPSCTASNS NHSQHLEHTP PKSGCKITTQ GPASSTNLVA QDQKMTIFTV NSVVYKAVRA
     HGQLPGSPNS CSVNDLTHSN LPANSTPNSK SLKSPSNTVD ERNEPLQEDE ILGPSKNFNL
     AAVSPPSTES QIHSCTMLEG LLFPAEYYVR TTRRMSDCQR KIALEAVIQS HLGVKKKELK
     KKTKATKAVV LSSEDTDQSE SGMLDTSTGQ SSSGSLSQKL LSPAEVSSPP GPAGKATTPP
     PGRGHRGKRK SARTSTLGHC QLLFPPCAAL AVNRSKGKFT KHKCQNRGVV IHDFELPDED
     FGLLKLEKLK SCSEKLIESP DSKNCGERLP REGNHAALEE LQRDSETEGL EEELTVPPGE
     AYRPGPTLRR QPGSKDLSSS IVLFTPADTA APNDSGRPPP SLCSPAFPIL GMTPALGSQA
     AGETLSTEAA QPCSTSQPPL LGDTNSLVNN SKQCNSSACS PKPDTNLQAS GRQGQPACDS
     DSGPQATPLP VESFTFRENQ LCGNACLELH EHSTEQTETA DRPACDNLNP GNLQLVSELK
     NPSSSCSVDV SAMWWERAGA KEPCIVTACE DVVSLWKPLN SLQWEKVHTW HFTEVPVLQI
     VPVPDVYNLI CVALGSLEIR EIRALLCSSG DDSEKQVLLK SGDIKAMLGL TKRRLVSSTG
     TFCNQQIQIM TFADDGSSKD EQLLMPPDET VLTFAEVQGT QEALLGTTTV NSIVIWNLKT
     GQLLKKMHID DSYQASVCHG AYSEKGLLFV VVSQPCAKES QALGSPVFQL LVINPKTAQS
     VGVLLCSLPQ GQAGRFLEGD VKDHVAAAVL TSGTIAIWDL LLGHCTALLP PVSDQSWSLV
     KWSGTDSHLL AGQKDGNIFI YRYF
//