R51A1_CHICK
ID R51A1_CHICK Reviewed; 253 AA.
AC A0A3Q2UEI8; E1C6H8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=RAD51-associated protein 1 {ECO:0000305};
DE Short=GgRAD51AP1 {ECO:0000303|PubMed:25288561};
GN Name=RAD51AP1 {ECO:0000303|PubMed:25288561};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION.
RX PubMed=25288561; DOI=10.1016/j.dnarep.2014.09.007;
RA Parplys A.C., Kratz K., Speed M.C., Leung S.G., Schild D., Wiese C.;
RT "RAD51AP1-deficiency in vertebrate cells impairs DNA replication.";
RL DNA Repair 24:87-97(2014).
CC -!- FUNCTION: Structure-specific DNA-binding protein involved in DNA repair
CC by promoting RAD51-mediated homologous recombination (By similarity).
CC Acts by stimulating D-Loop formation by RAD51: specifically enhances
CC joint molecule formation through its structure-specific DNA interaction
CC and its interaction with RAD51 (By similarity). Binds single-stranded
CC DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures,
CC such as D-loop structures: has a strong preference for branched-DNA
CC structures that are obligatory intermediates during joint molecule
CC formation (By similarity). Involved in mitotic recombination-dependent
CC replication fork processing (PubMed:25288561). Also involved in meiosis
CC by promoting DMC1-mediated homologous meiotic recombination (By
CC similarity). {ECO:0000250|UniProtKB:Q96B01,
CC ECO:0000269|PubMed:25288561}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96B01}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q96B01}.
CC Nucleus {ECO:0000250|UniProtKB:Q96B01}. Note=Colocalizes with RAD51 to
CC multiple nuclear foci. Colocalizes with DMC1 on meiotic chromatin.
CC {ECO:0000250|UniProtKB:Q8C551}.
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DR EMBL; AADN05000818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A3Q2UEI8; -.
DR STRING; 9031.ENSGALP00000027892; -.
DR Ensembl; ENSGALT00000104609; ENSGALP00000072778; ENSGALG00000017290.
DR VEuPathDB; HostDB:geneid_419042; -.
DR GeneTree; ENSGT00990000212409; -.
DR HOGENOM; CLU_067355_1_0_1; -.
DR OrthoDB; 1109145at2759; -.
DR TreeFam; TF335955; -.
DR Reactome; R-GGA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-GGA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-GGA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017290; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; A0A3Q2UEI8; baseline and differential.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0062037; F:D-loop DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000217; F:DNA secondary structure binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; ISS:UniProtKB.
DR InterPro; IPR026632; RAD51-assoc_prot_1.
DR PANTHER; PTHR15361:SF4; PTHR15361:SF4; 2.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..253
FT /note="RAD51-associated protein 1"
FT /id="PRO_0000451602"
FT REGION 32..51
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT REGION 33..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..241
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q96B01"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 28817 MW; C7E6D23E14D943CB CRC64;
MARMVRRNRK IVNYSEFGDF EDGDEDFACI AAPLTKKSRT QPKEPKKENK KKQKTQKEFT
SSQKQSPIGR TSLDDSFCER DLNVTLALSI KEKSANILEV QNSKEQGQVL DDDIPRNGCR
QWTAASKAFS HQKLLTIDSC DREHVTDSEP VTIPDEESEE DSDYREGNDE DCAMEKMKIN
GMKKKIKRQT RKEKKTPKSE NNTTVMELKS EQTQKMMSTS SEPVGRPLYT SSPVTNKKPK
WVPPGRACAV SFL
