RIF1_CHICK
ID RIF1_CHICK Reviewed; 2326 AA.
AC E1C2U2; A0A1D5PUQ3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Telomere-associated protein RIF1 {ECO:0000250|UniProtKB:Q5UIP0};
DE AltName: Full=Rap1-interacting factor 1 homolog {ECO:0000250|UniProtKB:Q5UIP0};
GN Name=RIF1 {ECO:0000250|UniProtKB:Q5UIP0};
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=23333306; DOI=10.1016/j.molcel.2013.01.001;
RA Escribano-Diaz C., Orthwein A., Fradet-Turcotte A., Xing M., Young J.T.,
RA Tkac J., Cook M.A., Rosebrock A.P., Munro M., Canny M.D., Xu D.,
RA Durocher D.;
RT "A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and
RT BRCA1-CtIP controls DNA repair pathway choice.";
RL Mol. Cell 49:872-883(2013).
CC -!- FUNCTION: Key regulator of TP53BP1 that plays a key role in the repair
CC of double-strand DNA breaks (DSBs) in response to DNA damage: acts by
CC promoting non-homologous end joining (NHEJ)-mediated repair of DSBs
CC (PubMed:23333306). In response to DNA damage, interacts with ATM-
CC phosphorylated TP53BP1, allowing recruitment to DNA DSBs (By
CC similarity). Once recruited to DSBs, RIF1 and TP53BP1 act by promoting
CC NHEJ-mediated repair of DSBs (PubMed:23333306). In the same time, RIF1
CC and TP53BP1 specifically counteract DSBs resection via homologous
CC recombination (HR) during G1 phase (By similarity).
CC {ECO:0000250|UniProtKB:Q5UIP0, ECO:0000250|UniProtKB:Q6PR54,
CC ECO:0000269|PubMed:23333306}.
CC -!- SUBUNIT: Interacts with TP53BP1 (when phosphorylated by ATM).
CC {ECO:0000250|UniProtKB:Q6PR54}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PR54}.
CC Chromosome {ECO:0000250|UniProtKB:Q6PR54}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q6PR54}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q5UIP0}. Note=Following interaction with
CC TP53BP1, recruited to sites of DNA damage, such as double-strand DNA
CC breaks (DSBs). {ECO:0000250|UniProtKB:Q5UIP0,
CC ECO:0000250|UniProtKB:Q6PR54}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E1C2U2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E1C2U2-2; Sequence=VSP_058928;
CC -!- SIMILARITY: Belongs to the RIF1 family. {ECO:0000305}.
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DR EMBL; AADN04023945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015145353.1; XM_015289867.1. [E1C2U2-2]
DR RefSeq; XP_422162.4; XM_422162.5. [E1C2U2-1]
DR AlphaFoldDB; E1C2U2; -.
DR STRING; 9031.ENSGALP00000036991; -.
DR PaxDb; E1C2U2; -.
DR GeneID; 424316; -.
DR KEGG; gga:424316; -.
DR CTD; 55183; -.
DR VEuPathDB; HostDB:geneid_424316; -.
DR eggNOG; ENOG502QV6C; Eukaryota.
DR HOGENOM; CLU_000989_0_0_1; -.
DR InParanoid; E1C2U2; -.
DR OrthoDB; 10400at2759; -.
DR TreeFam; TF323789; -.
DR PRO; PR:E1C2U2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028566; Rif1.
DR InterPro; IPR022031; Rif1_N.
DR PANTHER; PTHR22928; PTHR22928; 2.
DR Pfam; PF12231; Rif1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cell cycle; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..2326
FT /note="Telomere-associated protein RIF1"
FT /id="PRO_0000439953"
FT REGION 381..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1993..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2002..2036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2102..2127
FT /note="Missing (in isoform 2)"
FT /id="VSP_058928"
SQ SEQUENCE 2326 AA; 254281 MW; FE4A2677A5E16C52 CRC64;
MSGTVSAAAG LRPLLETLQD PAAPAGDLTD AHLSLVNRLS GEEGREFVAA VRKHFPRLCK
VFKAHISSEN SELSNAALQA LGFCVFNSKI TSELSASEVE DLLSTLNSIA VKTSDKNTRT
RALWVISKQT FPSEIIKKEV SSLISTLETI LTKGDVQSMI VEYEALNVVI RLMEQAPAQM
GEEAVRWAKL IIPLVVHSAH KVQLRGATAL EIGMPLLLQK QQEVAAVTEH LMTTKLISEL
QKLFSTKNET YVLKLWPLFV KLLGKTLHRS GSFINSLLQL EELGFRSGSP VVKKIAFIAW
KSLIDNFALN PDILCSAKRL KLLMQPLSSI HVRTEALALT KLEVWWYLLM RLGPQLPANF
EQVCIPLIQS TLSVDSAAAL QGTPSRVPSN PNSANPPQKP GPYPFASPAT PRMNLNSSTA
GLVAIPSIQL LGIEMLLHFL MGPEVLEFAK RNKLVLSLEP LQHPLISSPS FFCKHASTFI
NAVQDGFIAV GKEVPESMLN SIWKDINGHV KAAIESGNKK EKQGSEVLTM LLQALKNIVR
SNSLPVQKIL SLIDITVKEL PPKVLGSPAY QIADMDLLNG TPALFLVQLP FHNNLLEWCV
TDERFFIILE TLMRYVLSGP TSLLAFSESV LCVINQNAKQ VENKEHLWRM WSIVVNPLTD
WINRTNEVNQ GDALEHNFNA VYNALLLPVS HIFPVQEFPQ PTMKSLLRAW SDLYRAFARC
AALVATAEEN LCCEELCAKI ISGLEGETPV MSAMLDGLTH VVAVMVDCIN FAPYGTKYQP
KNRSPQTPTD WSKKKREPLG KLSSLFKLLV MLLDSFHALS SEETCPEPLA SVGHSLIAVL
HNIISHVSLP SMIGTMFAVF SKPLAVFYEK TKLADVPKAY SNLNSKLEKL LAEIILCLQS
HCMGCYDSEL LEQLSPLLCV IFQHKSKQMR KQCANFWNTT FAKAASLTYP EELKPVLSQA
KQKMPLLLPG FESIEIADEQ SGPFSDEAEN SQWDAKLSGM EVNLGQKRDS ILAQTGELKN
EVKDKSDNVQ VTSAKLKLEF SASKPKSDVL LEEEKSVDFV FIPPETKARI LTEHQKEVLR
SKRVGIPAMY NNLDSSQDTT LFSQYTQSQE DSLEKSPLEN AKEDFKNNPQ EENGKSESCI
ADSDGNTGDC KVDNPLEDVK EKSAYHIEKN SNSEEESSRG DRTGIIGEES SVGEALEKSG
TETASKESLV GNENTSAISC SSTSSDVICG TPQPASRRQS FITLEKFDSS ESRPFSPSAL
NSVSEVSQSA PVPDKQGNIN VCKTGRKPGK SGEESRKSSQ SEQISAAKRR LTRRQSKMEQ
QGNQQAKLVT NSEQEKGAQE SFVSNSVENS PESPCSMEDT ERVLTAQPQP VSSPEPDIKK
AEAVMAEIEK VRAFEMDSKE NTPPKTAVSS EQVMGDGSQG PHASLSQKTL RRSSRRRSEN
AEMAAGSQDK EDGYQKKDKR KEDEKALQKK VPQTKEDASQ KQKAVCGKAS EHAIKKESSL
PERSAAEDLG SKEPPAAKGA DEEANRSAGK PEDTLKSDSE GQDCSSDTVS EKKRERPRYH
TRRSSQGLLS SIENAEADGS ETKKESLKKK SGKTKNKSDS LEGKRKDVQP ESQSHGVSSQ
VDESKNLSGM NESELSSEVS TDAALMSAPS DVKNQVLLAG ADEAEGSASS RTSPSTQNVS
VEQSKAGVLP ESFSDPRVSD EVLKGDENKC IEKQSSVEQH SSVQPENVQG ANTSGSDLSS
LQMQDCQHKR SKRVRKAKSC DCCSKRVKQQ TSLSESKSED PRELIEPQAT PVQMAVSTAE
VSGSSNLEES LSITPCAMST PLPPAKESGM LSLERERTGE DNLQGNSGVM KEEAENPAHT
AGEVSDPVVE IKVKEEVDGN DRAEQCVSVS ECASDEPSDS SVAAGDQSEE KAAVEKEEES
QHGEMEEVPE ADGSKPETKQ MDELEGNRDG KEEAENALEE VCITPDNEMR EELLEAEITV
PENVAVGNKD VVVENKSADS PQKPEGLDSF TSVNGSPSGV QARCTWSPSA SPSTSILKRG
VKRHHEDDSL SPANKIRRVS FANPIYQEGL ADDIDRRSPV IRSHSSPSSR SLKILSNIQT
KHITTPTKGF LSPGSRNPKF KSSKKCLMTE MVKESLPSPT ECVYPALAGC KAPVDVILPQ
ITSNICARGL GQLIRAKNIK TVGDLSALTA SEIKTLPIRS PKVSNVKKAL RGYHEQQVKS
RGCEEIGALE DGERTVNSAE DKSPPVDEEK LATDLGEAIA LSSSSPPPAD LLSQMDLLAA
QLTSEDLRSY PGSRLFEMQE KLASMSDCIM KTLRSRWRSP PHDSAE
