PAXI1_XENLA
ID PAXI1_XENLA Reviewed; 1256 AA.
AC Q90WJ3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=PAX-interacting protein 1;
DE AltName: Full=PAX transactivation activation domain-interacting protein;
DE AltName: Full=SMAD wing for transcriptional activation;
DE Short=Protein Swift;
GN Name=paxip1; ORFNames=K14;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SMAD2, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=11359898; DOI=10.1128/mcb.21.12.3901-3912.2001;
RA Shimizu K., Bourillot P.-Y., Nielsen S.J., Zorn A.M., Gurdon J.B.;
RT "Swift is a novel BRCT domain coactivator of Smad2 in transforming growth
RT factor beta signaling.";
RL Mol. Cell. Biol. 21:3901-3912(2001).
RN [2]
RP FUNCTION IN DNA REPAIR.
RX PubMed=18353733; DOI=10.1016/j.dnarep.2008.02.001;
RA Gohler T., Munoz I.M., Rouse J., Blow J.J.;
RT "PTIP/Swift is required for efficient PCNA ubiquitination in response to
RT DNA damage.";
RL DNA Repair 7:775-787(2008).
CC -!- FUNCTION: Involved in DNA damage response. Promotes ubiquitination of
CC PCNA following UV irradiation and may regulate recruitment of
CC polymerase eta and rad51 to chromatin after DNA damage. May function as
CC transcriptional cofactor in TGF beta signaling. Accentuates smad2-
CC dependent transcription. {ECO:0000269|PubMed:11359898,
CC ECO:0000269|PubMed:18353733}.
CC -!- SUBUNIT: Interacts with smad2 via its last three BRCT domain-containing
CC regions in an activin signal-dependent manner.
CC {ECO:0000269|PubMed:11359898}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed, expression declines during
CC gastrulation and continues at a lower level until late stages.
CC Ubiquitously expressed at gastrula stage. Later in development, becomes
CC enriched in the head and brain. {ECO:0000269|PubMed:11359898}.
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DR EMBL; AF172855; AAK55123.1; -; mRNA.
DR AlphaFoldDB; Q90WJ3; -.
DR SMR; Q90WJ3; -.
DR PRIDE; Q90WJ3; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0044666; C:MLL3/4 complex; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10190; -; 6.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR037886; Paxip1.
DR PANTHER; PTHR23196:SF31; PTHR23196:SF31; 3.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 6.
DR SUPFAM; SSF52113; SSF52113; 5.
DR PROSITE; PS50172; BRCT; 4.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1256
FT /note="PAX-interacting protein 1"
FT /id="PRO_0000296265"
FT DOMAIN 8..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 94..183
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 794..883
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 890..978
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1053..1134
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1155..1196
FT /note="BRCT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 184..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 857..874
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 189..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 144187 MW; E7795B12C1A42DE1 CRC64;
MAEDEVKVPE DMFKDVKFYP VGDLDPKVVQ MLKAGKAKEV SYNALATHII AEDGDNPEVG
EAREVFDLPV VKPSWVILSV RCGVRLPENG FSPESGQIFF GVTACLSQVS PDDRNSLWAL
TTFYGGDCQL SLNKKCTHLI VPEPKGNKYE YAFQRGSIKI VTPDWVLDSV SEKTKKDEAL
YHPRLIVYEE EEEEEEEEAE NEEQESQNGS DEDKYSSKSS PVTSRDGSPV HNRESSPKRS
SSDKIKSELM FDDSSDSSPE KQERNLNWTP AEVPQMSTAK RQLHQGAPGS ERPDMMAFRS
PAVRTLRNIT NSADVQQVNR PSNVAHILQT LSASTKSLEQ RVNHPQQGHP NAVLFGQVKP
LTSEAQHLIQ QSHQPHHQQQ QQQQNHPIVQ LQPQQLLQLQ QQQQQITQQV FPQHQFPQVN
QQHPFTQLQF PQQQLHPQQQ LHRPQQQTIQ HFQQQHALQQ QLHQLQQQHL QPKPQTLQQN
MQQQNLQQPN LQQILQHQQT IQQTPSQQQA LQPAIQQQQM LQPNIQQQQT LQSNLQQQTL
QPIIQQQQGL QQQNLQQSLQ QIQQQMQHLT PQQKQQIQQQ QQQMLQKQQL QSQSLQQQQM
QTHVLQQQQI QTQALQQQQQ IQNQALQQPQ QNQVQTHALQ QHRLQSQTLQ QQHHVQGQTV
QQQTHQLQTQ TLQQQHQIQT LQIPHQIPAP NQQHQIPPQM LQQQTLQLQQ QMQPQIQQPQ
MQSGVQQQSS LQPQQMQQHK HNLQQVQHQL QQLQQQRMQQ RQMALPQQIA NQQPPQPHQL
HGHDPSVEIP EDFFLLGCVF AIADYPEQMP DKQLLATWKR IIQTHGGTVD AALSSRCTHL
LCESQVSSMY AQALKERKRC ITAHWLNAVL KKKKMVPPYR ALHFPVAFPP GGKPCSQHII
SVTGFVDSDR DDLKLMGYLA GAKYTGYLCR SNTVLICKEP SGLKYEKAKE WRIPCVNALW
LCDILLGNLE ALRQIQHSRY TVFNLQDPLA PSPHLVTDDL LDAWRMPLKV SSEVLMSIRM
PLKPKQNEPA VQPKRPRIED IPPPTKKLSP DQTPHVIFTG FDPLQVQQYI KKLYILGGEV
ADTAQKCTHL VANKVTRTVK FLTAISVAKH IVTPEWLDES FKSQKFAEEQ NYILRDAEAE
VLFCFSLEES LKKAHVNPLF KGKYFYITPG ICPSLSTMKA IVECAGGKIL TKQPSFRKIM
EHKQNKRLAE IILISCENDL HLCREYFAGS VDVHNAEFVL TGVLTQALDY ESYKFT
