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LRRF2_XENLA
ID   LRRF2_XENLA             Reviewed;         729 AA.
AC   Q6GNW0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE            Short=LRR FLII-interacting protein 2;
DE            Short=xLRRFIP2;
GN   Name=lrrfip2;
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] (ISOFORM 1), FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=15677333; DOI=10.1073/pnas.0409472102;
RA   Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S.,
RA   Schultz P.G.;
RT   "Identification of the Wnt signaling activator leucine-rich repeat in
RT   Flightless interaction protein 2 by a genome-wide functional analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Tail bud;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as activator of the canonical Wnt signaling
CC       pathway upstream of ctnnb1/beta-catenin. Might be required for dorsal
CC       axis formation. {ECO:0000269|PubMed:15677333}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6GNW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6GNW0-2; Sequence=VSP_035798, VSP_035799, VSP_035800;
CC   -!- DEVELOPMENTAL STAGE: A shorter isoform, which probably corresponds to
CC       isoform 2, is expressed both maternally and zygotically throughout
CC       early development. Isoform 1 is expressed only after the mid-blastula
CC       transition (MBT), becoming readily detectable after stage 14.
CC       {ECO:0000269|PubMed:15677333}.
CC   -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR   EMBL; BC073391; AAH73391.1; -; mRNA.
DR   RefSeq; NP_001085821.1; NM_001092352.1.
DR   AlphaFoldDB; Q6GNW0; -.
DR   SMR; Q6GNW0; -.
DR   DNASU; 444248; -.
DR   GeneID; 444248; -.
DR   KEGG; xla:444248; -.
DR   CTD; 444248; -.
DR   Xenbase; XB-GENE-950915; lrrfip2.L.
DR   OrthoDB; 1434475at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444248; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0030275; F:LRR domain binding; ISS:UniProtKB.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR   InterPro; IPR019139; LRRFIP1/2.
DR   PANTHER; PTHR19212; PTHR19212; 1.
DR   Pfam; PF09738; LRRFIP; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Developmental protein;
KW   Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..729
FT                   /note="Leucine-rich repeat flightless-interacting protein
FT                   2"
FT                   /id="PRO_0000245249"
FT   REGION          80..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          27..69
FT                   /evidence="ECO:0000255"
FT   COILED          357..531
FT                   /evidence="ECO:0000255"
FT   COILED          574..722
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        92..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         60..294
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_035798"
FT   VAR_SEQ         351..374
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_035799"
FT   VAR_SEQ         465..529
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_035800"
FT   CONFLICT        599
FT                   /note="K -> L (in Ref. 2; AAH73391)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   729 AA;  83500 MW;  9EC5FBC067BB1826 CRC64;
     MGTPGSGRKR TQIKDRFSAE DEALSHIARE AEARLAAKRA ARAEARDIRM RELERQQKEL
     THRYHDKKWG QIQKWMEDSD HARHLQRSSH RHSMASSRVT PNHRSSSVDV SGSHRGRESI
     SRRRDSVYNT LKDSSRRTSN SYSNSYDVKN TTSSSHRDLL SGLYHDQRKY SSLKYNKPIS
     THHIRSSSLY SEPLATKRTY GTSLYKDGLY NASSSRAPSE YSCYSSRASS ARSSPVCSDD
     EGSVSYSSCR GRRDSVSSDF SDQSESAADY FSRSNRRGSI VSDVDDVSIP DLNSLDEKTD
     KQFTTENYSR PSSRNATSGI PGTFTPLSGS SSRRGSGDAS CSLDPDASLS ELRDIYDLKD
     QIQDVEGRYM QGLKELRESL AEVEEKYKKA MVSNAQLDNE KSNLVYHVDT LKDVIEEMEE
     QMAEYHRENE EKSKELERQK HNCSILQHKL DEHKEGIRQR DEFIEENQRM QQRVDSLVRE
     VYDLQETINW KDKKIGALER QKEYFDCIKN ERDELRDELT AVKEKVKIGE KHGLVIIPDG
     TPNGDINHEP MVGAITVVSQ EAAHVLESAG EGPLDVRLRK LAEEKEELVA QIRKLKLQKD
     DERQKSAKNN STTTDPTGLE NGSDLQLIEM QRDANRQISE YKFRLSKSEQ DITTLEQNVM
     RLEGQVVRYK SAAENAEKVE DELKAEKRRL QRELRTALDK MEEMEMTNNH LVKRLEKMKA
     NRTALLSQQ
 
 
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