INVSB_XENLA
ID INVSB_XENLA Reviewed; 1002 AA.
AC Q71S21;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Inversin-B;
GN Name=invs-b; Synonyms=inv2, invs-2;
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], AND INTERACTION WITH CALMODULIN.
RA Yasuhiko Y., Shiokawa K., Yokoyama T.;
RT "The inv RNA randomizes left-right asymmetry in Xenopus embryos through
RT binding to calmodulin.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for normal renal development and establishment of
CC left-right axis. Probably acts as a molecular switch between different
CC Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting
CC cytoplasmic disheveled for degradation by the ubiquitin-proteasome.
CC This suggests that it is required in renal development to oppose the
CC repression of terminal differentiation of tubular epithelial cells by
CC Wnt signaling. Plays a central role in convergent extension movements
CC in gastrulating embryos, a processus regulated by Wnt signaling (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with apc2 (By similarity). Binds calmodulin.
CC {ECO:0000250, ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associates with the cytoskeleton. {ECO:0000250}.
CC -!- DOMAIN: The D-box (destruction box) mediate the interaction with APC
CC proteins, and may act as a recognition signal for degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000250}.
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DR EMBL; AF321229; AAQ14848.1; -; mRNA.
DR RefSeq; NP_001083066.1; NM_001089597.1.
DR AlphaFoldDB; Q71S21; -.
DR SMR; Q71S21; -.
DR PRIDE; Q71S21; -.
DR GeneID; 398717; -.
DR KEGG; xla:398717; -.
DR CTD; 398717; -.
DR Xenbase; XB-GENE-6255451; invs.L.
DR OrthoDB; 316949at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 398717; Expressed in blastula and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00248; ANK; 16.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 13.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW ANK repeat; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Developmental protein; Reference proteome; Repeat; Wnt signaling pathway.
FT CHAIN 1..1002
FT /note="Inversin-B"
FT /id="PRO_0000067021"
FT REPEAT 9..39
FT /note="ANK 1"
FT REPEAT 43..72
FT /note="ANK 2"
FT REPEAT 76..105
FT /note="ANK 3"
FT REPEAT 109..140
FT /note="ANK 4"
FT REPEAT 144..173
FT /note="ANK 5"
FT REPEAT 177..209
FT /note="ANK 6"
FT REPEAT 216..246
FT /note="ANK 7"
FT REPEAT 250..279
FT /note="ANK 8"
FT REPEAT 284..313
FT /note="ANK 9"
FT REPEAT 317..346
FT /note="ANK 10"
FT REPEAT 352..381
FT /note="ANK 11"
FT REPEAT 385..414
FT /note="ANK 12"
FT REPEAT 418..447
FT /note="ANK 13"
FT REPEAT 451..480
FT /note="ANK 14"
FT REPEAT 484..513
FT /note="ANK 15"
FT REPEAT 519..549
FT /note="ANK 16"
FT DOMAIN 551..580
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 966..995
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 586..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 486..494
FT /note="D-box 1"
FT MOTIF 959..967
FT /note="D-box 2"
FT COMPBIAS 586..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 111909 MW; 39183A2B1B3640AC CRC64;
MSNPPQGSSL ASPIQAAAVT GDKTTLLRLI ASSPQVIDQE DQLGRTPLMY SVLGDRRSCA
EALLKHGAKV NRPDRSGRTA LHLAAQTGNH RLLKLLLSRK ADCTHRDLCD ITALHLSTRH
QDTQCLVLLL KYTPPGQVDA QDQRKQTALH WSAYYNRPQH VRLLVRHGSN IGIPDTEGKI
PLHWAAGHKD PEAALTVRCL FEAAPTESLL NWQDYEGRTP LHLAVGDGNQ EVVRLLTSYR
GCNVAPYDNL FRTPLHWAAL LGHTPIAHLL LERNNSPNIP SDSQGATPLH YAAQGNCPDT
VRVLLSHPSV RDEADLEGRT ALMWAAGKGS DEVVRTMLEL NPKLEVNRTD KYGGTALHAA
SLSGQITTVR ILLENRAQAD AVDVMKHTPL FRACEMGHRE VIATLIKGGA KVHLVDKDGR
SPLHWAALGG NANVCQILIE NNINPDAQDY EGRTPLQCAA YGGYIGCMEV LMENKADPNI
QDKNGRTALH WSCNNGYLDA VKLLLGYNAF PNQMENTEER YTPLDYALLG GHQEVIQFML
EHGALSIAAI QDIAAFKIQA VYKGHKVRRA FQERKNLLMK HEQLRKGAAA KKREGENRQK
VKVGQTKGKQ KDADSMERQN KSNEQIIKNE VVHEWQGEAS GNAEDRKGKH REENLETNHL
QHSKHMAKNQ RITAQIQSSP SEHEHTNSIQ IRTSPSGTSN TQSSPLGNEI PKNMYWDDNP
SQKHTQTRRT SRHQMESPDV VVHRIEDLIQ KESRRKSHRE ERKGSHRQRQ SSDYRLHTSE
KEASDSAIHR EEEGKKKETK KGRRTVAVTP KIEACCKGGC GKLSQSEKVS LGIGIQGRVD
CITSPEPCET PSRVCRERKT ISAKTGQRPL TETHKPPGKA CRSSSALKSS LPSHIKQTAI
DSKCLDSTLS YIGFGEAIKP LFPMGILREG SFFSKWQNID IELIPVQARL QLVEREKARK
QLFQRKNHAA TVIQKAWRTY WVRKSSCKTR HSRSQNNPPA MV
