INVS_CHICK
ID INVS_CHICK Reviewed; 1106 AA.
AC Q8UVC3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Inversin;
GN Name=INVS;
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 [MRNA].
RX PubMed=11941489; DOI=10.1007/s00439-002-0696-4;
RA Morgan D., Goodship J., Essner J.J., Vogan K.J., Turnpenny L., Yost H.J.,
RA Tabin C.J., Strachan T.;
RT "The left-right determinant inversin has highly conserved ankyrin repeat
RT and IQ domains and interacts with calmodulin.";
RL Hum. Genet. 110:377-384(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds calmodulin via its IQ domains. Interacts with APC2 (By
CC similarity). {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL69975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF465207; AAL69975.1; ALT_INIT; mRNA.
DR RefSeq; NP_989882.1; NM_204551.1.
DR AlphaFoldDB; Q8UVC3; -.
DR SMR; Q8UVC3; -.
DR STRING; 9031.ENSGALP00000030342; -.
DR PaxDb; Q8UVC3; -.
DR PRIDE; Q8UVC3; -.
DR GeneID; 395234; -.
DR KEGG; gga:395234; -.
DR CTD; 27130; -.
DR VEuPathDB; HostDB:geneid_395234; -.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q8UVC3; -.
DR OrthoDB; 316949at2759; -.
DR PhylomeDB; Q8UVC3; -.
DR PRO; PR:Q8UVC3; -.
DR Proteomes; UP000000539; Unplaced.
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; PF12796; Ank_2; 6.
DR Pfam; PF13637; Ank_4; 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; 11.
DR PROSITE; PS50096; IQ; 2.
PE 2: Evidence at transcript level;
KW ANK repeat; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Developmental protein; Reference proteome; Repeat; Wnt signaling pathway.
FT CHAIN 1..1106
FT /note="Inversin"
FT /id="PRO_0000067018"
FT REPEAT 13..42
FT /note="ANK 1"
FT REPEAT 47..76
FT /note="ANK 2"
FT REPEAT 80..110
FT /note="ANK 3"
FT REPEAT 113..144
FT /note="ANK 4"
FT REPEAT 148..177
FT /note="ANK 5"
FT REPEAT 181..213
FT /note="ANK 6"
FT REPEAT 220..250
FT /note="ANK 7"
FT REPEAT 254..285
FT /note="ANK 8"
FT REPEAT 288..317
FT /note="ANK 9"
FT REPEAT 321..350
FT /note="ANK 10"
FT REPEAT 356..385
FT /note="ANK 11"
FT REPEAT 389..418
FT /note="ANK 12"
FT REPEAT 422..451
FT /note="ANK 13"
FT REPEAT 455..484
FT /note="ANK 14"
FT REPEAT 488..517
FT /note="ANK 15"
FT REPEAT 523..553
FT /note="ANK 16"
FT DOMAIN 555..584
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 951..980
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 589..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..498
FT /note="D-box 1"
FT MOTIF 944..952
FT /note="D-box 2"
FT COMPBIAS 589..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 122553 MW; BFD88648DB5F2032 CRC64;
MNISANCLFS GSSLASEVHA AAVNGDKSTL LKLIAGNSEL KDKEDQFGRT PLMYCVLADR
VDCAEALLKA GADVNRADRS RRTALHLAAQ KGNYRFMKLL LARRGNWMQK DLEGMTPLHL
TTRHKSPKCL ALLLKHMAPG EVDTQDRNKQ TALHWSAYYN NPEHVKLLIK HDSNIGIPDI
EGKIPLHWAA NNKDPSAIHT VKCILEAAPT ESLLNWQDYE GRTPLHFAVA DGNVAVVDVL
TSYEGCNVTS YDNLFRTPLH WAALLGHAQI VHLLLERNKF GTIPSDSQGA TPLHYAAQSN
FAETVEVFLK HPSVKDDSDL EGRTSFMWAA GKGSDNVIRT MLDLKLDIDI NMTDKYAGTA
LHAAALSGHV STVKLLLERN AQVDALDVMK HTPLFRACEM GHKEVIQTLI KGGARVDLVD
QDGHSPLHWA ALGGNADVCQ ILIENKINPN VQDYAGRTPL QCAAYGGYIN CMVVLLENNA
DPNIQDKEGR TALHWLCNNG YLDAIKLLLG FDAFPNHMEN SEERYTPLDY ALLGEHHEVI
QFMLEHGALS IAAIQDIAAF KIQAVYKGYK VRKAFQERKN LLMKHEQLRK DAAAKKREEE
SKRKEASLQK GMQNMEQNKF QVQLSTAVRE KTASTLQLSN KQTDLQNKRP LSVSASQIQL
GRNSRGSPKA CRSKGSPKES CLSSELQSEG HNIRQELLRK HIKSKPSCVH FHCGKVKEVT
KVEAKHQVAA ATELNGEKHK EHAVEANGTS AHGNRRHASA CGTAGAGEKT RDQSLSSSGN
RGHCEGTSVV VCNVSCAGGI ARNSKRCEAV PKSKRHQQKS RHKEVNYERC SPAGSSRPGS
AKVVFVNTRN ATVCAIEHAN NVGNHELAKK TSPLLSTETE STGTGPRNPA ACSALDDSLN
LEKTGEVGSR SAGDQLCSVA WQSTNIELIP LEIRMQIIEK ERTRKELFRK KNYAATVIQR
TWRSYRLRQE LSQLLSAKRQ RKEDEDKWRQ ETAAFLIQVA WKKQLNHSPQ KSVPSCKSLK
SVNKTSSAIK TSKQSILKQI YGRSQEGRVY QPARPPSKLK LSDVQLVSAN NLQYVNLLEN
VGKSKQFSYN MRPSTAAKSK STRLEH
