INVS_DANRE
ID INVS_DANRE Reviewed; 1021 AA.
AC Q8UVC1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Inversin;
GN Name=invs;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
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).
RN [2]
RP FUNCTION.
RX PubMed=12872123; DOI=10.1038/ng1217;
RA Otto E.A., Schermer B., Obara T., O'Toole J.F., Hiller K.S., Mueller A.M.,
RA Ruf R.G., Hoefele J., Beekmann F., Landau D., Foreman J.W., Goodship J.A.,
RA Strachan T., Kispert A., Wolf M.T., Gagnadoux M.F., Nivet H., Antignac C.,
RA Walz G., Drummond I.A., Benzing T., Hildebrandt F.;
RT "Mutations in INVS encoding inversin cause nephronophthisis type 2, linking
RT renal cystic disease to the function of primary cilia and left-right axis
RT determination.";
RL Nat. Genet. 34:413-420(2003).
RN [3]
RP FUNCTION.
RX PubMed=15852005; DOI=10.1038/ng1552;
RA Simons M., Gloy J., Ganner A., Bullerkotte A., Bashkurov M., Kroenig C.,
RA Schermer B., Benzing T., Cabello O.A., Jenny A., Mlodzik M., Polok B.,
RA Driever W., Obara T., Walz G.;
RT "Inversin, the gene product mutated in nephronophthisis type II, functions
RT as a molecular switch between Wnt signaling pathways.";
RL Nat. Genet. 37:537-543(2005).
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. {ECO:0000269|PubMed:12872123,
CC ECO:0000269|PubMed:15852005}.
CC -!- SUBUNIT: Binds calmodulin via its IQ domains. {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}.
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DR EMBL; AF465261; AAL69977.1; -; mRNA.
DR RefSeq; NP_694502.1; NM_152970.1.
DR AlphaFoldDB; Q8UVC1; -.
DR SMR; Q8UVC1; -.
DR STRING; 7955.ENSDARP00000014904; -.
DR PaxDb; Q8UVC1; -.
DR PRIDE; Q8UVC1; -.
DR GeneID; 245946; -.
DR KEGG; dre:245946; -.
DR CTD; 27130; -.
DR ZFIN; ZDB-GENE-020507-2; invs.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q8UVC1; -.
DR PRO; PR:Q8UVC1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005929; C:cilium; IDA:CACAO.
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:0010171; P:body morphogenesis; IMP:ZFIN.
DR GO; GO:0035844; P:cloaca development; IGI:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR GO; GO:0001736; P:establishment of planar polarity; IGI:ZFIN.
DR GO; GO:0001947; P:heart looping; IGI:ZFIN.
DR GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR GO; GO:0036372; P:opsin transport; IMP:ZFIN.
DR GO; GO:0072116; P:pronephros formation; IGI:ZFIN.
DR GO; GO:0072114; P:pronephros morphogenesis; IGI:ZFIN.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 5.
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; 5.
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; 10.
DR PROSITE; PS50096; IQ; 1.
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..1021
FT /note="Inversin"
FT /id="PRO_0000067019"
FT REPEAT 7..36
FT /note="ANK 1"
FT REPEAT 40..69
FT /note="ANK 2"
FT REPEAT 73..102
FT /note="ANK 3"
FT REPEAT 106..137
FT /note="ANK 4"
FT REPEAT 141..170
FT /note="ANK 5"
FT REPEAT 174..206
FT /note="ANK 6"
FT REPEAT 213..243
FT /note="ANK 7"
FT REPEAT 247..276
FT /note="ANK 8"
FT REPEAT 281..310
FT /note="ANK 9"
FT REPEAT 314..343
FT /note="ANK 10"
FT REPEAT 349..378
FT /note="ANK 11"
FT REPEAT 382..411
FT /note="ANK 12"
FT REPEAT 415..444
FT /note="ANK 13"
FT REPEAT 448..477
FT /note="ANK 14"
FT REPEAT 481..510
FT /note="ANK 15"
FT REPEAT 516..546
FT /note="ANK 16"
FT DOMAIN 548..577
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 869..898
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 579..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 483..491
FT /note="D-box 1"
FT MOTIF 862..870
FT /note="D-box 2"
FT COMPBIAS 579..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 113034 MW; 16816BD3C25EAA9B CRC64;
MAMLLPQNPS QVHAAAVNGD KNTLHKLITE SALRDSEDQF GRTPLMYCVL ADRLDCAEVL
LKAGAGINKT DHSQRTALHL AAQKGNVRFM KLLLSRHADW RLKDLEEMTP LHLASRHSSS
KPLSLLLKHM APGEVDTQDR NKQTALHWSA FYNHPEHVKL LIKHDSNIGI PDSEGKIPLH
WAAHNKHPNA TRTVRCILEA APTESLLNWQ DYEGRTPLHF AVADGNEAVV EVLTSYEGCS
VTAYDNLFRT PLHWAALLGH AKIVHLLLER NKSGMIPSDS QGATPLHYGA QSNFADTVAV
FLKHHSVRDE PDLEGRTAFM WAAGKGSNDV IKIMLDLKKD IDINMTDKYG GTALHAAALS
GHVSTVRLLL EQGGMVDPLD VMKHTPLFRA CEMGHRDVIL TLIKGGARVD LVDIDGHSAL
HWAALGGNAE VCEVLMENGI SPNLQDQAGR TPLQCAAYAG YINCMALLIQ HDADPNIQDK
EGRTALHWSC NNGYLDAVKL LLGCGAFPNH MEHTEERYTP LDYALLGEHQ ELTQFLLEHG
ALSIAAIQDI AASSIQALYK GYKVRRAFRE RKKLLMRHEQ LRKDAAKKRE EERRREAEQQ
LSFAEAGQKQ RVLLAAVGVE KLSLDEAEQR VKDSVAAKGH KHKKSSSAHN SQSRREKPSR
AERRTREPET SDAPSIRSLP PVTPMSTKKC PVTREEVCVR ETFGPDTGIS LNCGSANERR
SPAGSSRPGS AKPVHTGTHV APGHMETTPT PKPRPSTTGA HSKNASQDTP QHNETQTTSK
GNKPISEHKP TGSQPSNNTS VTRQKEKRQE KETHREKDKR SRTEGDKQTV REKQKGTGIE
RAKERLMGRT RKKLAEKEKE KKKDGTCSKN QAAVVIQRAW RRSCVRGRIR KVLCRSLKGV
ESAEATALLI QLLWEWPVLH DHTHRKPSDV QAPPTRIAGK KSSVLQNIYG AAPSKRGTSL
RAAALKTQSQ SQSQVLLDLS LRTHKQLSAV ECVNLVDSVS QAKQFSYHLR PSSGASQSSQ
N
