IQIP1_MOUSE
ID IQIP1_MOUSE Reviewed; 559 AA.
AC A0A088MLT8; A8IJC6; A8IJD0; A8IJD3; F6YL02; F8WI70; Q3TI53; Q52KH1; Q6P9Y8;
AC Q9CX07; Q9JLR0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 2.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=IQCJ-SCHIP1 readthrough transcript protein {ECO:0000305};
GN Name=Iqcj-Schip1 {ECO:0000250|UniProtKB:B3KU38};
GN Synonyms=Iqschfp {ECO:0000312|MGI:MGI:5439400},
GN Schip1 {ECO:0000312|EMBL:AIN40496.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AIN40496.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IQCJ-SCHIP1-1), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, INTERACTION WITH ANK3 AND CALMODULIN, MUTAGENESIS OF
RP 53-ILE-GLN-54, AND REGION.
RC STRAIN=FVB/NJ;
RX PubMed=18550753; DOI=10.1523/jneurosci.1044-08.2008;
RA Martin P.M., Carnaud M., Garcia del Cano G., Irondelle M., Irinopoulou T.,
RA Girault J.A., Dargent B., Goutebroze L.;
RT "Schwannomin-interacting protein-1 isoform IQCJ-SCHIP-1 is a late component
RT of nodes of Ranvier and axon initial segments.";
RL J. Neurosci. 28:6111-6117(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IQCJ-SCHIP1-2), FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25953347; DOI=10.1242/dev.119248;
RA Klingler E., Martin P.M., Garcia M., Moreau-Fauvarque C., Falk J.,
RA Chareyre F., Giovannini M., Chedotal A., Girault J.A., Goutebroze L.;
RT "The cytoskeleton-associated protein SCHIP1 is involved in axon guidance,
RT and is required for piriform cortex and anterior commissure development.";
RL Development 142:2026-2036(2015).
RN [3]
RP FUNCTION.
RX PubMed=25950943; DOI=10.1111/jnc.13158;
RA Papandreou M.J., Vacher H., Fache M.P., Klingler E., Rueda-Boroni F.,
RA Ferracci G., Debarnot C., Piperoglou C., Garcia Del Cano G., Goutebroze L.,
RA Dargent B.;
RT "CK2-regulated schwannomin-interacting protein IQCJ-SCHIP-1 association
RT with AnkG contributes to the maintenance of the axon initial segment.";
RL J. Neurochem. 134:527-537(2015).
RN [4]
RP FUNCTION, INTERACTION WITH KCNQ2; KCNQ3 AND SPTBN4, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27979964; DOI=10.1074/jbc.m116.758029;
RA Martin P.M., Cifuentes-Diaz C., Devaux J., Garcia M., Bureau J.,
RA Thomasseau S., Klingler E., Girault J.A., Goutebroze L.;
RT "Schwannomin-interacting protein 1 isoform IQCJ-SCHIP1 is a multipartner
RT ankyrin- and spectrin-binding protein involved in the organization of nodes
RT of Ranvier.";
RL J. Biol. Chem. 292:2441-2456(2017).
CC -!- FUNCTION: May play a role in action potential conduction in myelinated
CC cells through the organization of molecular complexes at nodes of
CC Ranvier and axon initial segments (PubMed:25953347, PubMed:25950943,
CC PubMed:27979964). May also play a role in axon outgrowth and guidance
CC (PubMed:25953347). {ECO:0000269|PubMed:25950943,
CC ECO:0000269|PubMed:25953347, ECO:0000269|PubMed:27979964}.
CC -!- SUBUNIT: Homooligomer (via coiled coil domain) (PubMed:27979964).
CC Interacts (via IQ domain) with calmodulin; the interaction is direct
CC and lost in presence of calcium (PubMed:18550753). Interacts with ANK3
CC (via ANK repeats); required for its localization at axon initial
CC segments (AIS) and nodes of Ranvier (PubMed:18550753). Interacts with
CC SPTBN4 (PubMed:27979964). Interacts with KCNQ2 and KCNQ3
CC (PubMed:27979964). {ECO:0000269|PubMed:18550753,
CC ECO:0000269|PubMed:27979964}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:18550753}. Cytoplasm
CC {ECO:0000250|UniProtKB:B3KU38}. Note=Localizes to the axon initial
CC segments (AIS) and nodes of Ranvier of neurons and is absent from
CC dendrites. {ECO:0000269|PubMed:18550753}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=Iqcj-schip1-1; Synonyms=IQCJ-SCHIP-1
CC {ECO:0000303|PubMed:18550753};
CC IsoId=A0A088MLT8-1; Sequence=Displayed;
CC Name=Iqcj-schip1-2;
CC IsoId=A0A088MLT8-2; Sequence=VSP_059226;
CC Name=Iqcj-1;
CC IsoId=Q8BPW0-1; Sequence=External;
CC Name=Schip1-1; Synonyms=Schip-1a;
CC IsoId=P0DPB4-1, Q3TI53-5;
CC Sequence=External;
CC Name=Schip1-2;
CC IsoId=P0DPB4-2, Q3TI53-1;
CC Sequence=External;
CC Name=Schip1-3;
CC IsoId=P0DPB4-3, Q3TI53-3;
CC Sequence=External;
CC Name=Schip1-4; Synonyms=Schip-1b;
CC IsoId=P0DPB4-4, Q3TI53-6;
CC Sequence=External;
CC -!- DISRUPTION PHENOTYPE: Mice lacking all isoforms encoded by both Schip1
CC and Iqcj-Schip1 are fertile and survive as long as wild-type mice.
CC However, they exhibit mild growth delay associated with ataxia and
CC reduced pain sensitivity. They display decreased thickness of the
CC piriform cortex and partial agenesis of the anterior comissure which
CC could be due to impaired axon elongation and guidance. The morphology
CC of nodes of Ranvier is affected but nerves do not exhibit significant
CC electrophysiological characteristic differences. A reduction in the
CC number of axonal projections in the peripheral nerve system is also
CC observed. {ECO:0000269|PubMed:25953347, ECO:0000269|PubMed:27979964}.
CC -!- MISCELLANEOUS: [Isoform Iqcj-schip1-1]: Based on a naturally occurring
CC readthrough transcript which produces an IQCJ-SCHIP1 fusion protein.
CC {ECO:0000269|PubMed:18550753}.
CC -!- MISCELLANEOUS: [Isoform Iqcj-schip1-2]: Based on a naturally occurring
CC readthrough transcript which produces an IQCJ-SCHIP1 fusion protein.
CC {ECO:0000269|PubMed:25950943}.
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DR EMBL; EU163409; ABW06762.1; -; mRNA.
DR EMBL; KJ941154; AIN40496.1; -; mRNA.
DR CCDS; CCDS79923.1; -. [A0A088MLT8-1]
DR RefSeq; NP_001106890.1; NM_001113419.2. [A0A088MLT8-1]
DR AlphaFoldDB; A0A088MLT8; -.
DR SMR; A0A088MLT8; -.
DR Ensembl; ENSMUST00000182006; ENSMUSP00000138212; ENSMUSG00000102422. [A0A088MLT8-1]
DR GeneID; 100505386; -.
DR KEGG; mmu:100505386; -.
DR UCSC; uc056zsu.1; mouse. [A0A088MLT8-1]
DR CTD; 100505386; -.
DR MGI; MGI:5439400; Iqschfp.
DR VEuPathDB; HostDB:ENSMUSG00000102422; -.
DR GeneTree; ENSGT00390000011127; -.
DR OMA; CGTCVPE; -.
DR OrthoDB; 1290403at2759; -.
DR ChiTaRS; Gm21949; mouse.
DR PRO; PR:A0A088MLT8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A0A088MLT8; protein.
DR Bgee; ENSMUSG00000102422; Expressed in dentate gyrus of hippocampal formation granule cell and 22 other tissues.
DR GO; GO:0043194; C:axon initial segment; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033268; C:node of Ranvier; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0008366; P:axon ensheathment; IMP:UniProtKB.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IBA:GO_Central.
DR InterPro; IPR029362; IQCJ-SCHIP1_N.
DR InterPro; IPR039045; SCHIP_1.
DR InterPro; IPR015649; SCHIP_1_C.
DR PANTHER; PTHR13103; PTHR13103; 1.
DR Pfam; PF15157; IQCJ-SCHIP1; 1.
DR Pfam; PF10148; SCHIP-1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Reference proteome.
FT CHAIN 1..559
FT /note="IQCJ-SCHIP1 readthrough transcript protein"
FT /id="PRO_0000442333"
FT DOMAIN 47..67
FT /note="IQ"
FT REGION 64..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..559
FT /note="Required for interaction with ankyrins"
FT /evidence="ECO:0000269|PubMed:18550753"
FT COILED 496..530
FT /evidence="ECO:0000255"
FT COMPBIAS 69..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 98..325
FT /note="Missing (in isoform Iqcj-schip1-2)"
FT /id="VSP_059226"
FT MUTAGEN 53..54
FT /note="IQ->AA: Loss of interaction with calmodulin."
FT /evidence="ECO:0000269|PubMed:18550753"
SQ SEQUENCE 559 AA; 61917 MW; 72C5FB63AD80036D CRC64;
MRLEELKRLQ NPLEQVDDGK YLLENHQLAM DVENNIENYP LSLQPLESKV KIIQRAWREY
LQRQDPLEKR SPSPPSVSSD KLSSSVSMNT FSDSSTPDYR EDGMDLGSDA GSSSSSRASS
QSNSTKVTPC SECKSSSSPG GSLDLVSALE DYEEPFPVYQ KKVIDEWAPE EDGEEEEEED
DRGYRDDGCP AREPGDVSAR IGSSGSGSRS AATTMPSPMP NGNLHPHDPQ DLRHNGNVVV
AGRPNASRVP RRPIQKTQPP GSRRGGRNRA SGGLCLQPPD GGTRVPEEPP APPMDWEALE
KHLAGLQFRE QEVRNQGQAR TNSTSAQKNE RESIRQKLAL GSFFDDGPGI YTSCSKSGKP
SLSARLQSGM NLQICFVNDS GSDKDSDADD SKTETSLDTP LSPMSKQSSS YSDRDTTEEE
SESLDDMDFL TRQKKLQAEA KMALAMAKPM AKMQVEVEKQ NRKKSPVADL LPHMPHISEC
LMKRSLKPTD LRDMTIGQLQ VIVNDLHSQI ESLNEELVQL LLIRDELHTE QDAMLVDIED
LTRHAESQQK HMAEKMPAK
