SCHI1_MOUSE
ID SCHI1_MOUSE Reviewed; 484 AA.
AC P0DPB4; 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 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Schwannomin-interacting protein 1 {ECO:0000303|PubMed:18550753};
DE Short=SCHIP-1 {ECO:0000303|PubMed:18550753};
GN Name=Schip1 {ECO:0000312|MGI:MGI:1353557};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SCHIP1-1 AND SCHIP1-4), AND
RP ALTERNATIVE SPLICING.
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 [LARGE SCALE MRNA] (ISOFORMS SCHIP1-2 AND SCHIP1-3).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Head, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SCHIP1-2 AND SCHIP1-3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-484 (ISOFORMS SCHIP1-1/SCHIP1-2).
RC TISSUE=Brain;
RX PubMed=10669747; DOI=10.1128/mcb.20.5.1699-1712.2000;
RA Goutebroze L., Brault E., Muchardt C., Camonis J., Thomas G.;
RT "Cloning and characterization of SCHIP-1, a novel protein interacting
RT specifically with spliced isoforms and naturally occurring mutant NF2
RT proteins.";
RL Mol. Cell. Biol. 20:1699-1712(2000).
RN [6]
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 [7]
RP DISRUPTION 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 -!- SUBUNIT: Homooligomer (via coiled coil domain) (By similarity).
CC Interacts with NF2; the interaction is direct (By similarity).
CC Interacts with ANK3 (By similarity). {ECO:0000250|UniProtKB:P0DPB3}.
CC -!- INTERACTION:
CC P0DPB4; P35240: NF2; Xeno; NbExp=2; IntAct=EBI-1397475, EBI-1014472;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Schip1-1; Synonyms=Schip-1a {ECO:0000303|PubMed:18550753};
CC IsoId=P0DPB4-1, Q3TI53-5;
CC Sequence=Displayed;
CC Name=Schip1-2;
CC IsoId=P0DPB4-2, Q3TI53-1;
CC Sequence=VSP_046119;
CC Name=Schip1-3;
CC IsoId=P0DPB4-3, Q3TI53-3;
CC Sequence=VSP_025831, VSP_025834;
CC Name=Schip1-4; Synonyms=Schip-1b {ECO:0000303|PubMed:18550753};
CC IsoId=P0DPB4-4, Q3TI53-6;
CC Sequence=VSP_046121;
CC Name=Iqcj-schip1-1; Synonyms=IQCJ-SCHIP-1;
CC IsoId=A0A088MLT8-1; Sequence=External;
CC Name=Iqcj-schip1-2;
CC IsoId=A0A088MLT8-2; 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 -!- SIMILARITY: Belongs to the SCHIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94348.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH94348.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAB32387.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB32387.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; EU163407; ABW06760.1; -; mRNA.
DR EMBL; EU163408; ABW06761.1; -; mRNA.
DR EMBL; AK021361; BAB32387.1; ALT_SEQ; mRNA.
DR EMBL; AK168005; BAE39993.1; -; mRNA.
DR EMBL; AK146930; BAE27541.1; -; mRNA.
DR EMBL; AC093360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060529; AAH60529.1; -; mRNA.
DR EMBL; BC094348; AAH94348.1; ALT_SEQ; mRNA.
DR EMBL; AF145716; AAF34244.1; -; mRNA.
DR CCDS; CCDS50926.1; -.
DR CCDS; CCDS50927.1; -. [P0DPB4-4]
DR CCDS; CCDS50929.1; -. [P0DPB4-3]
DR CCDS; CCDS71249.1; -. [P0DPB4-2]
DR RefSeq; NP_001106891.1; NM_001113420.1. [P0DPB4-4]
DR RefSeq; NP_001106892.1; NM_001113421.1. [P0DPB4-1]
DR RefSeq; NP_001268973.1; NM_001282044.1. [P0DPB4-2]
DR RefSeq; NP_001268974.1; NM_001282045.1. [P0DPB4-2]
DR RefSeq; NP_038956.2; NM_013928.5. [P0DPB4-3]
DR AlphaFoldDB; P0DPB4; -.
DR SMR; P0DPB4; -.
DR IntAct; P0DPB4; 1.
DR STRING; 10090.ENSMUSP00000029346; -.
DR iPTMnet; P0DPB4; -.
DR PhosphoSitePlus; P0DPB4; -.
DR PRIDE; P0DPB4; -.
DR ProteomicsDB; 253406; -.
DR ProteomicsDB; 253407; -. [P0DPB4-2]
DR ProteomicsDB; 253408; -. [P0DPB4-3]
DR ProteomicsDB; 253409; -. [P0DPB4-4]
DR DNASU; 30953; -.
DR Ensembl; ENSMUST00000029346; ENSMUSP00000029346; ENSMUSG00000027777. [P0DPB4-1]
DR Ensembl; ENSMUST00000169909; ENSMUSP00000129152; ENSMUSG00000027777. [P0DPB4-4]
DR Ensembl; ENSMUST00000170788; ENSMUSP00000126443; ENSMUSG00000027777. [P0DPB4-3]
DR Ensembl; ENSMUST00000182532; ENSMUSP00000138245; ENSMUSG00000027777. [P0DPB4-2]
DR Ensembl; ENSMUST00000182719; ENSMUSP00000138207; ENSMUSG00000027777. [P0DPB4-2]
DR GeneID; 30953; -.
DR KEGG; mmu:30953; -.
DR CTD; 29970; -.
DR MGI; MGI:1353557; Schip1.
DR VEuPathDB; HostDB:ENSMUSG00000027777; -.
DR eggNOG; KOG4847; Eukaryota.
DR GeneTree; ENSGT00390000011127; -.
DR OrthoDB; 1290403at2759; -.
DR PRO; PR:P0DPB4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P0DPB4; protein.
DR Bgee; ENSMUSG00000027777; Expressed in dentate gyrus of hippocampal formation granule cell and 158 other tissues.
DR ExpressionAtlas; P0DPB4; baseline and differential.
DR Genevisible; Q3TI53; MM.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; IGI:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IGI:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0001553; P:luteinization; IGI:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR InterPro; IPR039045; SCHIP_1.
DR InterPro; IPR015649; SCHIP_1_C.
DR PANTHER; PTHR13103; PTHR13103; 1.
DR Pfam; PF10148; SCHIP-1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Reference proteome.
FT CHAIN 1..484
FT /note="Schwannomin-interacting protein 1"
FT /id="PRO_0000288928"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..455
FT /evidence="ECO:0000255"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..240
FT /note="Missing (in isoform Schip1-3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025831"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform Schip1-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_046119"
FT VAR_SEQ 23..250
FT /note="Missing (in isoform Schip1-4)"
FT /evidence="ECO:0000303|PubMed:18550753"
FT /id="VSP_046121"
FT VAR_SEQ 241..250
FT /note="QGQARTNSTS -> MVHQENCSYQ (in isoform Schip1-3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025834"
FT CONFLICT 166
FT /note="A -> V (in Ref. 5; AAF34244)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="K -> R (in Ref. 2; BAB32387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53306 MW; D6940356290904EC CRC64;
MERSEQRVRA AWDCDPGKQA DRDYREDGMD LGSDAGSSSS SRASSQSNST KVTPCSECKS
SSSPGGSLDL VSALEDYEEP FPVYQKKVID EWAPEEDGEE EEEEDDRGYR DDGCPAREPG
DVSARIGSSG SGSRSAATTM PSPMPNGNLH PHDPQDLRHN GNVVVAGRPN ASRVPRRPIQ
KTQPPGSRRG GRNRASGGLC LQPPDGGTRV PEEPPAPPMD WEALEKHLAG LQFREQEVRN
QGQARTNSTS AQKNERESIR QKLALGSFFD DGPGIYTSCS KSGKPSLSAR LQSGMNLQIC
FVNDSGSDKD SDADDSKTET SLDTPLSPMS KQSSSYSDRD TTEEESESLD DMDFLTRQKK
LQAEAKMALA MAKPMAKMQV EVEKQNRKKS PVADLLPHMP HISECLMKRS LKPTDLRDMT
IGQLQVIVND LHSQIESLNE ELVQLLLIRD ELHTEQDAML VDIEDLTRHA ESQQKHMAEK
MPAK
