IQIP1_HUMAN
ID IQIP1_HUMAN Reviewed; 563 AA.
AC B3KU38; B3KRM0; O75543; Q00P30; Q00P31; Q7Z3Y3; Q8IY83; Q9P0W3; Q9P0W4;
AC Q9P0W5;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=IQCJ-SCHIP1 readthrough transcript protein {ECO:0000312|HGNC:HGNC:38842};
GN Name=IQCJ-SCHIP1 {ECO:0000312|HGNC:HGNC:38842};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:BAG53300.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IQCJ-SCHIP1-1 AND IQCJ-SCHIP1-2),
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17045569; DOI=10.1016/j.bbrc.2006.09.136;
RA Kwasnicka-Crawford D.A., Carson A.R., Scherer S.W.;
RT "IQCJ-SCHIP1, a novel fusion transcript encoding a calmodulin-binding IQ
RT motif protein.";
RL Biochem. Biophys. Res. Commun. 350:890-899(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IQCJ-SCHIP1-1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP FUNCTION, AND INTERACTION WITH ANK3.
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).
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:25950943). May also play a
CC role in axon outgrowth and guidance (By similarity).
CC {ECO:0000250|UniProtKB:A0A088MLT8, ECO:0000269|PubMed:25950943}.
CC -!- SUBUNIT: Homooligomer (via coiled coil domain). Interacts (via IQ
CC domain) with calmodulin; the interaction is direct and lost in presence
CC of calcium (By similarity). Interacts with ANK3 (via ANK repeats);
CC required for localization at axon initial segments (AIS) and nodes of
CC Ranvier (PubMed:25950943). Interacts with SPTBN4. Interacts with KCNQ2
CC and KCNQ3 (By similarity). {ECO:0000250|UniProtKB:A0A088MLT8,
CC ECO:0000269|PubMed:25950943}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:A0A088MLT8}. Cytoplasm
CC {ECO:0000269|PubMed:17045569}. Note=Localizes to the axon initial
CC segments (AIS) and nodes of Ranvier of neurons and is absent from
CC dendrites. {ECO:0000250|UniProtKB:A0A088MLT8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=IQCJ-SCHIP1-1;
CC IsoId=B3KU38-1; Sequence=Displayed;
CC Name=IQCJ-SCHIP1-2;
CC IsoId=B3KU38-2; Sequence=VSP_059227;
CC Name=SCHIP1-1; Synonyms=SCHIP-1, SCHIP-1a;
CC IsoId=P0DPB3-1, Q9P0W5-1;
CC Sequence=External;
CC Name=SCHIP1-2; Synonyms=SCHIP-1-D241/253;
CC IsoId=P0DPB3-2, Q9P0W5-2;
CC Sequence=External;
CC Name=SCHIP1-3; Synonyms=SCHIP-1-D22/253;
CC IsoId=P0DPB3-3, Q9P0W5-3;
CC Sequence=External;
CC Name=SCHIP1-4;
CC IsoId=P0DPB3-4, Q9P0W5-4;
CC Sequence=External;
CC Name=IQCJ-1;
CC IsoId=Q1A5X6-1; Sequence=External;
CC Name=IQCJ-2;
CC IsoId=Q1A5X6-2; Sequence=External;
CC Name=IQCJ-3;
CC IsoId=Q1A5X6-3; Sequence=External;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and to a lower extent in
CC heart and kidney. {ECO:0000269|PubMed:17045569}.
CC -!- DEVELOPMENTAL STAGE: Isoform IQCJ-SCHIP1-1 and isoform IQCJ-SCHIP1-2
CC are expressed in fetal brain, kidney, spleen and skeletal muscle.
CC Isoform IQCJ-SCHIP1-2 is also detected in fetal heart and lung.
CC {ECO:0000269|PubMed:17045569}.
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:17045569}.
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:17045569}.
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DR EMBL; DQ157847; ABA42889.1; -; mRNA.
DR EMBL; DQ157848; ABA42890.1; -; mRNA.
DR EMBL; AK096479; BAG53300.1; -; mRNA.
DR EMBL; AC021654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS56289.1; -. [B3KU38-1]
DR CCDS; CCDS56291.1; -. [B3KU38-2]
DR RefSeq; NP_001184042.1; NM_001197113.1. [B3KU38-1]
DR RefSeq; NP_001184043.1; NM_001197114.1. [B3KU38-2]
DR AlphaFoldDB; B3KU38; -.
DR SMR; B3KU38; -.
DR STRING; 9606.ENSP00000420182; -.
DR iPTMnet; B3KU38; -.
DR BioMuta; IQCJ-SCHIP1; -.
DR jPOST; B3KU38; -.
DR MassIVE; B3KU38; -.
DR MaxQB; B3KU38; -.
DR PRIDE; B3KU38; -.
DR Antibodypedia; 78841; 124 antibodies from 12 providers.
DR DNASU; 100505385; -.
DR Ensembl; ENST00000476809.7; ENSP00000418692.1; ENSG00000283154.3. [B3KU38-2]
DR Ensembl; ENST00000485419.7; ENSP00000420182.1; ENSG00000283154.3. [B3KU38-1]
DR GeneID; 100505385; -.
DR KEGG; hsa:100505385; -.
DR CTD; 100505385; -.
DR DisGeNET; 100505385; -.
DR GeneCards; IQCJ-SCHIP1; -.
DR HGNC; HGNC:38842; IQCJ-SCHIP1.
DR HPA; ENSG00000283154; Tissue enhanced (brain, choroid plexus).
DR neXtProt; NX_B3KU38; -.
DR OpenTargets; ENSG00000283154; -.
DR VEuPathDB; HostDB:ENSG00000283154; -.
DR eggNOG; KOG4847; Eukaryota.
DR GeneTree; ENSGT00390000011127; -.
DR OMA; CGTCVPE; -.
DR OrthoDB; 1290403at2759; -.
DR PathwayCommons; B3KU38; -.
DR BioGRID-ORCS; 100505385; 11 hits in 1003 CRISPR screens.
DR ChiTaRS; IQCJ-SCHIP1; human.
DR GenomeRNAi; 100505385; -.
DR Pharos; B3KU38; Tdark.
DR PRO; PR:B3KU38; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000283154; Expressed in ventricular zone and 99 other tissues.
DR ExpressionAtlas; B3KU38; baseline and differential.
DR Genevisible; B3KU38; HS.
DR GO; GO:0043194; C:axon initial segment; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IMP: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 Phosphoprotein; Reference proteome.
FT CHAIN 1..563
FT /note="IQCJ-SCHIP1 readthrough transcript protein"
FT /id="PRO_0000442334"
FT DOMAIN 47..67
FT /note="IQ"
FT REGION 63..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..563
FT /note="Required for interaction with ankyrins"
FT /evidence="ECO:0000250|UniProtKB:A0A088MLT8"
FT COILED 500..534
FT /evidence="ECO:0000255"
FT COMPBIAS 69..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 26..52
FT /note="Missing (in isoform IQCJ-SCHIP1-2)"
FT /id="VSP_059227"
FT CONFLICT 230
FT /note="Q -> R (in Ref. 2; BAG53300 and 1; ABA42890/
FT ABA42889)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="D -> A (in Ref. 2; BAG53300 and 1; ABA42890/
FT ABA42889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 62248 MW; 54C0F2D21E4B2739 CRC64;
MRLEELKRLQ NPLEQVNDGK YSFENHQLAM DAENNIEKYP LNLQPLESKV KIIQRAWREY
LQRQEPLGKR SPSPPSVSSE KLSSSVSMNT FSDSSTPDYR EDGMDLGSDA GSSSSSSRAS
SQSNSTKVTP CSECKSSSSP GGSLDLVSAL EDYEEPFPVY QKKVIDEWAP EEDGEEEEEE
DERDQRGYRD DRSPAREPGD VSARTRSGGG GGRSATTAMP PPVPNGNLHQ HDPQDLRHNG
NVVVAGRPSC SRGPRRAIQK PQPAGGRRSG RGPAAGGLCL QPPDGGTCVP EEPPVPPMDW
EALEKHLAGL QFREQEVRNQ GQARTNSTSA QKNERESIRQ KLALGSFFDD GPGIYTSCSK
SGKPSLSSRL QSGMNLQICF VNDSGSDKDS DADDSKTETS LDTPLSPMSK QSSSYSDRDT
TEEESESLDD MDFLTRQKKL QAEAKMALAM AKPMAKMQVE VEKQNRKKSP VADLLPHMPH
ISECLMKRSL KPTDLRDMTI GQLQVIVNDL HSQIESLNEE LVQLLLIRDE LHTEQDAMLV
DIEDLTRHAE SQQKHMAEKM PAK
