GIPC1_MOUSE
ID GIPC1_MOUSE Reviewed; 333 AA.
AC Q9Z0G0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=PDZ domain-containing protein GIPC1;
DE AltName: Full=GAIP C-terminus-interacting protein;
DE AltName: Full=RGS-GAIP-interacting protein;
DE AltName: Full=RGS19-interacting protein 1;
DE AltName: Full=SemaF cytoplasmic domain-associated protein 1;
DE Short=SEMCAP-1;
DE AltName: Full=Synectin;
GN Name=Gipc1; Synonyms=Gipc, Rgs19ip1, Semcap1;
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], AND INTERACTION WITH RGS19.
RX PubMed=9770488; DOI=10.1073/pnas.95.21.12340;
RA De Vries L., Lou X., Zhao G., Zheng B., Farquhar M.G.;
RT "GIPC, a PDZ domain containing protein, interacts specifically with the C-
RT terminus of RGS-GAIP.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SEM4C.
RX PubMed=10318831; DOI=10.1074/jbc.274.20.14137;
RA Wang L.-H., Kalb R.G., Strittmatter S.M.;
RT "A PDZ protein regulates the distribution of the transmembrane semaphorin,
RT M-SemF.";
RL J. Biol. Chem. 274:14137-14146(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SDC4.
RX PubMed=10911369;
RX DOI=10.1002/1097-4652(200009)184:3<373::aid-jcp12>3.0.co;2-i;
RA Gao Y., Li M., Chen W., Simons M.;
RT "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell
RT migration.";
RL J. Cell. Physiol. 184:373-379(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15527962; DOI=10.1016/j.gene.2004.07.028;
RA Zhang Y., Chittenden T., Simons M.;
RT "Characterization of synectin expression and promoter activity.";
RL Gene 342:29-34(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits endothelial cell migration (in vitro). May be
CC involved in G protein-linked signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6 and
CC PLEKHG5 (By similarity). Interacts with RGS19 C-terminus. Interacts
CC with SDC4/syndecan-4 and SEMA4C/semaphorin-4C. {ECO:0000250,
CC ECO:0000269|PubMed:10318831, ECO:0000269|PubMed:10911369,
CC ECO:0000269|PubMed:9770488}.
CC -!- INTERACTION:
CC Q9Z0G0; A2ARV4: Lrp2; NbExp=2; IntAct=EBI-300855, EBI-300875;
CC Q9Z0G0; Q64151: Sema4c; NbExp=8; IntAct=EBI-300855, EBI-987075;
CC Q9Z0G0; Q9UM54: MYO6; Xeno; NbExp=4; IntAct=EBI-300855, EBI-350606;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14908}.
CC Membrane {ECO:0000250|UniProtKB:O14908}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15527962}.
CC -!- DEVELOPMENTAL STAGE: Detected already at 4.5 dpc, expression peaks at
CC 11.5-12.5 dpc and gradually declines to its adult levels by 18.5 dpc.
CC {ECO:0000269|PubMed:15527962}.
CC -!- SIMILARITY: Belongs to the GIPC family. {ECO:0000305}.
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DR EMBL; AF089818; AAC67550.1; -; mRNA.
DR EMBL; AF104358; AAD12262.1; -; mRNA.
DR EMBL; AF061263; AAC72311.1; -; mRNA.
DR EMBL; AK086506; BAC39680.1; -; mRNA.
DR EMBL; BC003490; AAH03490.1; -; mRNA.
DR CCDS; CCDS22457.1; -.
DR RefSeq; NP_061241.1; NM_018771.3.
DR PDB; 5V6B; X-ray; 1.90 A; A/B=52-327.
DR PDB; 5V6E; X-ray; 3.51 A; A/C/E/G/I=258-333.
DR PDB; 5V6T; X-ray; 3.19 A; B=52-333.
DR PDB; 7NRN; NMR; -; A=255-333.
DR PDBsum; 5V6B; -.
DR PDBsum; 5V6E; -.
DR PDBsum; 5V6T; -.
DR PDBsum; 7NRN; -.
DR AlphaFoldDB; Q9Z0G0; -.
DR SMR; Q9Z0G0; -.
DR BioGRID; 212526; 9.
DR CORUM; Q9Z0G0; -.
DR DIP; DIP-33281N; -.
DR ELM; Q9Z0G0; -.
DR IntAct; Q9Z0G0; 6.
DR MINT; Q9Z0G0; -.
DR STRING; 10090.ENSMUSP00000019577; -.
DR iPTMnet; Q9Z0G0; -.
DR PhosphoSitePlus; Q9Z0G0; -.
DR EPD; Q9Z0G0; -.
DR jPOST; Q9Z0G0; -.
DR MaxQB; Q9Z0G0; -.
DR PaxDb; Q9Z0G0; -.
DR PeptideAtlas; Q9Z0G0; -.
DR PRIDE; Q9Z0G0; -.
DR ProteomicsDB; 268880; -.
DR Antibodypedia; 13703; 297 antibodies from 34 providers.
DR DNASU; 67903; -.
DR Ensembl; ENSMUST00000019577; ENSMUSP00000019577; ENSMUSG00000019433.
DR GeneID; 67903; -.
DR KEGG; mmu:67903; -.
DR UCSC; uc009mkr.1; mouse.
DR CTD; 10755; -.
DR MGI; MGI:1926252; Gipc1.
DR VEuPathDB; HostDB:ENSMUSG00000019433; -.
DR eggNOG; KOG3938; Eukaryota.
DR GeneTree; ENSGT00390000003420; -.
DR HOGENOM; CLU_044527_1_0_1; -.
DR InParanoid; Q9Z0G0; -.
DR OMA; QIEPQFD; -.
DR OrthoDB; 1442796at2759; -.
DR PhylomeDB; Q9Z0G0; -.
DR TreeFam; TF313878; -.
DR BioGRID-ORCS; 67903; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Gipc1; mouse.
DR PRO; PR:Q9Z0G0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z0G0; protein.
DR Bgee; ENSMUSG00000019433; Expressed in lip and 252 other tissues.
DR ExpressionAtlas; Q9Z0G0; baseline and differential.
DR Genevisible; Q9Z0G0; MM.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IPI:MGI.
DR GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0017022; F:myosin binding; IPI:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0014047; P:glutamate secretion; IMP:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR017379; GIPC1/2/3.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12259; PTHR12259; 1.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF038083; UCP038083_GIPC; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..333
FT /note="PDZ domain-containing protein GIPC1"
FT /id="PRO_0000087493"
FT DOMAIN 133..213
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14908"
FT CONFLICT 39
FT /note="A -> G (in Ref. 1; AAC67550)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="A -> S (in Ref. 1; AAC67550)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> D (in Ref. 1; AAC67550)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> S (in Ref. 1; AAC67550)"
FT /evidence="ECO:0000305"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 123..137
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5V6B"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5V6B"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:5V6B"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:5V6B"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:5V6B"
SQ SEQUENCE 333 AA; 36129 MW; 52E5ED6092EA9300 CRC64;
MPLGLGRRKK APPLVENEEA EPSRSGLGVG EPGPLGGSAA GESQMGLPPP PAALRPRLVF
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPAAEVMFC TLNTHKVDMD KLLGGQIGLE
DFIFAHVKGQ RKEVEVFKSE EALGLTITDN GAGYAFIKRI KEGSVIDHIQ LISVGDMIEA
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGHP GSGPQLGTGR
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
