GIPC1_RAT
ID GIPC1_RAT Reviewed; 333 AA.
AC Q9Z254; Q6GR70; Q9QUQ4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PDZ domain-containing protein GIPC1;
DE AltName: Full=GAIP C-terminus-interacting protein;
DE AltName: Full=GLUT1 C-terminal-binding protein;
DE Short=GLUT1CBP;
DE AltName: Full=RGS-GAIP-interacting protein;
DE AltName: Full=RGS19-interacting protein 1;
DE AltName: Full=Synectin;
GN Name=Gipc1; Synonyms=Gipc, Rgs19ip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH RGS19.
RC TISSUE=Pituitary;
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 ACTN1; GLUT1; KIF1B AND
RP MYO6.
RC STRAIN=Fischer 344; TISSUE=Brain;
RX PubMed=10198040; DOI=10.1091/mbc.10.4.819;
RA Bunn R.C., Jensen M.A., Reed B.C.;
RT "Protein interactions with the glucose transporter binding protein GLUT1CBP
RT that provide a link between GLUT1 and the cytoskeleton.";
RL Mol. Biol. Cell 10:819-832(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP INTERACTION WITH PLEKHG5.
RX PubMed=16467373; DOI=10.1091/mbc.e06-01-0002;
RA Liu M., Horowitz A.;
RT "A PDZ-binding motif as a critical determinant of Rho guanine exchange
RT factor function and cell phenotype.";
RL Mol. Biol. Cell 17:1880-1887(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May be involved in G protein-linked signaling. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SDC4/syndecan-4 and SEMA4C/semaphorin-4C (By
CC similarity). Interacts with RGS19 (C-terminus), GLUT1 (C-terminus),
CC ACTN1, KIF1B, MYO6 and PLEKHG5. {ECO:0000250,
CC ECO:0000269|PubMed:10198040, ECO:0000269|PubMed:16467373,
CC ECO:0000269|PubMed:9770488}.
CC -!- INTERACTION:
CC Q9Z254; Q6RFZ7: Plekhg5; NbExp=3; IntAct=EBI-991162, EBI-9079908;
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.
CC -!- SIMILARITY: Belongs to the GIPC family. {ECO:0000305}.
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DR EMBL; AF089817; AAC67549.1; -; mRNA.
DR EMBL; AF032120; AAC69268.1; -; mRNA.
DR EMBL; BC070505; AAH70505.1; -; mRNA.
DR RefSeq; NP_445793.1; NM_053341.1.
DR RefSeq; XP_017456861.1; XM_017601372.1.
DR AlphaFoldDB; Q9Z254; -.
DR SMR; Q9Z254; -.
DR BioGRID; 249850; 4.
DR IntAct; Q9Z254; 4.
DR MINT; Q9Z254; -.
DR STRING; 10116.ENSRNOP00000005374; -.
DR iPTMnet; Q9Z254; -.
DR PhosphoSitePlus; Q9Z254; -.
DR jPOST; Q9Z254; -.
DR PaxDb; Q9Z254; -.
DR PRIDE; Q9Z254; -.
DR Ensembl; ENSRNOT00000005374; ENSRNOP00000005374; ENSRNOG00000003864.
DR GeneID; 83823; -.
DR KEGG; rno:83823; -.
DR CTD; 10755; -.
DR RGD; 68338; Gipc1.
DR eggNOG; KOG3938; Eukaryota.
DR GeneTree; ENSGT00390000003420; -.
DR HOGENOM; CLU_044527_1_0_1; -.
DR InParanoid; Q9Z254; -.
DR OMA; QIEPQFD; -.
DR OrthoDB; 1442796at2759; -.
DR PhylomeDB; Q9Z254; -.
DR TreeFam; TF313878; -.
DR PRO; PR:Q9Z254; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000003864; Expressed in esophagus and 20 other tissues.
DR Genevisible; Q9Z254; RN.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0014047; P:glutamate secretion; ISO:RGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
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 Cytoplasm; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..333
FT /note="PDZ domain-containing protein GIPC1"
FT /id="PRO_0000087494"
FT DOMAIN 133..213
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..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 253
FT /note="V -> I (in Ref. 1; AAC67549)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> E (in Ref. 1; AAC67549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36133 MW; 2DE14E6839A218D6 CRC64;
MPLGLGRRKK APPLVENEEA EPSRSGLGVG EPGPLGGSGA GESQMGLPPP PASLRPRLVF
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPAAEVMFC TLNTHKVDMD KLLGGQIGLE
DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIQ LISVGDMIEA
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSSGGHP GSGPQLGTGR
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
