Full text data of GIPC1
GIPC1
(C19orf3, GIPC, RGS19IP1)
[Confidence: low (only semi-automatic identification from reviews)]
PDZ domain-containing protein GIPC1 (GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; RGS19-interacting protein 1; Tax interaction protein 2; TIP-2)
PDZ domain-containing protein GIPC1 (GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; RGS19-interacting protein 1; Tax interaction protein 2; TIP-2)
UniProt
O14908
ID GIPC1_HUMAN Reviewed; 333 AA.
AC O14908; A8K4I3; A8MZG3; Q9BTC9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 122.
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=Tax interaction protein 2;
DE Short=TIP-2;
GN Name=GIPC1; Synonyms=C19orf3, GIPC, RGS19IP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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
RT the C-terminus of RGS-GAIP.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-333 (ISOFORM 1/2), AND INTERACTION
RP WITH HTLV-I TAX.
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
RT with the PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-232, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in G protein-linked signaling.
CC -!- SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6,
CC PLEKHG5, SDC4/syndecan-4 and SEMA4C/semaphorin-4C (By similarity).
CC Interacts with RGS19 C-terminus. Interacts with HTLV-I Tax through
CC the PDZ domain.
CC -!- INTERACTION:
CC Q03167:TGFBR3; NbExp=3; IntAct=EBI-373132, EBI-2852679;
CC P17643:TYRP1; NbExp=3; IntAct=EBI-373132, EBI-7900408;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14908-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14908-2; Sequence=VSP_044296;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the GIPC family.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR EMBL; AF089816; AAC67548.1; -; mRNA.
DR EMBL; AK290948; BAF83637.1; -; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84423.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84425.1; -; Genomic_DNA.
DR EMBL; BC000410; AAH00410.1; -; mRNA.
DR EMBL; BC004226; AAH04226.2; -; mRNA.
DR EMBL; BC012810; AAH12810.1; -; mRNA.
DR EMBL; BC016169; AAH16169.1; -; mRNA.
DR EMBL; AF028824; AAB84249.1; -; mRNA.
DR RefSeq; NP_005707.1; NM_005716.3.
DR RefSeq; NP_974197.1; NM_202468.2.
DR RefSeq; NP_974198.1; NM_202469.2.
DR RefSeq; NP_974199.1; NM_202470.2.
DR RefSeq; NP_974223.1; NM_202494.2.
DR RefSeq; XP_005259769.1; XM_005259712.1.
DR UniGene; Hs.655012; -.
DR UniGene; Hs.741240; -.
DR ProteinModelPortal; O14908; -.
DR SMR; O14908; 127-217.
DR IntAct; O14908; 12.
DR MINT; MINT-5003771; -.
DR STRING; 9606.ENSP00000340698; -.
DR PhosphoSite; O14908; -.
DR PaxDb; O14908; -.
DR PeptideAtlas; O14908; -.
DR PRIDE; O14908; -.
DR DNASU; 10755; -.
DR Ensembl; ENST00000345425; ENSP00000340698; ENSG00000123159.
DR Ensembl; ENST00000393028; ENSP00000376748; ENSG00000123159.
DR Ensembl; ENST00000393029; ENSP00000376749; ENSG00000123159.
DR Ensembl; ENST00000393033; ENSP00000376753; ENSG00000123159.
DR Ensembl; ENST00000586027; ENSP00000466747; ENSG00000123159.
DR Ensembl; ENST00000591349; ENSP00000467077; ENSG00000123159.
DR GeneID; 10755; -.
DR KEGG; hsa:10755; -.
DR UCSC; uc002myt.4; human.
DR CTD; 10755; -.
DR GeneCards; GC19M014600; -.
DR HGNC; HGNC:1226; GIPC1.
DR HPA; HPA043958; -.
DR MIM; 605072; gene.
DR neXtProt; NX_O14908; -.
DR PharmGKB; PA34371; -.
DR eggNOG; NOG313930; -.
DR HOGENOM; HOG000293347; -.
DR HOVERGEN; HBG000898; -.
DR InParanoid; O14908; -.
DR OMA; THKVDME; -.
DR OrthoDB; EOG793B86; -.
DR PhylomeDB; O14908; -.
DR SignaLink; O14908; -.
DR ChiTaRS; GIPC1; human.
DR GeneWiki; GIPC1; -.
DR GenomeRNAi; 10755; -.
DR NextBio; 40843; -.
DR PRO; PR:O14908; -.
DR ArrayExpress; O14908; -.
DR Bgee; O14908; -.
DR CleanEx; HS_GIPC1; -.
DR Genevestigator; O14908; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
DR GO; GO:0012506; C:vesicle membrane; ISS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; ISS:BHF-UCL.
DR GO; GO:0017022; F:myosin binding; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0043542; P:endothelial cell migration; ISS:BHF-UCL.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0014047; P:glutamate secretion; ISS:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; ISS:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISS:BHF-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:BHF-UCL.
DR GO; GO:0007268; P:synaptic transmission; ISS:BHF-UCL.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR017379; UCP038083_PDZ.
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 Alternative splicing; Complete proteome; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 333 PDZ domain-containing protein GIPC1.
FT /FTId=PRO_0000087492.
FT DOMAIN 133 213 PDZ.
FT COMPBIAS 36 42 Poly-Gly.
FT COMPBIAS 48 52 Poly-Pro.
FT MOD_RES 225 225 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine.
FT VAR_SEQ 1 97 Missing (in isoform 2).
FT /FTId=VSP_044296.
SQ SEQUENCE 333 AA; 36049 MW; AA980A4B907E3FD9 CRC64;
MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE
DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
//
ID GIPC1_HUMAN Reviewed; 333 AA.
AC O14908; A8K4I3; A8MZG3; Q9BTC9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 122.
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=Tax interaction protein 2;
DE Short=TIP-2;
GN Name=GIPC1; Synonyms=C19orf3, GIPC, RGS19IP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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
RT the C-terminus of RGS-GAIP.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-333 (ISOFORM 1/2), AND INTERACTION
RP WITH HTLV-I TAX.
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
RT with the PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-232, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in G protein-linked signaling.
CC -!- SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6,
CC PLEKHG5, SDC4/syndecan-4 and SEMA4C/semaphorin-4C (By similarity).
CC Interacts with RGS19 C-terminus. Interacts with HTLV-I Tax through
CC the PDZ domain.
CC -!- INTERACTION:
CC Q03167:TGFBR3; NbExp=3; IntAct=EBI-373132, EBI-2852679;
CC P17643:TYRP1; NbExp=3; IntAct=EBI-373132, EBI-7900408;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14908-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14908-2; Sequence=VSP_044296;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the GIPC family.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF089816; AAC67548.1; -; mRNA.
DR EMBL; AK290948; BAF83637.1; -; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84423.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84425.1; -; Genomic_DNA.
DR EMBL; BC000410; AAH00410.1; -; mRNA.
DR EMBL; BC004226; AAH04226.2; -; mRNA.
DR EMBL; BC012810; AAH12810.1; -; mRNA.
DR EMBL; BC016169; AAH16169.1; -; mRNA.
DR EMBL; AF028824; AAB84249.1; -; mRNA.
DR RefSeq; NP_005707.1; NM_005716.3.
DR RefSeq; NP_974197.1; NM_202468.2.
DR RefSeq; NP_974198.1; NM_202469.2.
DR RefSeq; NP_974199.1; NM_202470.2.
DR RefSeq; NP_974223.1; NM_202494.2.
DR RefSeq; XP_005259769.1; XM_005259712.1.
DR UniGene; Hs.655012; -.
DR UniGene; Hs.741240; -.
DR ProteinModelPortal; O14908; -.
DR SMR; O14908; 127-217.
DR IntAct; O14908; 12.
DR MINT; MINT-5003771; -.
DR STRING; 9606.ENSP00000340698; -.
DR PhosphoSite; O14908; -.
DR PaxDb; O14908; -.
DR PeptideAtlas; O14908; -.
DR PRIDE; O14908; -.
DR DNASU; 10755; -.
DR Ensembl; ENST00000345425; ENSP00000340698; ENSG00000123159.
DR Ensembl; ENST00000393028; ENSP00000376748; ENSG00000123159.
DR Ensembl; ENST00000393029; ENSP00000376749; ENSG00000123159.
DR Ensembl; ENST00000393033; ENSP00000376753; ENSG00000123159.
DR Ensembl; ENST00000586027; ENSP00000466747; ENSG00000123159.
DR Ensembl; ENST00000591349; ENSP00000467077; ENSG00000123159.
DR GeneID; 10755; -.
DR KEGG; hsa:10755; -.
DR UCSC; uc002myt.4; human.
DR CTD; 10755; -.
DR GeneCards; GC19M014600; -.
DR HGNC; HGNC:1226; GIPC1.
DR HPA; HPA043958; -.
DR MIM; 605072; gene.
DR neXtProt; NX_O14908; -.
DR PharmGKB; PA34371; -.
DR eggNOG; NOG313930; -.
DR HOGENOM; HOG000293347; -.
DR HOVERGEN; HBG000898; -.
DR InParanoid; O14908; -.
DR OMA; THKVDME; -.
DR OrthoDB; EOG793B86; -.
DR PhylomeDB; O14908; -.
DR SignaLink; O14908; -.
DR ChiTaRS; GIPC1; human.
DR GeneWiki; GIPC1; -.
DR GenomeRNAi; 10755; -.
DR NextBio; 40843; -.
DR PRO; PR:O14908; -.
DR ArrayExpress; O14908; -.
DR Bgee; O14908; -.
DR CleanEx; HS_GIPC1; -.
DR Genevestigator; O14908; -.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
DR GO; GO:0012506; C:vesicle membrane; ISS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; ISS:BHF-UCL.
DR GO; GO:0017022; F:myosin binding; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0043542; P:endothelial cell migration; ISS:BHF-UCL.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0014047; P:glutamate secretion; ISS:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; ISS:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISS:BHF-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:BHF-UCL.
DR GO; GO:0007268; P:synaptic transmission; ISS:BHF-UCL.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR017379; UCP038083_PDZ.
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 Alternative splicing; Complete proteome; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 333 PDZ domain-containing protein GIPC1.
FT /FTId=PRO_0000087492.
FT DOMAIN 133 213 PDZ.
FT COMPBIAS 36 42 Poly-Gly.
FT COMPBIAS 48 52 Poly-Pro.
FT MOD_RES 225 225 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine.
FT VAR_SEQ 1 97 Missing (in isoform 2).
FT /FTId=VSP_044296.
SQ SEQUENCE 333 AA; 36049 MW; AA980A4B907E3FD9 CRC64;
MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF
HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE
DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA
INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR
GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
//
MIM
605072
*RECORD*
*FIELD* NO
605072
*FIELD* TI
*605072 GIPC PDZ DOMAIN-CONTAINING FAMILY, MEMBER 1; GIPC1
;;GAIP C-TERMINUS-INTERACTING PROTEIN 1;;
read moreGIPC;;
RGS19-INTERACTING PROTEIN 1; RGS19IP1;;
CHROMOSOME 19 OPEN READING FRAME 3; C19ORF3;;
GLUT1 C-TERMINUS-BINDING PROTEIN; GLUT1CBP;;
SYNECTIN
*FIELD* TX
DESCRIPTION
GIPC1 is a scaffolding protein that regulates cell surface receptor
expression and trafficking (Lee et al., 2008).
CLONING
Regulators of G protein signaling (e.g., RGS3; 602189) act as
GTPase-activating and -enhancing proteins that bind to the alpha
subunits of heterotrimeric G proteins. Although their RGS domains are
diagnostic and highly homologous, RGS proteins are highly divergent at
their N and C termini. GAIP (RGS19; 605071) is a membrane-anchored RGS
protein located on clathrin-coated vesicles involved in membrane
trafficking. By screening a rat pituitary cell library using a yeast
2-hybrid system with GAIP as bait, and by searching an EST database, De
Vries et al. (1998) obtained a cDNA encoding GIPC1, which they called
GIPC. The predicted 36-kD, hydrophilic GIPC1 protein contains 333 amino
acids, including multiple phosphorylation sites and an 80- to 100-amino
acid PDZ domain. PDZ domain-containing proteins (see DLG4; 602887)
typically recognize C-terminal amino acids and are involved in protein
network signaling. GIPC1 shares 96% amino acid identity with rat Gipc.
Northern blot analysis detected a 1.8-kb transcript in all tissues
tested, with strongest expression in pancreas, followed by skeletal
muscle, brain, kidney, placenta, lung, liver, and lowest expression in
heart. Expression levels did not correlate with those of GAIP.
Immunoblot analysis demonstrated the presence of GIPC1 primarily in
cytosolic fractions but also in membrane fractions. Immunofluorescence
analysis showed expression of endogenous GIPC1 in both a diffuse and a
punctate staining pattern throughout the cytoplasm.
Using a yeast 2-hybrid system, Bunn et al. (1999) isolated a cDNA
encoding GIPC1, which they called GLUT1CBP (GLUT1 (SLC2A1; 138140)
C-terminus-binding protein). SDS-PAGE and Western blot analyses showed
expression of a 39-kD protein in all tissues tested except small
intestine. Northern blot analysis revealed similar expression patterns
for GIPC1 and SLC2A1, with both being expressed most strongly in brain.
GENE FUNCTION
Using yeast 2-hybrid analysis, De Vries et al. (1998) found that GIPC1
bound GAIP and no other RGS proteins, and that the interaction occurred
between the C-terminal alanine of GAIP and the PDZ domain of GIPC1.
By yeast 2-hybrid analysis, Bunn et al. (1999) showed that C19ORF3 bound
SLC2A1 through its PDZ domain. Using a yeast 2-hybrid screen for
brain-interacting proteins, they determined that only SLC2A1, KIF1B, and
alpha actinin-1 (ACTN1; 102575) bound C19ORF3 through its PDZ domain;
myosin VI (MYO6; 600970) was shown to interact with C19ORF3, but not via
the PDZ domain.
Naccache et al. (2006) found that Myo6 recruitment to uncoated endocytic
vesicles in cultured mouse kidney epithelial cells was dependent on
synectin. Myo6 bound a C-terminal domain of synectin, and Myo6
recruitment required the interaction between the PDZ-binding domains of
engulfed receptors, such as megalin (LRP2; 600073), and the PDZ domain
of synectin.
Endoglin (131195) is a TGF-beta (TGFB1; 190180) coreceptor expressed
predominantly in endothelial cells. Using predominantly embryonic mouse
endothelial cell lines, Lee et al. (2008) showed that endoglin and Gipc
interacted directly. The interaction enhanced TGF-beta-1-induced
phosphorylation of Smad1 (601595)/Smad5 (603110)/Smad8 (SMAD9; 603295),
increased a Smad1/Smad5/Smad8-responsive promoter, and inhibited
endothelial cell migration.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GIPC1
gene to chromosome 19 (TMAP sts-W73036). By radiation hybrid analysis
and FISH, Von Kap-Herr et al. (2000) localized the GIPC1 gene to
chromosome 19p13.1.
ANIMAL MODEL
Chittenden et al. (2006) found that synectin-null mice were smaller than
wildtype mice and had reduced numbers of arteries and an altered pattern
of arterial branching in multiple vascular beds, whereas the venous
system remained normal. Primary arterial, but not venous, endothelial
cells from synectin-null mice showed decreased in vitro tube formation,
migration, and proliferation and impaired polarization due to abnormal
localization of activated Rac1 (602048). A similar defect in the
arterial system was present in synectin-null zebrafish embryos.
Naccache et al. (2006) found that synectin-null mice, like megalin-null
mice, showed proteinuria. Urine from synectin-null mice contained
retinol-binding protein (see RBP1; 180260), a known megalin ligand.
Myo6, an actin-based molecular motor involved in endocytic trafficking,
was upregulated in synectin-null kidneys. Megalin expression in proximal
tubules of synectin-null mouse kidneys was normal compared to wildtype,
suggesting that megalin recycling is defective in synectin-null mice.
Naccache et al. (2006) concluded that synectin is required for proper
megalin trafficking in vivo.
*FIELD* RF
1. Bunn, R. C.; Jensen, M. A.; Reed, B. C.: Protein interactions
with the glucose transporter binding protein GLUT1CBP that provide
a link between GLUT1 and the cytoskeleton. Molec. Biol. Cell 10:
819-832, 1999.
2. Chittenden, T. W.; Claes, F.; Lanahan, A. A.; Autiero, M.; Palac,
R. T.; Tkachenko, E. V.; Elfenbein, A.; Ruiz de Almodovar, C.; Dedkov,
E.; Tomanek, R.; Li, W.; Westmore, M.; Singh, J.; Horowitz, A.; Mulligan-Kehoe,
M. J.; Moodie, K. L.; Zhuang, Z. W.; Carmeliet, P.; Simons, M.: Selective
regulation of arterial branching morphogenesis by synectin. Dev.
Cell 10: 783-795, 2006.
3. De Vries, L.; Lou, X.; Zhao, G.; Zheng, B.; Farquhar, M. G.: GIPC,
a PDZ domain containing protein, interacts specifically with the C
terminus of RGS-GAIP. Proc. Nat. Acad. Sci. 95: 12340-12345, 1998.
4. Lee, N. Y.; Ray, B.; How, T.; Blobe, G. C.: Endoglin promotes
transforming growth factor beta-mediated Smad 1/5/8 signaling and
inhibits endothelial cell migration through its association with GIPC. J.
Biol. Chem. 283: 32527-32533, 2008.
5. Naccache, S. N.; Hasson, T.; Horowitz, A.: Binding of internalized
receptors to the PDZ domain of GIPC/synectin recruits myosin VI to
endocytic vesicles. Proc. Nat. Acad. Sci. 103: 12735-12740, 2006.
Note: Erratum: Proc. Nat. Acad. Sci. 103: 15272 only, 2006.
6. Von Kap-Herr, C.; Kandala, G.; Mann, S. S.; Hart, T. C.; Pettenati,
M. J.; Setaluri, V.: Assignment of PDZ domain-containing protein
GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization
and radiation hybrid mapping. Cytogenet. Cell Genet. 89: 234-235,
2000.
*FIELD* CN
Patricia A. Hartz - updated: 4/21/2009
Patricia A. Hartz - updated: 10/10/2006
Patricia A. Hartz - updated: 7/11/2006
Carol A. Bocchini - updated: 1/16/2001
*FIELD* CD
Paul J. Converse: 6/23/2000
*FIELD* ED
wwang: 07/28/2011
mgross: 4/24/2009
terry: 4/21/2009
wwang: 12/1/2006
wwang: 10/11/2006
terry: 10/10/2006
mgross: 7/11/2006
terry: 7/11/2006
mgross: 1/28/2002
cwells: 5/24/2001
mcapotos: 1/17/2001
carol: 1/16/2001
mgross: 6/26/2000
mgross: 6/23/2000
*RECORD*
*FIELD* NO
605072
*FIELD* TI
*605072 GIPC PDZ DOMAIN-CONTAINING FAMILY, MEMBER 1; GIPC1
;;GAIP C-TERMINUS-INTERACTING PROTEIN 1;;
read moreGIPC;;
RGS19-INTERACTING PROTEIN 1; RGS19IP1;;
CHROMOSOME 19 OPEN READING FRAME 3; C19ORF3;;
GLUT1 C-TERMINUS-BINDING PROTEIN; GLUT1CBP;;
SYNECTIN
*FIELD* TX
DESCRIPTION
GIPC1 is a scaffolding protein that regulates cell surface receptor
expression and trafficking (Lee et al., 2008).
CLONING
Regulators of G protein signaling (e.g., RGS3; 602189) act as
GTPase-activating and -enhancing proteins that bind to the alpha
subunits of heterotrimeric G proteins. Although their RGS domains are
diagnostic and highly homologous, RGS proteins are highly divergent at
their N and C termini. GAIP (RGS19; 605071) is a membrane-anchored RGS
protein located on clathrin-coated vesicles involved in membrane
trafficking. By screening a rat pituitary cell library using a yeast
2-hybrid system with GAIP as bait, and by searching an EST database, De
Vries et al. (1998) obtained a cDNA encoding GIPC1, which they called
GIPC. The predicted 36-kD, hydrophilic GIPC1 protein contains 333 amino
acids, including multiple phosphorylation sites and an 80- to 100-amino
acid PDZ domain. PDZ domain-containing proteins (see DLG4; 602887)
typically recognize C-terminal amino acids and are involved in protein
network signaling. GIPC1 shares 96% amino acid identity with rat Gipc.
Northern blot analysis detected a 1.8-kb transcript in all tissues
tested, with strongest expression in pancreas, followed by skeletal
muscle, brain, kidney, placenta, lung, liver, and lowest expression in
heart. Expression levels did not correlate with those of GAIP.
Immunoblot analysis demonstrated the presence of GIPC1 primarily in
cytosolic fractions but also in membrane fractions. Immunofluorescence
analysis showed expression of endogenous GIPC1 in both a diffuse and a
punctate staining pattern throughout the cytoplasm.
Using a yeast 2-hybrid system, Bunn et al. (1999) isolated a cDNA
encoding GIPC1, which they called GLUT1CBP (GLUT1 (SLC2A1; 138140)
C-terminus-binding protein). SDS-PAGE and Western blot analyses showed
expression of a 39-kD protein in all tissues tested except small
intestine. Northern blot analysis revealed similar expression patterns
for GIPC1 and SLC2A1, with both being expressed most strongly in brain.
GENE FUNCTION
Using yeast 2-hybrid analysis, De Vries et al. (1998) found that GIPC1
bound GAIP and no other RGS proteins, and that the interaction occurred
between the C-terminal alanine of GAIP and the PDZ domain of GIPC1.
By yeast 2-hybrid analysis, Bunn et al. (1999) showed that C19ORF3 bound
SLC2A1 through its PDZ domain. Using a yeast 2-hybrid screen for
brain-interacting proteins, they determined that only SLC2A1, KIF1B, and
alpha actinin-1 (ACTN1; 102575) bound C19ORF3 through its PDZ domain;
myosin VI (MYO6; 600970) was shown to interact with C19ORF3, but not via
the PDZ domain.
Naccache et al. (2006) found that Myo6 recruitment to uncoated endocytic
vesicles in cultured mouse kidney epithelial cells was dependent on
synectin. Myo6 bound a C-terminal domain of synectin, and Myo6
recruitment required the interaction between the PDZ-binding domains of
engulfed receptors, such as megalin (LRP2; 600073), and the PDZ domain
of synectin.
Endoglin (131195) is a TGF-beta (TGFB1; 190180) coreceptor expressed
predominantly in endothelial cells. Using predominantly embryonic mouse
endothelial cell lines, Lee et al. (2008) showed that endoglin and Gipc
interacted directly. The interaction enhanced TGF-beta-1-induced
phosphorylation of Smad1 (601595)/Smad5 (603110)/Smad8 (SMAD9; 603295),
increased a Smad1/Smad5/Smad8-responsive promoter, and inhibited
endothelial cell migration.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GIPC1
gene to chromosome 19 (TMAP sts-W73036). By radiation hybrid analysis
and FISH, Von Kap-Herr et al. (2000) localized the GIPC1 gene to
chromosome 19p13.1.
ANIMAL MODEL
Chittenden et al. (2006) found that synectin-null mice were smaller than
wildtype mice and had reduced numbers of arteries and an altered pattern
of arterial branching in multiple vascular beds, whereas the venous
system remained normal. Primary arterial, but not venous, endothelial
cells from synectin-null mice showed decreased in vitro tube formation,
migration, and proliferation and impaired polarization due to abnormal
localization of activated Rac1 (602048). A similar defect in the
arterial system was present in synectin-null zebrafish embryos.
Naccache et al. (2006) found that synectin-null mice, like megalin-null
mice, showed proteinuria. Urine from synectin-null mice contained
retinol-binding protein (see RBP1; 180260), a known megalin ligand.
Myo6, an actin-based molecular motor involved in endocytic trafficking,
was upregulated in synectin-null kidneys. Megalin expression in proximal
tubules of synectin-null mouse kidneys was normal compared to wildtype,
suggesting that megalin recycling is defective in synectin-null mice.
Naccache et al. (2006) concluded that synectin is required for proper
megalin trafficking in vivo.
*FIELD* RF
1. Bunn, R. C.; Jensen, M. A.; Reed, B. C.: Protein interactions
with the glucose transporter binding protein GLUT1CBP that provide
a link between GLUT1 and the cytoskeleton. Molec. Biol. Cell 10:
819-832, 1999.
2. Chittenden, T. W.; Claes, F.; Lanahan, A. A.; Autiero, M.; Palac,
R. T.; Tkachenko, E. V.; Elfenbein, A.; Ruiz de Almodovar, C.; Dedkov,
E.; Tomanek, R.; Li, W.; Westmore, M.; Singh, J.; Horowitz, A.; Mulligan-Kehoe,
M. J.; Moodie, K. L.; Zhuang, Z. W.; Carmeliet, P.; Simons, M.: Selective
regulation of arterial branching morphogenesis by synectin. Dev.
Cell 10: 783-795, 2006.
3. De Vries, L.; Lou, X.; Zhao, G.; Zheng, B.; Farquhar, M. G.: GIPC,
a PDZ domain containing protein, interacts specifically with the C
terminus of RGS-GAIP. Proc. Nat. Acad. Sci. 95: 12340-12345, 1998.
4. Lee, N. Y.; Ray, B.; How, T.; Blobe, G. C.: Endoglin promotes
transforming growth factor beta-mediated Smad 1/5/8 signaling and
inhibits endothelial cell migration through its association with GIPC. J.
Biol. Chem. 283: 32527-32533, 2008.
5. Naccache, S. N.; Hasson, T.; Horowitz, A.: Binding of internalized
receptors to the PDZ domain of GIPC/synectin recruits myosin VI to
endocytic vesicles. Proc. Nat. Acad. Sci. 103: 12735-12740, 2006.
Note: Erratum: Proc. Nat. Acad. Sci. 103: 15272 only, 2006.
6. Von Kap-Herr, C.; Kandala, G.; Mann, S. S.; Hart, T. C.; Pettenati,
M. J.; Setaluri, V.: Assignment of PDZ domain-containing protein
GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization
and radiation hybrid mapping. Cytogenet. Cell Genet. 89: 234-235,
2000.
*FIELD* CN
Patricia A. Hartz - updated: 4/21/2009
Patricia A. Hartz - updated: 10/10/2006
Patricia A. Hartz - updated: 7/11/2006
Carol A. Bocchini - updated: 1/16/2001
*FIELD* CD
Paul J. Converse: 6/23/2000
*FIELD* ED
wwang: 07/28/2011
mgross: 4/24/2009
terry: 4/21/2009
wwang: 12/1/2006
wwang: 10/11/2006
terry: 10/10/2006
mgross: 7/11/2006
terry: 7/11/2006
mgross: 1/28/2002
cwells: 5/24/2001
mcapotos: 1/17/2001
carol: 1/16/2001
mgross: 6/26/2000
mgross: 6/23/2000