GRDN_MOUSE
ID GRDN_MOUSE Reviewed; 1873 AA.
AC Q5SNZ0; Q5M6X2; Q5M6X4; Q5M6X5; Q5SNZ1; Q8C486; Q8CFU7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Girdin;
DE AltName: Full=Akt phosphorylation enhancer;
DE Short=APE;
DE AltName: Full=Coiled-coil domain-containing protein 88A;
DE AltName: Full=G alpha-interacting vesicle-associated protein;
DE Short=GIV;
DE AltName: Full=Girders of actin filament;
DE AltName: Full=Hook-related protein 1;
DE Short=HkRP1;
GN Name=Ccdc88a; Synonyms=Grdn, Kiaa1212;
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] {ECO:0000305, ECO:0000312|EMBL:BAD98263.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH AKT1,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:15753085};
RX PubMed=15753085; DOI=10.1074/jbc.m500586200;
RA Anai M., Shojima N., Katagiri H., Ogihara T., Sakoda H., Onishi Y., Ono H.,
RA Fujishiro M., Fukushima Y., Horike N., Viana A., Kikuchi M., Noguchi N.,
RA Takahashi S., Takata K., Oka Y., Uchijima Y., Kurihara H., Asano T.;
RT "A novel protein kinase B (PKB)/AKT-binding protein enhances PKB kinase
RT activity and regulates DNA synthesis.";
RL J. Biol. Chem. 280:18525-18535(2005).
RN [2]
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH37020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1086-1873 (ISOFORMS 2/3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH37020.1};
RC TISSUE=Retina {ECO:0000312|EMBL:AAH37020.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC38612.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1623-1873.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38612.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAC38612.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7] {ECO:0000305}
RP SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15882442; DOI=10.1111/j.1600-0854.2005.00289.x;
RA Simpson F., Martin S., Evans T.M., Kerr M., James D.E., Parton R.G.,
RA Teasdale R.D., Wicking C.;
RT "A novel hook-related protein family and the characterization of hook-
RT related protein 1.";
RL Traffic 6:442-458(2005).
RN [8] {ECO:0000305}
RP REVIEW.
RX PubMed=17185515; DOI=10.1196/annals.1377.016;
RA Enomoto A., Ping J., Takahashi M.;
RT "Girdin, a novel actin-binding protein, and its family of proteins possess
RT versatile functions in the Akt and Wnt signaling pathways.";
RL Ann. N. Y. Acad. Sci. 1086:169-184(2006).
RN [9]
RP FUNCTION, INTERACTION WITH DISC1 AND AKT PROTEINS, AND TISSUE SPECIFICITY.
RX PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
RA Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
RA Kang E., Song H., Ming G.L.;
RT "DISC1 regulates new neuron development in the adult brain via modulation
RT of AKT-mTOR signaling through KIAA1212.";
RL Neuron 63:761-773(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-237 AND SER-1677,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=26917597; DOI=10.1093/brain/aww014;
RA Nahorski M.S., Asai M., Wakeling E., Parker A., Asai N., Canham N.,
RA Holder S.E., Chen Y.C., Dyer J., Brady A.F., Takahashi M., Woods C.G.;
RT "CCDC88A mutations cause PEHO-like syndrome in humans and mouse.";
RL Brain 139:1036-1044(2016).
CC -!- FUNCTION: Bifunctional modulator of guanine nucleotide-binding proteins
CC (G proteins) (By similarity). Acts as a non-receptor guanine nucleotide
CC exchange factor which binds to and activates guanine nucleotide-binding
CC protein G(i) alpha subunits (By similarity). Also acts as a guanine
CC nucleotide dissociation inhibitor for guanine nucleotide-binding
CC protein G(s) subunit alpha GNAS (By similarity). Essential for cell
CC migration (By similarity). Interacts in complex with G(i) alpha
CC subunits with the EGFR receptor, retaining EGFR at the cell membrane
CC following ligand stimulation and promoting EGFR signaling which
CC triggers cell migration (By similarity). Binding to Gi-alpha subunits
CC displaces the beta and gamma subunits from the heterotrimeric G-protein
CC complex which enhances phosphoinositide 3-kinase (PI3K)-dependent
CC phosphorylation and kinase activity of AKT1/PKB (By similarity).
CC Phosphorylation of AKT1/PKB induces the phosphorylation of downstream
CC effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell
CC proliferation (PubMed:15753085). Binds in its tyrosine-phosphorylated
CC form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit
CC PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor,
CC enhancing PI3K activity and cell migration (By similarity). Plays a
CC role as a key modulator of the AKT-mTOR signaling pathway, controlling
CC the tempo of the process of newborn neuron integration during adult
CC neurogenesis, including correct neuron positioning, dendritic
CC development and synapse formation (PubMed:19778506). Inhibition of G(s)
CC subunit alpha GNAS leads to reduced cellular levels of cAMP and
CC suppression of cell proliferation (By similarity). Essential for the
CC integrity of the actin cytoskeleton (By similarity). Required for
CC formation of actin stress fibers and lamellipodia (By similarity). May
CC be involved in membrane sorting in the early endosome (By similarity).
CC Plays a role in ciliogenesis and cilium morphology and positioning and
CC this may partly be through regulation of the localization of
CC scaffolding protein CROCC/Rootletin (By similarity).
CC {ECO:0000250|UniProtKB:Q3V6T2, ECO:0000269|PubMed:15753085,
CC ECO:0000269|PubMed:19778506}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via GBA motif) with
CC guanine nucleotide-binding protein G(i) alpha subunits GNAI1, GNAI2 and
CC GNAI3 (By similarity). Also interacts (via GNA motif) with guanine
CC nucleotide-binding protein G(s) alpha subunit GNAS (By similarity).
CC Interaction with G(i) alpha subunits occurs before interaction with
CC GNAS and is regulated by phosphorylation; phosphorylation at Ser-1677
CC enhances binding to G(i) alpha subunits while phosphorylation at Ser-
CC 1692 abolishes G(i) alpha subunit binding, promoting binding to GNAS
CC (By similarity). Interacts (via C-terminal SH2-like region) with growth
CC factor receptors EGFR, INSR and KDR/VEGFR2 (via their
CC autophosphorylated cytoplasmic tails) (By similarity). Forms a complex
CC with EGFR and GNAI3 which leads to enhanced EGFR signaling and
CC triggering of cell migration; ligand stimulation is required for
CC recruitment of GNAI3 to the complex (By similarity). Interacts
CC (tyrosine-phosphorylated form) with phosphatidylinositol 3-kinase
CC (PI3K) regulatory subunit PIK3R1/p85a (via SH2 domains); the
CC interaction enables recruitment of PIK3R1 to the EGFR receptor,
CC enhancing PI3K activity and cell migration (By similarity). Interacts
CC with serine/threonine-protein kinase PRKCQ; the interaction leads to
CC phosphorylation of CCDC88A and inhibition of its guanine nucleotide
CC exchange factor activity (By similarity). Interacts (via C-terminus)
CC with DISC1; the interaction is direct (PubMed:19778506). Interacts with
CC AKT proteins; the interaction is inhibited in the presence of DISC1
CC (PubMed:19778506). Interacts with AKT1/PKB (via C-terminus)
CC (PubMed:15753085). The non-phosphorylated form interacts with
CC phosphatidylinositol 4-phosphate [Pi(4)P] and weakly with
CC phosphatidylinositol 3-phosphate [Pi(3)P] (By similarity). Interacts
CC with microtubules (PubMed:15882442). Interacts with actin (By
CC similarity). {ECO:0000250|UniProtKB:Q3V6T2,
CC ECO:0000269|PubMed:15753085, ECO:0000269|PubMed:15882442,
CC ECO:0000269|PubMed:19778506}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3V6T2};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q3V6T2}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q3V6T2}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q3V6T2}. Note=Localizes to the cytosol in
CC unstimulated cells while EGF stimulation promotes membrane localization
CC and guanine nucleotide exchange factor activity (By similarity).
CC Localizes to the cell membrane through interaction with
CC phosphoinositides (By similarity). {ECO:0000250|UniProtKB:Q3V6T2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SNZ0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15753085};
CC IsoId=Q5SNZ0-2; Sequence=VSP_052411;
CC Name=3;
CC IsoId=Q5SNZ0-3; Sequence=VSP_052410, VSP_052411;
CC -!- TISSUE SPECIFICITY: Expressed in the dentate gyrus, pyramidal cell
CC layer of hippocampal regions CA1 and CA3 at postnatal 15. Expressed
CC highly in neurons. Weakly in neuron progenitors (at protein level).
CC Expressed in the dentate granule cell layer of the hippocampus.
CC Expressed highly in the adult testis, moderately in the brain and at a
CC low level in the spleen, lungs and fat. {ECO:0000269|PubMed:15753085,
CC ECO:0000269|PubMed:15882442, ECO:0000269|PubMed:19778506}.
CC -!- DEVELOPMENTAL STAGE: Temporally and spatially restricted during
CC embryogenesis. At 10.5 dpc, expressed in the branchial arches, nasal
CC processes, limbs, somites and dorsal root ganglia. At 11.5 dpc,
CC expression persists at these sites in addition to the eye and fore-,
CC mid- and hindbrain. By 12.5 dpc, expressed in the interdigital
CC mesenchyme of the limbs. At 13.5 dpc, expression in the limbs flanks
CC the digits and also appears in a subset of tendons in the hind- and
CC forelimbs. {ECO:0000269|PubMed:15882442}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000250|UniProtKB:Q3V6T2}.
CC -!- DOMAIN: In the presence of tyrosine-autophosphorylated growth factor
CC receptors, the C-terminus folds into an SH2-like region which promotes
CC the stable recruitment of CCDC88A to the growth factor receptors. The
CC SH2-like region is phosphorylated by the growth factor receptors prior
CC to completion of folding. {ECO:0000250|UniProtKB:Q3V6T2}.
CC -!- PTM: Phosphorylation is induced by epidermal growth factor (EGF) in a
CC phosphoinositide 3-kinase (PI3K)-dependent manner (By similarity).
CC Phosphorylation by AKT1/PKB is necessary for the delocalization from
CC the cell membrane and for cell migration (By similarity).
CC Phosphorylated on tyrosine residues which promotes binding to
CC phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1/p85a and
CC enhances PI3K activity (By similarity). Tyrosine-phosphorylated by both
CC receptor and non-receptor tyrosine kinases in vitro (By similarity).
CC Tyrosine phosphorylation is required for AKT1-dependent phosphorylation
CC of Ser-1417 (By similarity). Phosphorylation at Ser-1692 by PRKCQ
CC disrupts interaction with GNAI3 and inhibits guanine nucleotide
CC exchange factor activity (By similarity).
CC {ECO:0000250|UniProtKB:Q3V6T2}.
CC -!- DISRUPTION PHENOTYPE: CCDC88A knockout mice display mesial-temporal
CC lobe epilepsy and early demise, and structural brain developmental
CC defects affecting the corpus callosum and cerebrum.
CC {ECO:0000269|PubMed:26917597}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37020.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI24877.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB087827; BAD98263.1; -; mRNA.
DR EMBL; AL935054; CAI24877.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL935054; CAI24878.1; -; Genomic_DNA.
DR EMBL; BX284634; CAI24878.1; JOINED; Genomic_DNA.
DR EMBL; BX284634; CAI35999.1; -; Genomic_DNA.
DR EMBL; BX284634; CAI36000.1; -; Genomic_DNA.
DR EMBL; BX284634; CAI36001.1; -; Genomic_DNA.
DR EMBL; AL935054; CAI36001.1; JOINED; Genomic_DNA.
DR EMBL; BX284634; CAI36002.1; -; Genomic_DNA.
DR EMBL; BC037020; AAH37020.1; ALT_INIT; mRNA.
DR EMBL; AK082771; BAC38612.1; -; mRNA.
DR CCDS; CCDS24494.1; -. [Q5SNZ0-2]
DR RefSeq; NP_789811.2; NM_176841.4. [Q5SNZ0-2]
DR RefSeq; XP_006514518.1; XM_006514455.3. [Q5SNZ0-1]
DR AlphaFoldDB; Q5SNZ0; -.
DR SMR; Q5SNZ0; -.
DR BioGRID; 224370; 7.
DR IntAct; Q5SNZ0; 3.
DR STRING; 10090.ENSMUSP00000048978; -.
DR iPTMnet; Q5SNZ0; -.
DR PhosphoSitePlus; Q5SNZ0; -.
DR EPD; Q5SNZ0; -.
DR jPOST; Q5SNZ0; -.
DR MaxQB; Q5SNZ0; -.
DR PaxDb; Q5SNZ0; -.
DR PeptideAtlas; Q5SNZ0; -.
DR PRIDE; Q5SNZ0; -.
DR ProteomicsDB; 271329; -. [Q5SNZ0-1]
DR ProteomicsDB; 271330; -. [Q5SNZ0-2]
DR ProteomicsDB; 271331; -. [Q5SNZ0-3]
DR Antibodypedia; 47423; 255 antibodies from 33 providers.
DR DNASU; 108686; -.
DR Ensembl; ENSMUST00000040182; ENSMUSP00000048978; ENSMUSG00000032740. [Q5SNZ0-2]
DR GeneID; 108686; -.
DR KEGG; mmu:108686; -.
DR UCSC; uc007igw.2; mouse. [Q5SNZ0-2]
DR CTD; 55704; -.
DR MGI; MGI:1925177; Ccdc88a.
DR VEuPathDB; HostDB:ENSMUSG00000032740; -.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000155559; -.
DR HOGENOM; CLU_001421_1_0_1; -.
DR InParanoid; Q5SNZ0; -.
DR OMA; XEEKTEQ; -.
DR OrthoDB; 59187at2759; -.
DR PhylomeDB; Q5SNZ0; -.
DR TreeFam; TF320231; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 108686; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc88a; mouse.
DR PRO; PR:Q5SNZ0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SNZ0; protein.
DR Bgee; ENSMUSG00000032740; Expressed in rostral migratory stream and 249 other tissues.
DR ExpressionAtlas; Q5SNZ0; baseline and differential.
DR Genevisible; Q5SNZ0; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR027717; Girdin.
DR InterPro; IPR043936; HOOK_N.
DR PANTHER; PTHR18947:SF30; PTHR18947:SF30; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; DNA replication; Guanine-nucleotide releasing factor;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1873
FT /note="Girdin"
FT /id="PRO_0000287430"
FT DOMAIN 12..132
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 816..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1408
FT /note="Phosphoinositide-binding"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT REGION 1407..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1825
FT /note="SH2-like; required for interaction with growth
FT factor receptors"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT REGION 1738..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..425
FT /evidence="ECO:0000255"
FT COILED 458..1232
FT /evidence="ECO:0000255"
FT COILED 1268..1385
FT /evidence="ECO:0000255"
FT MOTIF 1674..1704
FT /note="GBA"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT COMPBIAS 1416..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1417
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1421
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1767
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1801
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT MOD_RES 1839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V6T2"
FT VAR_SEQ 1000..1054
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_052410"
FT VAR_SEQ 1463..1491
FT /note="MVALKRLPFLRNRPKDKDKMKACYRRSMS -> T (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15753085"
FT /id="VSP_052411"
FT CONFLICT 952
FT /note="Missing (in Ref. 2; CAI35999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1086..1089
FT /note="LQRQ -> PRVR (in Ref. 3; AAH37020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1873 AA; 215918 MW; 0E827E3D9336161F CRC64;
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ VMLQINPKSE
SQRVNKKVNN DASLRIHNLS ILVKQIKFYY QETLQQLIMM PLPDILIIGK NPFSEQGTEE
VKKLLLLLLG CAVQCQKKEE FIEKIQGLDF DTKAAVAAHI QEVTHNQENV FDLQWMEVTD
MSQEDIEPLL KNMVSHLRRL IDERDEHSET IVELSEERDG VHFLPHASSS AQSPCGSPGM
KRTESRQHLS VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQIEVELKR LQQENMNLLS
DARSARMYRD ELDALREKAV RVDKLESELS RYKERLHDIE FYKARVEELK EDNQVLLETK
TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM DRKKIEELME ENMTLEMAQK
QSMDESLHLG WELEQISRTS ELAEAPQKSL GHEVNELTSS KLLKLEMENQ SLTKTVEELR
STADSAAGST SKILKVEKEN QRLNKKVEIL ENEIIQEKQS LQNCQNLSKD LMKEKAQLEK
TIETLRENSE RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETC
GKLSKIEFEK RQMKKELELY KEKGERAEEL ENELNHLGKE NELLQKKITN LKITCEKLET
LEQENSELER ENRKFKKTLD SFKNLTFQLE SLEKENSQLD EENLELRRSV ESLKCASMRM
AQLQLENKEL ESEKEQLRKG LELMRASFKK TERLEVSYQG LDTENQRLQK ALENSNKKIQ
QLESELQDLE MENQTLQKSL EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR
LRQQAEIKDT TLEENNVKIG NLEKENKTLF KEINVYKESC VRLKELEKEN KELVKRATID
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD DSRYKLLESK
LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRHELKTV KKNYEALKQR QDEERMVQSS
IPVSGEDDKW GRESQEATRE LLKVKDRLIE VERNNATLQA EKQALKTQLK QLETQNNNLQ
AQILALQRQT VSLQEQNTTL QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE
SIMKEREDLK SLYDALIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHKDLED
RYNQLLKQKG QLEDLEKMIK TEQEKMLLES KNHEVVASEY KKLCGENDRL NYTYSQLLKE
TEILQMDHKN LKSVLNNSKL EQTRLEAEFS KLKEQYQQLD ITSTKLNNQC ELLSQLKGNL
EEENRHLLDQ IQTLMLQNRT LLEQNMESKD LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ
YKFYDPSPPR RRGNWITLKM RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ
DSSSVGSNSL EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV
LAGGQWTGST ENLEVPDDIS TGKRRKELGA MAFSTTAINF STVNSSAAFR SKQLVNNKDT
TSFEDISPQG ISDDSSTGSR VHASRPASLD SGRTSTSNSN NNASLHEVKA GAVNIQSRPQ
SHSSGDFSLL HDHETWSSSG SSPIQYLKRQ TRSSPMLQHK ISETIESRAH HKMKAGSPGS
EVVTLQQFLE ESNKLTSIQL KSSSQENLLD EVMKSLSVSS DFLGKDKPVS CTLARSVSGK
TPGDFYDRRT TKPEFLRTGP QKTEDAYTIS SAGKPTPSTQ GKIKLVKETS VSRQSKDSNP
YATLPRASSV ISTAEGTTRR TSIHDFLSKD SRLPVSVDSS PPTAGSSSTT ASNVNKVQES
RNSKSRSREQ QSS
