ID KALRN_MOUSE Reviewed; 2964 AA. AC A2CG49; A2CG50; A2CG51; A2CG52; A2CG53; B2RXR5; D3Z559; Q3TXY8; Q3TYL1; AC Q3UTA5; Q8BTT9; Q8C4Q2; Q9CVA9; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 24-JAN-2024, entry version 148. DE RecName: Full=Kalirin {ECO:0000250|UniProtKB:P97924}; DE EC=2.7.11.1; DE AltName: Full=Protein Duo; DE AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain; GN Name=Kalrn {ECO:0000312|MGI:MGI:2685385}; 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:BAB25925.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2964 (ISOFORM 2). RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25925.1}, and NOD RC {ECO:0000312|EMBL:BAC40535.1}; RC TISSUE=Egg {ECO:0000312|EMBL:BAE24075.1}, Embryonic head RC {ECO:0000312|EMBL:BAC38239.1}, Stomach {ECO:0000312|EMBL:BAB25925.1}, RC Thymus {ECO:0000312|EMBL:BAC40535.1}, and Visual cortex RC {ECO:0000312|EMBL:BAE34552.1}; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9). RC TISSUE=Brain; 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:0000312|EMBL:CAM18305.1} RP PROTEIN SEQUENCE OF 2034-2042, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722 AND SER-1771, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722; SER-1771; SER-1789; RP THR-1881 AND THR-1884, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen; 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: Promotes the exchange of GDP by GTP. Activates specific Rho CC GTPase family members, thereby inducing various signaling mechanisms CC that regulate neuronal shape, growth, and plasticity, through their CC effects on the actin cytoskeleton. Induces lamellipodia independent of CC its GEF activity (By similarity). {ECO:0000250|UniProtKB:P97924}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000250|UniProtKB:O60229}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O60229}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:O60229}; CC -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha- CC amidating monooxygenase (PAM) and with the huntingtin-associated CC protein 1 (HAP1). Interacts with FASLG (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60229, CC ECO:0000250|UniProtKB:P97924}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=10; CC Name=1; Synonyms=Kalirin-12A {ECO:0000250|UniProtKB:P97924}; CC IsoId=A2CG49-1; Sequence=Displayed; CC Name=2; Synonyms=Kalirin-9A {ECO:0000250|UniProtKB:P97924}; CC IsoId=A2CG49-2; Sequence=VSP_052576, VSP_052579; CC Name=3 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-3; Sequence=VSP_052562; CC Name=4 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-4; Sequence=VSP_052563, VSP_052570, VSP_052571, CC VSP_052573, VSP_052577, VSP_052578; CC Name=5 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-5; Sequence=VSP_052564, VSP_052567, VSP_052568, CC VSP_052569; CC Name=6 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-6; Sequence=VSP_052563, VSP_052570, VSP_052573, CC VSP_052574, VSP_052575; CC Name=7 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-7; Sequence=VSP_052565, VSP_052572; CC Name=8 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-8; Sequence=VSP_052566, VSP_052567, VSP_052568, CC VSP_052569; CC Name=9 {ECO:0000269|PubMed:16141072}; Synonyms=Kalirin-7c CC {ECO:0000250|UniProtKB:P97924}; CC IsoId=A2CG49-9; Sequence=VSP_052566, VSP_052568, VSP_052569; CC Name=10; Synonyms=Delta Kalirin-7 {ECO:0000250|UniProtKB:P97924}; CC IsoId=A2CG49-10; Sequence=VSP_052564, VSP_052568, VSP_052569; CC -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1 and CC RhoA which are bound by DH1 and DH2 respectively. The two GEF domains CC appear to play differing roles in neuronal development and axonal CC outgrowth. SH3 1 binds to the first GEF domain inhibiting GEF activity CC only when in the presence of a PXXP peptide, suggesting that the SH3 CC domain/peptide interaction mediates binding to GEF1. CRK1 SH3 domain CC binds to and inhibits GEF1 activity (By similarity). CC {ECO:0000250|UniProtKB:P97924}. CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative initiation at Met- CC 624 of isoform 1. Inferred by similarity. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK008844; BAB25925.1; -; mRNA. DR EMBL; AK081504; BAC38239.1; -; mRNA. DR EMBL; AK088732; BAC40535.1; -; mRNA. DR EMBL; AK139581; BAE24075.1; -; mRNA. DR EMBL; AK158544; BAE34552.1; -; mRNA. DR EMBL; AK159031; BAE34776.1; -; mRNA. DR EMBL; CT010573; CAM18305.1; -; Genomic_DNA. DR EMBL; AC154524; CAM18305.1; JOINED; Genomic_DNA. DR EMBL; AC155257; CAM18305.1; JOINED; Genomic_DNA. DR EMBL; AC165079; CAM18305.1; JOINED; Genomic_DNA. DR EMBL; CT010573; CAM18306.1; -; Genomic_DNA. DR EMBL; AC154524; CAM18306.1; JOINED; Genomic_DNA. DR EMBL; AC165079; CAM18306.1; JOINED; Genomic_DNA. DR EMBL; CT010573; CAM18307.1; -; Genomic_DNA. DR EMBL; AC154524; CAM18307.1; JOINED; Genomic_DNA. DR EMBL; AC154588; CAM18307.1; JOINED; Genomic_DNA. DR EMBL; CT010573; CAM18308.1; -; Genomic_DNA. DR EMBL; AC154524; CAM18308.1; JOINED; Genomic_DNA. DR EMBL; AC154588; CAM18308.1; JOINED; Genomic_DNA. DR EMBL; CT010573; CAM18309.1; -; Genomic_DNA. DR EMBL; AC154524; CAM18309.1; JOINED; Genomic_DNA. DR EMBL; AC154588; CAM18309.1; JOINED; Genomic_DNA. DR EMBL; BC157950; AAI57951.1; -; mRNA. DR EMBL; BC172101; AAI72101.1; -; mRNA. DR CCDS; CCDS49836.1; -. [A2CG49-9] DR RefSeq; NP_001157740.1; NM_001164268.1. [A2CG49-9] DR RefSeq; XP_006522445.1; XM_006522382.3. [A2CG49-8] DR PDB; 1WFW; NMR; -; A=2295-2354. DR PDB; 7UR2; X-ray; 1.89 A; A/B/C/D/E/F/G/H=4-172. DR PDBsum; 1WFW; -. DR PDBsum; 7UR2; -. DR SMR; A2CG49; -. DR BioGRID; 244011; 61. DR IntAct; A2CG49; 62. DR MINT; A2CG49; -. DR STRING; 10090.ENSMUSP00000110611; -. DR GlyGen; A2CG49; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A2CG49; -. DR PhosphoSitePlus; A2CG49; -. DR SwissPalm; A2CG49; -. DR MaxQB; A2CG49; -. DR PaxDb; 10090-ENSMUSP00000110611; -. DR PeptideAtlas; A2CG49; -. DR ProteomicsDB; 301718; -. [A2CG49-1] DR ProteomicsDB; 301719; -. [A2CG49-2] DR ProteomicsDB; 301720; -. [A2CG49-3] DR ProteomicsDB; 301721; -. [A2CG49-4] DR ProteomicsDB; 301722; -. [A2CG49-5] DR ProteomicsDB; 301723; -. [A2CG49-6] DR ProteomicsDB; 301724; -. [A2CG49-7] DR ProteomicsDB; 301725; -. [A2CG49-8] DR ProteomicsDB; 301726; -. [A2CG49-9] DR ProteomicsDB; 301727; -. [A2CG49-10] DR Pumba; A2CG49; -. DR Antibodypedia; 2142; 205 antibodies from 34 providers. DR DNASU; 545156; -. DR Ensembl; ENSMUST00000076810.12; ENSMUSP00000076088.6; ENSMUSG00000061751.17. [A2CG49-1] DR Ensembl; ENSMUST00000089655.12; ENSMUSP00000087084.6; ENSMUSG00000061751.17. [A2CG49-8] DR Ensembl; ENSMUST00000114949.8; ENSMUSP00000110599.2; ENSMUSG00000061751.17. [A2CG49-10] DR Ensembl; ENSMUST00000114953.8; ENSMUSP00000110603.2; ENSMUSG00000061751.17. [A2CG49-5] DR Ensembl; ENSMUST00000114954.8; ENSMUSP00000110604.2; ENSMUSG00000061751.17. [A2CG49-5] DR Ensembl; ENSMUST00000114960.9; ENSMUSP00000110611.3; ENSMUSG00000061751.17. [A2CG49-9] DR Ensembl; ENSMUST00000232157.2; ENSMUSP00000156147.2; ENSMUSG00000061751.17. [A2CG49-4] DR GeneID; 545156; -. DR KEGG; mmu:545156; -. DR UCSC; uc007zar.2; mouse. [A2CG49-3] DR UCSC; uc007zas.1; mouse. [A2CG49-6] DR UCSC; uc007zat.1; mouse. [A2CG49-4] DR UCSC; uc007zav.1; mouse. [A2CG49-5] DR UCSC; uc007zax.2; mouse. [A2CG49-9] DR UCSC; uc012aew.1; mouse. [A2CG49-1] DR AGR; MGI:2685385; -. DR CTD; 8997; -. DR MGI; MGI:2685385; Kalrn. DR VEuPathDB; HostDB:ENSMUSG00000061751; -. DR eggNOG; KOG4240; Eukaryota. DR GeneTree; ENSGT00940000155248; -. DR InParanoid; A2CG49; -. DR OMA; AKXFIMA; -. DR OrthoDB; 2906033at2759; -. DR PhylomeDB; A2CG49; -. DR TreeFam; TF318080; -. DR Reactome; R-MMU-193648; NRAGE signals death through JNK. DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-416482; G alpha (12/13) signalling events. DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013408; RHOG GTPase cycle. DR BioGRID-ORCS; 545156; 4 hits in 81 CRISPR screens. DR ChiTaRS; Kalrn; mouse. DR EvolutionaryTrace; A2CG49; -. DR PRO; PR:A2CG49; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; A2CG49; Protein. DR Bgee; ENSMUSG00000061751; Expressed in cingulate cortex and 248 other cell types or tissues. DR ExpressionAtlas; A2CG49; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:0098793; C:presynapse; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0007409; P:axonogenesis; ISO:MGI. DR GO; GO:0046959; P:habituation; IMP:MGI. DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI. DR GO; GO:0007595; P:lactation; IMP:MGI. DR GO; GO:0042711; P:maternal behavior; IMP:MGI. DR GO; GO:0060137; P:maternal process involved in parturition; IMP:MGI. DR GO; GO:0007613; P:memory; IMP:MGI. DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:MGI. DR GO; GO:0060125; P:negative regulation of growth hormone secretion; IMP:MGI. DR GO; GO:0007399; P:nervous system development; ISO:MGI. DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI. DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI. DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; ISO:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:MGI. DR GO; GO:0050773; P:regulation of dendrite development; ISO:MGI. DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI. DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI. DR GO; GO:0035176; P:social behavior; IMP:MGI. DR CDD; cd00063; FN3; 1. DR CDD; cd13240; PH1_Kalirin_Trio_like; 1. DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1. DR CDD; cd00160; RhoGEF; 2. DR CDD; cd00170; SEC14; 1. DR CDD; cd11852; SH3_Kalirin_1; 1. DR CDD; cd11853; SH3_Kalirin_2; 1. DR CDD; cd00176; SPEC; 5. DR CDD; cd14115; STKc_Kalirin_C; 1. DR Gene3D; 1.20.58.60; -; 5. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR036865; CRAL-TRIO_dom_sf. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR047054; Kalirin_TRIO_PH_1. DR InterPro; IPR028570; Kalirin_TRIO_SH3_1. DR InterPro; IPR047053; Kalirin_TRIO_SH3_2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR22826:SF49; KALIRIN; 1. DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1. DR Pfam; PF13716; CRAL_TRIO_2; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00621; RhoGEF; 2. DR Pfam; PF16609; SH3-RhoG_link; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF00435; Spectrin; 4. DR SMART; SM00060; FN3; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00325; RhoGEF; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00516; SEC14; 1. DR SMART; SM00326; SH3; 2. DR SMART; SM00150; SPEC; 7. DR SUPFAM; SSF52087; CRAL/TRIO domain; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF50729; PH domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50044; SH3-domain; 2. DR SUPFAM; SSF46966; Spectrin repeat; 6. DR PROSITE; PS50191; CRAL_TRIO; 1. DR PROSITE; PS50010; DH_2; 2. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50002; SH3; 2. DR Genevisible; A2CG49; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Alternative splicing; ATP-binding; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond; KW Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain; KW Transferase. FT CHAIN 1..2964 FT /note="Kalirin" FT /id="PRO_0000308173" FT DOMAIN 17..162 FT /note="CRAL-TRIO" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056" FT REPEAT 149..290 FT /note="Spectrin 1" FT /evidence="ECO:0000255" FT REPEAT 292..399 FT /note="Spectrin 2" FT /evidence="ECO:0000255" FT REPEAT 400..517 FT /note="Spectrin 3" FT /evidence="ECO:0000255" FT REPEAT 518..621 FT /note="Spectrin 4" FT /evidence="ECO:0000255" FT REPEAT 622..752 FT /note="Spectrin 5" FT /evidence="ECO:0000255" FT REPEAT 753..870 FT /note="Spectrin 6" FT /evidence="ECO:0000255" FT REPEAT 871..977 FT /note="Spectrin 7" FT /evidence="ECO:0000255" FT REPEAT 978..1101 FT /note="Spectrin 8" FT /evidence="ECO:0000255" FT REPEAT 1102..1207 FT /note="Spectrin 9" FT /evidence="ECO:0000255" FT DOMAIN 1254..1429 FT /note="DH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 1441..1553 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 1619..1684 FT /note="SH3 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 1900..2075 FT /note="DH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 2087..2197 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 2292..2357 FT /note="SH3 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 2443..2536 FT /note="Ig-like C2-type" FT /evidence="ECO:0000255" FT DOMAIN 2543..2637 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 2656..2910 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 692..717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1568..1615 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1700..1825 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1869..1888 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2215..2285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2384..2426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 703..717 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1590..1615 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1700..1745 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1754..1776 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1785..1809 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2257..2271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2384..2406 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2775 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027" FT BINDING 2662..2670 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 2685 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:O60229, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1722 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1725 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60229" FT MOD_RES 1771 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1784 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P97924" FT MOD_RES 1789 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1881 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1884 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2233 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60229" FT DISULFID 2464..2520 FT /evidence="ECO:0000250|UniProtKB:O60229, FT ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..2731 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052562" FT VAR_SEQ 1..1669 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052563" FT VAR_SEQ 1..623 FT /note="Missing (in isoform 5 and isoform 10)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052564" FT VAR_SEQ 1..4 FT /note="MVLS -> MNPPEGASEEGGAADSDVDAFFRT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052565" FT VAR_SEQ 1..4 FT /note="MVLS -> MTDRFWDQWYLWYLRLLRLLDR (in isoform 8 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_052566" FT VAR_SEQ 923 FT /note="E -> ESLFHATSLQ (in isoform 5 and isoform 8)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052567" FT VAR_SEQ 1617..1636 FT /note="LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFSTYV (in FT isoform 5, isoform 8, isoform 9 and isoform 10)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_052568" FT VAR_SEQ 1637..2964 FT /note="Missing (in isoform 5, isoform 8, isoform 9 and FT isoform 10)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_052569" FT VAR_SEQ 1670..1697 FT /note="QEGLVPSSALCISHSRSSVEMDCFFPLK -> MKGGDQAYTRGPSLGWLFAK FT CCCCFPCR (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052570" FT VAR_SEQ 1828..1858 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052571" FT VAR_SEQ 1859..1898 FT /note="TLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKAL -> VSGHAGGS FT SELPLTSVWLPGPQPGPRTGLPHPNFTNRNCI (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052572" FT VAR_SEQ 2285 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052573" FT VAR_SEQ 2357..2364 FT /note="KATAAAES -> QSQSRGRK (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052574" FT VAR_SEQ 2365..2964 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052575" FT VAR_SEQ 2371..2375 FT /note="KSCSW -> TLLKP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052576" FT VAR_SEQ 2372..2374 FT /note="SCS -> EPY (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052577" FT VAR_SEQ 2375..2964 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052578" FT VAR_SEQ 2376..2964 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_052579" FT CONFLICT 1824 FT /note="Q -> H (in Ref. 1; BAC40535)" FT /evidence="ECO:0000305" FT CONFLICT 2316 FT /note="G -> S (in Ref. 1; BAB25925)" FT /evidence="ECO:0000305" FT CONFLICT 2344 FT /note="E -> K (in Ref. 1; BAB25925)" FT /evidence="ECO:0000305" FT CONFLICT 2355 FT /note="L -> F (in Ref. 1; BAB25925)" FT /evidence="ECO:0000305" FT STRAND 2296..2298 FT /evidence="ECO:0007829|PDB:1WFW" FT STRAND 2307..2309 FT /evidence="ECO:0007829|PDB:1WFW" FT STRAND 2318..2324 FT /evidence="ECO:0007829|PDB:1WFW" FT STRAND 2328..2334 FT /evidence="ECO:0007829|PDB:1WFW" FT STRAND 2338..2348 FT /evidence="ECO:0007829|PDB:1WFW" FT HELIX 2349..2351 FT /evidence="ECO:0007829|PDB:1WFW" FT CONFLICT A2CG49-5:711 FT /note="E -> K (in Ref. 1; BAE34776)" FT /evidence="ECO:0000305" SQ SEQUENCE 2964 AA; 337000 MW; 76064FE06AA2BD9C CRC64; MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEVLEDV CADSVDAVQE LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP TEARDSAMSN NKTPHSSSIS HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDLDLA AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL QAGHYDADAI RECAEKVALH WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEMDH VIPLLSKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEYYLSTH TSTGETTEET QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEINEEKRK SARKKEFIMA ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI SSYLIKPVQR VTKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK GALKEPIQLP KTPAKLRNNS KRDGVEDGDS QGDGSSQPDT ISIASRTSQN TVESDKLSGG CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSALC ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ PSLNSIHSSP GPKRSTNTLK KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE DEPDEESHTP LPPPMKIFDN DPTQDEMSSL LAARQAPPDV PTAADLVSAI EKLVKNKLTL EGGSYRGSLK DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG IVVEGFMKRI EEKGVPEDMR GKEKIVFGNI HQIYDWHKDF FLAELEKCIQ EQDRLAQLFI KHERKLHIYV WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL LKDFLRYSEK AGLECSDIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF YVIELDAGMQ SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEDNVDGD PCKFALMNRE TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA VIRSQPPRVP QASPRPYSSG PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF DASKQNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS PAAEGWVPGS ILAPLAKATA AAESSDGSIK KSCSWHTLRM RKRADVENSG KNEATGPRKP KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVRLPEYDAA ADGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK MKKKEQAAHE AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE KVAFYIRDIM EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH HLLGNPEFAA PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPHEYFCGVS NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF IERRKHQNDV RPIPNVKSYI VNRVNQGTSL SHNP //