ID KALRN_MOUSE Reviewed; 2964 AA. AC A2CG49; A2CG50; A2CG51; A2CG52; A2CG53; B2RXR5; Q3TXY8; Q3TYL1; AC Q3UTA5; Q8BTT9; Q8C4Q2; Q9CVA9; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 14-OCT-2015, entry version 92. DE RecName: Full=Kalirin; 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RC NOD {ECO:0000312|EMBL:BAC40535.1}; RC TISSUE=Egg {ECO:0000312|EMBL:BAE24075.1}, RC Embryonic head {ECO:0000312|EMBL:BAC38239.1}, RC Stomach {ECO:0000312|EMBL:BAB25925.1}, RC Thymus {ECO:0000312|EMBL:BAC40535.1}, and RC Visual cortex {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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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 RP 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; RP SER-1789; THR-1881 AND THR-1884, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific CC Rho GTPase family members, thereby inducing various signaling CC mechanisms that regulate neuronal shape, growth, and plasticity, CC through their effects on the actin cytoskeleton. Induces CC lamellipodia independent of its GEF activity (By similarity). CC {ECO:0000250|UniProtKB:P97924}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {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). CC {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=9; CC Name=1; CC IsoId=A2CG49-1; Sequence=Displayed; CC Note=Produced by alternative splicing. {ECO:0000305}; CC Name=2; CC IsoId=A2CG49-2; Sequence=VSP_052576, VSP_052579; CC Note=Produced by alternative splicing. No experimental CC confirmation available. {ECO:0000305}; CC Name=3 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-3; Sequence=VSP_052562; CC Note=Produced by alternative splicing. No experimental CC confirmation available. {ECO:0000305}; 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 Note=Produced by alternative splicing. No experimental CC confirmation available. {ECO:0000305}; CC Name=5 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-5; Sequence=VSP_052564, VSP_052567, VSP_052568, CC VSP_052569; CC Note=Produced by alternative initiation at Met-624 of isoform 1. CC Inferred by similarity. Ref.1 (BAE34776) sequence is in conflict CC in position: 711:E->K. {ECO:0000305}; CC Name=6 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-6; Sequence=VSP_052563, VSP_052570, VSP_052573, CC VSP_052574, VSP_052575; CC Note=Produced by alternative splicing. No experimental CC confirmation available. {ECO:0000305}; CC Name=7 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-7; Sequence=VSP_052565, VSP_052572; CC Note=Produced by alternative splicing. {ECO:0000305}; CC Name=8 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-8; Sequence=VSP_052566, VSP_052567, VSP_052568, CC VSP_052569; CC Note=Produced by alternative splicing. No experimental CC confirmation available. {ECO:0000305}; CC Name=9 {ECO:0000269|PubMed:16141072}; CC IsoId=A2CG49-9; Sequence=VSP_052566, VSP_052568, VSP_052569; CC Note=Produced by alternative splicing. {ECO:0000305}; CC -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1 CC and RhoA which are bound by DH1 and DH2 respectively. The two GEF CC domains appear to play differing roles in neuronal development and CC axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting CC GEF activity only when in the presence of a PXXP peptide, CC suggesting that the SH3 domain/peptide interaction mediates CC binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1 CC activity (By similarity). {ECO:0000250|UniProtKB:P97924}. CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain. {ECO:0000255|PROSITE- CC ProRule:PRU00056}. CC -!- SIMILARITY: Contains 2 DH (DBL-homology) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00062}. CC -!- SIMILARITY: Contains 1 fibronectin type-III domain. CC {ECO:0000255|PROSITE-ProRule:PRU00316}. CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like) CC domain. {ECO:0000255}. CC -!- SIMILARITY: Contains 2 PH domains. {ECO:0000255|PROSITE- CC ProRule:PRU00145}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 2 SH3 domains. {ECO:0000255|PROSITE- CC ProRule:PRU00192}. CC -!- SIMILARITY: Contains 9 spectrin repeats. {ECO:0000255}. 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_006522382.2. [A2CG49-8] DR UniGene; Mm.82274; -. DR PDB; 1WFW; NMR; -; A=2295-2354. DR PDBsum; 1WFW; -. DR ProteinModelPortal; A2CG49; -. DR SMR; A2CG49; 1252-1555, 1618-1684, 1890-2219, 2296-2361. DR IntAct; A2CG49; 6. DR PhosphoSite; A2CG49; -. DR MaxQB; A2CG49; -. DR PaxDb; A2CG49; -. DR PRIDE; A2CG49; -. DR Ensembl; ENSMUST00000076810; ENSMUSP00000076088; ENSMUSG00000061751. [A2CG49-1] DR Ensembl; ENSMUST00000089655; ENSMUSP00000087084; ENSMUSG00000061751. [A2CG49-8] DR Ensembl; ENSMUST00000114953; ENSMUSP00000110603; ENSMUSG00000061751. [A2CG49-5] DR Ensembl; ENSMUST00000114954; ENSMUSP00000110604; ENSMUSG00000061751. [A2CG49-5] DR Ensembl; ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751. [A2CG49-9] 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 CTD; 8997; -. DR MGI; MGI:2685385; Kalrn. DR eggNOG; COG0515; -. DR GeneTree; ENSGT00760000119030; -. DR HOVERGEN; HBG108598; -. DR InParanoid; A2CG49; -. DR KO; K15048; -. DR OMA; GHSSELT; -. DR PhylomeDB; A2CG49; -. DR TreeFam; TF318080; -. DR Reactome; R-MMU-193648; NRAGE signals death through JNK. DR Reactome; R-MMU-194840; Rho GTPase cycle. 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 ChiTaRS; Kalrn; mouse. DR EvolutionaryTrace; A2CG49; -. DR NextBio; 412318; -. DR PRO; PR:A2CG49; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; A2CG49; -. DR CleanEx; MM_KALRN; -. DR ExpressionAtlas; A2CG49; baseline and differential. DR Genevisible; A2CG49; MM. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI. DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. DR Gene3D; 1.20.900.10; -; 2. DR Gene3D; 2.30.29.30; -; 2. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.40.525.10; -; 1. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR028569; Kalirin. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR011993; PH/PTB_dom. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR22826:SF49; PTHR22826:SF49; 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; PF00018; SH3_1; 1. DR Pfam; PF00435; Spectrin; 4. DR SMART; SM00060; FN3; 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; SSF48065; SSF48065; 2. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF49265; SSF49265; 1. DR SUPFAM; SSF50044; SSF50044; 2. DR SUPFAM; SSF52087; SSF52087; 1. DR SUPFAM; SSF56112; SSF56112; 1. 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; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Alternative splicing; KW ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; KW 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; KW SH3 domain; Transferase. FT CHAIN 1 2964 Kalirin. FT /FTId=PRO_0000308173. FT DOMAIN 17 162 CRAL-TRIO. {ECO:0000255|PROSITE- FT ProRule:PRU00056}. FT REPEAT 149 290 Spectrin 1. {ECO:0000255}. FT REPEAT 292 399 Spectrin 2. {ECO:0000255}. FT REPEAT 400 517 Spectrin 3. {ECO:0000255}. FT REPEAT 518 621 Spectrin 4. {ECO:0000255}. FT REPEAT 622 752 Spectrin 5. {ECO:0000255}. FT REPEAT 753 870 Spectrin 6. {ECO:0000255}. FT REPEAT 871 977 Spectrin 7. {ECO:0000255}. FT REPEAT 978 1101 Spectrin 8. {ECO:0000255}. FT REPEAT 1102 1207 Spectrin 9. {ECO:0000255}. FT DOMAIN 1254 1429 DH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00062}. FT DOMAIN 1441 1553 PH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT DOMAIN 1619 1684 SH3 1. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT DOMAIN 1900 2075 DH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00062}. FT DOMAIN 2087 2197 PH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT DOMAIN 2292 2357 SH3 2. {ECO:0000255|PROSITE- FT ProRule:PRU00192}. FT DOMAIN 2443 2536 Ig-like C2-type. {ECO:0000255}. FT DOMAIN 2543 2637 Fibronectin type-III. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 2656 2910 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 2662 2670 ATP. {ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159}. FT COMPBIAS 664 669 Poly-Gln. {ECO:0000255}. FT ACT_SITE 2775 2775 Proton acceptor. FT {ECO:0000250|UniProtKB:P28523, FT ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027}. FT BINDING 2685 2685 ATP. {ECO:0000250|UniProtKB:O60229, FT ECO:0000255|PROSITE-ProRule:PRU00159}. FT MOD_RES 1722 1722 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 1725 1725 Phosphoserine. FT {ECO:0000250|UniProtKB:O60229}. FT MOD_RES 1771 1771 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 1784 1784 Phosphothreonine. FT {ECO:0000250|UniProtKB:P97924}. FT MOD_RES 1789 1789 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1881 1881 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 1884 1884 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 2233 2233 Phosphoserine. FT {ECO:0000250|UniProtKB:O60229}. FT DISULFID 2464 2520 {ECO:0000250|UniProtKB:O60229, FT ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 1 2731 Missing (in isoform 3). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052562. FT VAR_SEQ 1 1669 Missing (in isoform 4 and isoform 6). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052563. FT VAR_SEQ 1 623 Missing (in isoform 5). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052564. FT VAR_SEQ 1 4 MVLS -> MNPPEGASEEGGAADSDVDAFFRT (in FT isoform 7). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052565. FT VAR_SEQ 1 4 MVLS -> MTDRFWDQWYLWYLRLLRLLDR (in FT isoform 8 and isoform 9). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052566. FT VAR_SEQ 923 923 E -> ESLFHATSLQ (in isoform 5 and isoform FT 8). {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052567. FT VAR_SEQ 1617 1636 LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFS FT TYV (in isoform 5, isoform 8 and isoform FT 9). {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052568. FT VAR_SEQ 1637 2964 Missing (in isoform 5, isoform 8 and FT isoform 9). {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052569. FT VAR_SEQ 1670 1697 QEGLVPSSALCISHSRSSVEMDCFFPLK -> MKGGDQAYT FT RGPSLGWLFAKCCCCFPCR (in isoform 4 and FT isoform 6). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052570. FT VAR_SEQ 1828 1858 Missing (in isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052571. FT VAR_SEQ 1859 1898 TLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKAL FT -> VSGHAGGSSELPLTSVWLPGPQPGPRTGLPHPNFTNRN FT CI (in isoform 7). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052572. FT VAR_SEQ 2285 2285 Missing (in isoform 4 and isoform 6). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052573. FT VAR_SEQ 2357 2364 KATAAAES -> QSQSRGRK (in isoform 6). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052574. FT VAR_SEQ 2365 2964 Missing (in isoform 6). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052575. FT VAR_SEQ 2371 2375 KSCSW -> TLLKP (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052576. FT VAR_SEQ 2372 2374 SCS -> EPY (in isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052577. FT VAR_SEQ 2375 2964 Missing (in isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052578. FT VAR_SEQ 2376 2964 Missing (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_052579. FT CONFLICT 1824 1824 Q -> H (in Ref. 1; BAC40535). FT {ECO:0000305}. FT CONFLICT 2316 2316 G -> S (in Ref. 1; BAB25925). FT {ECO:0000305}. FT CONFLICT 2344 2344 E -> K (in Ref. 1; BAB25925). FT {ECO:0000305}. FT CONFLICT 2355 2355 L -> F (in Ref. 1; BAB25925). FT {ECO:0000305}. FT STRAND 2296 2298 {ECO:0000244|PDB:1WFW}. FT STRAND 2307 2309 {ECO:0000244|PDB:1WFW}. FT STRAND 2318 2324 {ECO:0000244|PDB:1WFW}. FT STRAND 2328 2334 {ECO:0000244|PDB:1WFW}. FT STRAND 2338 2348 {ECO:0000244|PDB:1WFW}. FT HELIX 2349 2351 {ECO:0000244|PDB:1WFW}. 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 //