GRP2_MOUSE
ID GRP2_MOUSE Reviewed; 608 AA.
AC Q9QUG9; O09004; Q80WC0; Q8BSC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=RAS guanyl-releasing protein 2;
DE AltName: Full=Calcium and DAG-regulated guanine nucleotide exchange factor I;
DE Short=CalDAG-GEFI;
DE AltName: Full=F25B3.3 kinase-like protein;
GN Name=Rasgrp2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A RAP ACTIVATOR.
RX PubMed=9789079; DOI=10.1073/pnas.95.22.13278;
RA Kawasaki H., Springett G.M., Toki S., Canales J.J., Harlan P.,
RA Blumenstiel J.P., Chen E.J., Bany I.A., Mochizuki N., Ashbacher A.,
RA Matsuda M., Housman D.E., Graybiel A.M.;
RT "A Rap guanine nucleotide exchange factor enriched highly in the basal
RT ganglia.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13278-13283(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-608 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 349-608 (ISOFORM 1).
RX PubMed=9341881; DOI=10.1007/s004390050562;
RA Kedra D., Seroussi E., Fransson I., Trifunovic J., Clark M.,
RA Lagercrantz J., Blennow E., Mehlin H., Dumanski J.;
RT "The germinal centre kinase gene and a novel CDC25-like gene are located in
RT the vicinity of the PYGM gene on 11q13.";
RL Hum. Genet. 100:611-619(1997).
RN [5]
RP FUNCTION.
RX PubMed=10777492; DOI=10.1074/jbc.m000981200;
RA Ohba Y., Mochizuki N., Yamashita S., Chan A.M., Schrader J.W., Hattori S.,
RA Nagashima K., Matsuda M.;
RT "Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3.";
RL J. Biol. Chem. 275:20020-20026(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10835426; DOI=10.1074/jbc.m003414200;
RA Yamashita S., Mochizuki N., Ohba Y., Tobiume M., Okada Y., Sawa H.,
RA Nagashima K., Matsuda M.;
RT "CalDAG-GEFIII activation of Ras, R-ras, and Rap1.";
RL J. Biol. Chem. 275:25488-25493(2000).
RN [7]
RP FUNCTION AS RAP2 ACTIVATOR.
RX PubMed=10913189; DOI=10.1128/mcb.20.16.6074-6083.2000;
RA Ohba Y., Mochizuki N., Matsuo K., Yamashita S., Nakaya M., Hashimoto Y.,
RA Hamaguchi M., Kurata T., Nagashima K., Matsuda M.;
RT "Rap2 as a slowly responding molecular switch in the Rap1 signaling
RT cascade.";
RL Mol. Cell. Biol. 20:6074-6083(2000).
RN [8]
RP FUNCTION.
RX PubMed=11432821; DOI=10.1093/emboj/20.13.3333;
RA Ohba Y., Ikuta K., Ogura A., Matsuda J., Mochizuki N., Nagashima K.,
RA Kurokawa K., Mayer B.J., Maki K., Miyazaki J., Matsuda M.;
RT "Requirement for C3G-dependent Rap1 activation for cell adhesion and
RT embryogenesis.";
RL EMBO J. 20:3333-3341(2001).
RN [9]
RP FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11278453; DOI=10.1074/jbc.m008970200;
RA Dupuy A.J., Morgan K., von Lintig F.C., Shen H., Acar H., Hasz D.E.,
RA Jenkins N.A., Copeland N.G., Boss G.R., Largaespada D.A.;
RT "Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF I, in
RT BXH-2 murine myeloid leukemia.";
RL J. Biol. Chem. 276:11804-11811(2001).
RN [10]
RP FUNCTION.
RX PubMed=12239348; DOI=10.1073/pnas.202380099;
RA Eto K., Murphy R., Kerrigan S.W., Bertoni A., Stuhlmann H., Nakano T.,
RA Leavitt A.D., Shattil S.J.;
RT "Megakaryocytes derived from embryonic stem cells implicate CalDAG-GEFI in
RT integrin signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12819-12824(2002).
RN [11]
RP FUNCTION IN PLATELET AGGREGATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP RAP1, AND TISSUE SPECIFICITY.
RX PubMed=15334074; DOI=10.1038/nm1098;
RA Crittenden J.R., Bergmeier W., Zhang Y., Piffath C.L., Liang Y.,
RA Wagner D.D., Housman D.E., Graybiel A.M.;
RT "CalDAG-GEFI integrates signaling for platelet aggregation and thrombus
RT formation.";
RL Nat. Med. 10:982-986(2004).
RN [12]
RP FUNCTION.
RX PubMed=16357324; DOI=10.1182/blood-2005-07-3023;
RA Bernardi B., Guidetti G.F., Campus F., Crittenden J.R., Graybiel A.M.,
RA Balduini C., Torti M.;
RT "The small GTPase Rap1b regulates the cross talk between platelet integrin
RT alpha2beta1 and integrin alphaIIbbeta3.";
RL Blood 107:2728-2735(2006).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17492052; DOI=10.1172/jci30575;
RA Bergmeier W., Goerge T., Wang H.-W., Crittenden J.R., Baldwin A.C.W.,
RA Cifuni S.M., Housman D.E., Graybiel A.M., Wagner D.D.;
RT "Mice lacking the signaling molecule CalDAG-GEFI represent a model for
RT leukocyte adhesion deficiency type III.";
RL J. Clin. Invest. 117:1699-1707(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-117, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-117; SER-147 AND
RP SER-554, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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: Functions as a calcium- and DAG-regulated nucleotide exchange
CC factor specifically activating Rap through the exchange of bound GDP
CC for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS,
CC KRAS but not HRAS. Functions in aggregation of platelets and adhesion
CC of T-lymphocytes and neutrophils probably through inside-out integrin
CC activation. May function in the muscarinic acetylcholine receptor
CC M1/CHRM1 signaling pathway. {ECO:0000269|PubMed:10777492,
CC ECO:0000269|PubMed:10913189, ECO:0000269|PubMed:11278453,
CC ECO:0000269|PubMed:11432821, ECO:0000269|PubMed:12239348,
CC ECO:0000269|PubMed:15334074, ECO:0000269|PubMed:16357324,
CC ECO:0000269|PubMed:17492052, ECO:0000269|PubMed:9789079}.
CC -!- SUBUNIT: Forms a signaling complex with RAP1 and BRAF. Interacts with
CC F-actin (By similarity). Interacts with RAP1. {ECO:0000250,
CC ECO:0000269|PubMed:15334074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}. Cell projection, ruffle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Found
CC both in the cytosol and associated with membranes. Enriched at
CC juxtamembrane areas and membrane ruffles. Localizes to the cell bodies
CC and axons of striatal neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CalDAG-GEF1a;
CC IsoId=Q9QUG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QUG9-2; Sequence=VSP_030579;
CC Name=3; Synonyms=CalDAG-GEF1b;
CC IsoId=Q9QUG9-3; Sequence=VSP_030577, VSP_030578;
CC -!- TISSUE SPECIFICITY: Detected in megakaryocytes, platelet and
CC neutrophils but not in lymphocytes (at protein level). Isoform 1 and
CC isoform 3 are detected in brain basal glanglia, heart, lung, spleen,
CC liver and kidney interstitial cells. {ECO:0000269|PubMed:10835426,
CC ECO:0000269|PubMed:11278453, ECO:0000269|PubMed:15334074}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo with higher expression between
CC 15 dpc and 17 dpc. {ECO:0000269|PubMed:11278453}.
CC -!- DOMAIN: The N-terminal Ras-GEF domain mediates association with F-
CC actin. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice have a combination of defects in leukocytes
CC and platelet functions which are reminiscent of the human leukocyte
CC adhesion deficiency type III syndrome (LAD3). They display bleeding
CC diathesis due to a defect in platelet aggregation and are resistant to
CC collagen-induced thrombosis. In parallel, they also display impaired
CC response to acute inflammation associated with defects in beta-1 and
CC beta-2 integrin-mediated adhesion of neutrophils.
CC {ECO:0000269|PubMed:15334074, ECO:0000269|PubMed:17492052}.
CC -!- MISCELLANEOUS: [Isoform 3]: The corresponding protein is not
CC undetectable. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF081193; AAC79697.1; -; mRNA.
DR EMBL; U78171; AAD12742.1; -; mRNA.
DR EMBL; BC051474; AAH51474.1; -; mRNA.
DR EMBL; AK034683; BAC28797.1; ALT_INIT; mRNA.
DR EMBL; Y12339; CAA73008.1; -; mRNA.
DR CCDS; CCDS37898.1; -. [Q9QUG9-1]
DR CCDS; CCDS89325.1; -. [Q9QUG9-3]
DR RefSeq; NP_035372.2; NM_011242.2. [Q9QUG9-1]
DR RefSeq; XP_006531748.1; XM_006531685.3. [Q9QUG9-1]
DR RefSeq; XP_006531749.1; XM_006531686.3. [Q9QUG9-1]
DR RefSeq; XP_006531750.1; XM_006531687.2. [Q9QUG9-1]
DR RefSeq; XP_006531751.1; XM_006531688.3. [Q9QUG9-1]
DR RefSeq; XP_006531752.1; XM_006531689.3. [Q9QUG9-1]
DR RefSeq; XP_006531753.1; XM_006531690.3. [Q9QUG9-1]
DR RefSeq; XP_006531754.1; XM_006531691.3. [Q9QUG9-1]
DR AlphaFoldDB; Q9QUG9; -.
DR BMRB; Q9QUG9; -.
DR SMR; Q9QUG9; -.
DR IntAct; Q9QUG9; 1.
DR MINT; Q9QUG9; -.
DR STRING; 10090.ENSMUSP00000109104; -.
DR iPTMnet; Q9QUG9; -.
DR PhosphoSitePlus; Q9QUG9; -.
DR EPD; Q9QUG9; -.
DR jPOST; Q9QUG9; -.
DR MaxQB; Q9QUG9; -.
DR PaxDb; Q9QUG9; -.
DR PeptideAtlas; Q9QUG9; -.
DR PRIDE; Q9QUG9; -.
DR ProteomicsDB; 271334; -. [Q9QUG9-1]
DR ProteomicsDB; 271335; -. [Q9QUG9-2]
DR ProteomicsDB; 271336; -. [Q9QUG9-3]
DR Antibodypedia; 2786; 138 antibodies from 27 providers.
DR DNASU; 19395; -.
DR Ensembl; ENSMUST00000035716; ENSMUSP00000041135; ENSMUSG00000032946. [Q9QUG9-1]
DR Ensembl; ENSMUST00000113471; ENSMUSP00000109099; ENSMUSG00000032946. [Q9QUG9-3]
DR Ensembl; ENSMUST00000113472; ENSMUSP00000109100; ENSMUSG00000032946. [Q9QUG9-3]
DR Ensembl; ENSMUST00000113475; ENSMUSP00000109103; ENSMUSG00000032946. [Q9QUG9-3]
DR Ensembl; ENSMUST00000113476; ENSMUSP00000109104; ENSMUSG00000032946. [Q9QUG9-1]
DR Ensembl; ENSMUST00000167240; ENSMUSP00000129873; ENSMUSG00000032946. [Q9QUG9-1]
DR GeneID; 19395; -.
DR KEGG; mmu:19395; -.
DR UCSC; uc008gip.1; mouse. [Q9QUG9-1]
DR UCSC; uc008gir.1; mouse. [Q9QUG9-2]
DR CTD; 10235; -.
DR MGI; MGI:1333849; Rasgrp2.
DR VEuPathDB; HostDB:ENSMUSG00000032946; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000160483; -.
DR HOGENOM; CLU_019261_1_0_1; -.
DR InParanoid; Q9QUG9; -.
DR OMA; PPVLDEW; -.
DR OrthoDB; 355412at2759; -.
DR PhylomeDB; Q9QUG9; -.
DR TreeFam; TF312918; -.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR BioGRID-ORCS; 19395; 0 hits in 70 CRISPR screens.
DR PRO; PR:Q9QUG9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9QUG9; protein.
DR Bgee; ENSMUSG00000032946; Expressed in granulocyte and 59 other tissues.
DR ExpressionAtlas; Q9QUG9; baseline and differential.
DR Genevisible; Q9QUG9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome; Zinc;
KW Zinc-finger.
FT CHAIN 1..608
FT /note="RAS guanyl-releasing protein 2"
FT /id="PRO_0000315609"
FT DOMAIN 4..126
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 154..387
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 426..461
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 463..490
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT ZN_FING 498..548
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 382..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C643"
FT VAR_SEQ 125..141
FT /note="PTYKWKRQVTQRNPVEQ -> CVGAERKGHYACYTICA (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030577"
FT VAR_SEQ 142..608
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030578"
FT VAR_SEQ 472..608
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030579"
FT CONFLICT 2
FT /note="T -> A (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="M -> V (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="I -> V (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="Q -> P (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> K (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="C -> S (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="E -> D (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="S -> T (in Ref. 1; AAC79697/AAD12742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 69446 MW; 1E6F768EF00B0468 CRC64;
MTSTLDLDKG CTVEELLRGC IEAFDDSGKV RDPQLVRMFL MMHPWYIPSS QLASKLLHFY
QQSRKDNSNS LQMKTCHLVR YWISAFPAEF DLNPELAEQI KELKALLDQE GNRRHSSLID
IESVPTYKWK RQVTQRNPVE QKKRKMSLLF DHLEPMELAE HLTYLEYRSF CKILFQDYHS
FVTHGCTVDN PVLERFISLF NSVSQWVQLM ILSKPTATQR ALVITHFVHV AERLLQLQNF
NTLMAVVGGL SHSSISRLKE THSHVSPDTI KLWEGLTELV TATGNYSNYR RRLAACVGFR
FPILGVHLKD LVALQLALPD WLDPGRTRLN GAKMRQLFCI LEELAMVTSL RPPVQANPDL
LSLLTVSLDQ YQTEDELYQL SLQREPRSKS SPTSPTSCTP PPRPPVLEEW TSVAKPKLDQ
ALVAEHIEKM VESVFRNFDV DGDGHISQEE FQIIRGNFPY LSAFGDLDQN QDGCISREEM
ISYFLRSSSV LGGRMGFVHN FQESNSLRPV ACRHCKALIL GIYKQGLKCR ACGVNCHKQC
KERLSVECRR RAQSVSLEGS APSPSPTHTH HRAFSFSLPR PGRRSSRPPE IREEEVQSVE
DGVFDIHL
