GAPD1_MOUSE
ID GAPD1_MOUSE Reviewed; 1458 AA.
AC Q6PAR5; A0PJI8; A2AR09; A2AR10; A2AR17; A2AR18; Q3TNS1; Q3UDL0; Q3UYD5;
AC Q6ZPP0; Q80V37; Q80ZK4; Q8BTS5; Q9CRS2; Q9CTI1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
DE AltName: Full=GAPex-5;
DE AltName: Full=Rab5-activating protein 6;
GN Name=Gapvd1; Synonyms=Gapex5, Kiaa1521;
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 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH TRIP10.
RC STRAIN=Swiss albino;
RX PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
RA Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M.,
RA Pessin J.E., Saltiel A.R.;
RT "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4
RT trafficking in adipocytes.";
RL Cell Metab. 5:59-72(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 973-1458 (ISOFORM 6).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Liver, Medulla oblongata, and Thymus;
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 [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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Brain, Kidney, and Mammary tumor;
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 [6]
RP FUNCTION.
RX PubMed=16880210; DOI=10.1074/jbc.m602873200;
RA Su X., Lodhi I.J., Saltiel A.R., Stahl P.D.;
RT "Insulin-stimulated Interaction between insulin receptor substrate 1 and
RT p85alpha and activation of protein kinase B/Akt require Rab5.";
RL J. Biol. Chem. 281:27982-27990(2006).
RN [7]
RP FUNCTION.
RX PubMed=17545148; DOI=10.1074/jbc.m703725200;
RA Su X., Kong C., Stahl P.D.;
RT "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal
RT growth factor receptor.";
RL J. Biol. Chem. 282:21278-21284(2007).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566; SER-569; SER-742;
RP SER-757; SER-902; SER-908 AND SER-1044, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine
CC nucleotide exchange factor (GEF), and participates in various processes
CC such as endocytosis, insulin receptor internalization or LC2A4/GLUT4
CC trafficking. Acts as a GEF for the Ras-related protein RAB31 by
CC exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4
CC trafficking. In the absence of insulin, it maintains RAB31 in an active
CC state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles
CC and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon
CC insulin stimulation, it is translocated to the plasma membrane,
CC releasing LC2A4/GLUT4 from intracellular storage vesicles. Also
CC involved in EGFR trafficking and degradation, possibly by promoting
CC EGFR ubiquitination and subsequent degradation by the proteasome. Has
CC GEF activity for Rab5 and GAP activity for Ras.
CC {ECO:0000269|PubMed:16880210, ECO:0000269|PubMed:17189207,
CC ECO:0000269|PubMed:17545148}.
CC -!- SUBUNIT: Interacts with RAB5A (By similarity). Interacts with
CC TRIP10/CIP4. {ECO:0000250, ECO:0000269|PubMed:17189207}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17189207};
CC Peripheral membrane protein {ECO:0000269|PubMed:17189207}. Endosome
CC {ECO:0000250}. Note=Recruited to the plasma membrane by TRIP10/CIP4 in
CC response to insulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q6PAR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PAR5-2; Sequence=VSP_032366;
CC Name=3;
CC IsoId=Q6PAR5-3; Sequence=VSP_032363, VSP_032364;
CC Name=4;
CC IsoId=Q6PAR5-4; Sequence=VSP_032365, VSP_032366;
CC Name=5;
CC IsoId=Q6PAR5-5; Sequence=VSP_032366, VSP_032368;
CC Name=6;
CC IsoId=Q6PAR5-6; Sequence=VSP_032367;
CC -!- TISSUE SPECIFICITY: Present in adipocytes and fibroblasts (at protein
CC level). Ubiquitously expressed. {ECO:0000269|PubMed:17189207}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31478.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH43715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH48847.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH57164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29377.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE22277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE29251.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAM15445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM15446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM15455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM15456.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM24604.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM24605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF155419; ABM68541.1; -; mRNA.
DR EMBL; AK129381; BAC98191.1; ALT_INIT; Transcribed_RNA.
DR EMBL; AK014474; BAB29377.2; ALT_INIT; mRNA.
DR EMBL; AK088851; BAC40613.1; -; mRNA.
DR EMBL; AK003521; BAB22834.1; -; mRNA.
DR EMBL; AK134776; BAE22277.1; ALT_INIT; mRNA.
DR EMBL; AK150026; BAE29251.1; ALT_FRAME; mRNA.
DR EMBL; AK165047; BAE38017.1; -; mRNA.
DR EMBL; AL845262; CAM15445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929106; CAM15445.1; JOINED; Genomic_DNA.
DR EMBL; AL845262; CAM15446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929106; CAM15446.1; JOINED; Genomic_DNA.
DR EMBL; AL845262; CAM15447.1; -; Genomic_DNA.
DR EMBL; AL929106; CAM15447.1; JOINED; Genomic_DNA.
DR EMBL; AL845262; CAM15455.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845262; CAM15456.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929106; CAM24604.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845262; CAM24604.1; JOINED; Genomic_DNA.
DR EMBL; AL929106; CAM24605.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845262; CAM24605.1; JOINED; Genomic_DNA.
DR EMBL; AL929106; CAM24606.1; -; Genomic_DNA.
DR EMBL; AL845262; CAM24606.1; JOINED; Genomic_DNA.
DR EMBL; BC031478; AAH31478.1; ALT_SEQ; mRNA.
DR EMBL; BC043715; AAH43715.1; ALT_INIT; mRNA.
DR EMBL; BC048847; AAH48847.1; ALT_SEQ; mRNA.
DR EMBL; BC057164; AAH57164.1; ALT_INIT; mRNA.
DR EMBL; BC060123; AAH60123.1; -; mRNA.
DR CCDS; CCDS15949.1; -. [Q6PAR5-2]
DR CCDS; CCDS89478.1; -. [Q6PAR5-1]
DR RefSeq; NP_079985.2; NM_025709.2. [Q6PAR5-2]
DR RefSeq; XP_011237449.1; XM_011239147.1.
DR RefSeq; XP_011237450.1; XM_011239148.2.
DR AlphaFoldDB; Q6PAR5; -.
DR SMR; Q6PAR5; -.
DR BioGRID; 211649; 2.
DR IntAct; Q6PAR5; 2.
DR STRING; 10090.ENSMUSP00000108723; -.
DR iPTMnet; Q6PAR5; -.
DR PhosphoSitePlus; Q6PAR5; -.
DR EPD; Q6PAR5; -.
DR jPOST; Q6PAR5; -.
DR MaxQB; Q6PAR5; -.
DR PaxDb; Q6PAR5; -.
DR PeptideAtlas; Q6PAR5; -.
DR PRIDE; Q6PAR5; -.
DR ProteomicsDB; 271662; -. [Q6PAR5-1]
DR ProteomicsDB; 271663; -. [Q6PAR5-2]
DR ProteomicsDB; 271664; -. [Q6PAR5-3]
DR ProteomicsDB; 271665; -. [Q6PAR5-4]
DR ProteomicsDB; 271666; -. [Q6PAR5-5]
DR ProteomicsDB; 271667; -. [Q6PAR5-6]
DR Antibodypedia; 30544; 101 antibodies from 18 providers.
DR DNASU; 66691; -.
DR Ensembl; ENSMUST00000028224; ENSMUSP00000028224; ENSMUSG00000026867. [Q6PAR5-2]
DR Ensembl; ENSMUST00000102800; ENSMUSP00000099864; ENSMUSG00000026867. [Q6PAR5-2]
DR Ensembl; ENSMUST00000113099; ENSMUSP00000108723; ENSMUSG00000026867. [Q6PAR5-1]
DR GeneID; 66691; -.
DR KEGG; mmu:66691; -.
DR UCSC; uc008jiq.2; mouse. [Q6PAR5-2]
DR UCSC; uc008jir.1; mouse. [Q6PAR5-3]
DR UCSC; uc012bug.1; mouse. [Q6PAR5-4]
DR CTD; 26130; -.
DR MGI; MGI:1913941; Gapvd1.
DR VEuPathDB; HostDB:ENSMUSG00000026867; -.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000156611; -.
DR HOGENOM; CLU_002165_1_0_1; -.
DR InParanoid; Q6PAR5; -.
DR OMA; SCFLGKK; -.
DR OrthoDB; 944088at2759; -.
DR PhylomeDB; Q6PAR5; -.
DR TreeFam; TF105908; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 66691; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gapvd1; mouse.
DR PRO; PR:Q6PAR5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6PAR5; protein.
DR Bgee; ENSMUSG00000026867; Expressed in manus and 228 other tissues.
DR ExpressionAtlas; Q6PAR5; baseline and differential.
DR Genevisible; Q6PAR5; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; IMP:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endocytosis; Endosome; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1458
FT /note="GTPase-activating protein and VPS9 domain-containing
FT protein 1"
FT /id="PRO_0000324772"
FT DOMAIN 131..353
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1318..1458
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 447..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT VAR_SEQ 373..379
FT /note="GCVAAFL -> VGMSVVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032363"
FT VAR_SEQ 380..1458
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032364"
FT VAR_SEQ 480
FT /note="I -> IGQQLAAITAWDSSATNLTAHIPLVTPF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032365"
FT VAR_SEQ 557..577
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17189207"
FT /id="VSP_032366"
FT VAR_SEQ 1055
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032367"
FT VAR_SEQ 1202
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_032368"
FT CONFLICT 581
FT /note="N -> D (in Ref. 3; BAE29251)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="G -> E (in Ref. 5; AAH31478)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="Y -> H (in Ref. 3; BAE22277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1257
FT /note="A -> V (in Ref. 2; BAC98191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1458 AA; 162402 MW; CA3D2EAF22051FD7 CRC64;
MVKLDIHTLA HHLKQERLYV SSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII
TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL
NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI
LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPAQ QEKLFGEKGS
DRFRQKVQEM VDSNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG
EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGTEEGD
PRTKNSLGKF DKGCVAAFLD VVIGGRAVET PPMSSVNLLE GLSRTVVYIS YSQLITLVNF
MKSVMSGDQL KEDRMALDNL LANLPQAKPG KSSSLDMTPY STPQMSPATT PANKKNRLPI
ATRSRSRSNM LMDLHMDHEG SSQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL
SDGGQGDVPV DENKLHGKPD KTLRFSLCSD NLEGISEGPS NRSNSVSSLD LEGESVSELG
AGPSGSNGVE ALQLLEHEQA TTQDNLDDKL RKFEIRDMMG LTDDRDISET VSETWSTDVL
GSDFDPNVDE DRLQEIAGAA AENVLGSLLC LPGSGSVLLD PCTGSTISET TSEAWSVEVL
PSDSEAPDLK QEERLQELES CSGLGSTSDD TDVREVSSRP STPGLSVVSG ISATSEDIPN
KIEDLRSECS SDFGGKDSVT SPDMDDIAHG AHQLTSPPSQ SESLLAMFDP LSSHEGASAV
VRPKVHYARP SHPPPDPPIL EGAVGGNEAR LPNFGSHVLT AAEMEAFKQR HSYPERLVRS
RSSDIVSSVR RPMSDPSWNR RPGNEELPPA AATGATSLVA APHSSSSSPS KDSSRGETEE
RKDSDDERSD RSRPWWRKRF VSAMPKAPIP FRKKEKQEKD KDDLGPDRFS TLTDEPSPRL
SAQAQVAEDI LDKYRNAIKR TSPSEGAMAN DESAEVMGDG ESAHDSPREE ALQNISADDL
PDSASQAAHP QDSAFSYRDV KKKLRLALCS ADSVAFPVLT HSTRNGLPDH TDPEDNEIVC
FLKVQIAEAI NLQDKSLMAQ LQETMRCVCR FDNRTCRKLL ASIAEDYRKR APYIAYLTRC
RQGLQTTQAH LERLLQRVLR DKEVANRYFT TVCVRLLLES KEKKIREFIQ DFQKLTAADD
KTAQVEDFLQ FLYGVMAQDV IWQNASEEQL QDAQLAIERS VMNRIFKLAF YPNQDGDILR
DQVLHEHIQR LSKVVTANHR ALQIPEVYLR EAPWPSAQSE IRTISAYKTP RDKVQCILRM
CSTIMNLLSL ANEDSVPGAD DFVPVLVFVL IKANPPCLLS TVQYISSFYA SCLSGEESYW
WMQFTAAVEF IKTIDDRK
