TGO1_MOUSE
ID TGO1_MOUSE Reviewed; 1930 AA.
AC Q8BI84; A0JLX8; Q3UFI9; Q571D7; Q8BJE9; Q8BL31; Q8C5B9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Transport and Golgi organization protein 1 homolog {ECO:0000305};
DE Short=TANGO1 {ECO:0000305};
DE AltName: Full=Melanoma inhibitory activity protein 3 {ECO:0000312|MGI:MGI:2443183};
DE Flags: Precursor;
GN Name=Mia3 {ECO:0000312|MGI:MGI:2443183};
GN Synonyms=Kiaa0268 {ECO:0000312|EMBL:BAD90177.1},
GN Tango {ECO:0000303|PubMed:15183315};
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 [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1382 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1726-1930 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Cecum, Corpora quadrigemina, Fetal eye, Pancreas, and Retina;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1467-1930.
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1469-1930.
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 [5]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15183315; DOI=10.1016/j.modgep.2003.12.002;
RA Bosserhoff A.K., Moser M., Buettner R.;
RT "Characterization and expression pattern of the novel MIA homolog TANGO.";
RL Gene Expr. Patterns 4:473-479(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1754 AND SER-1915, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1766, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1915, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1458; SER-1693; SER-1705;
RP SER-1754 AND SER-1766, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1805, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays a role in the transport of cargos that are too large to
CC fit into COPII-coated vesicles and require specific mechanisms to be
CC incorporated into membrane-bound carriers and exported from the
CC endoplasmic reticulum. This protein is required for collagen VII
CC (COL7A1) secretion by loading COL7A1 into transport carriers. It may
CC participate in cargo loading of COL7A1 at endoplasmic reticulum exit
CC sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound
CC COL7A1 into a growing carrier. Does not play a role in global protein
CC secretion and is apparently specific to COL7A1 cargo loading. However,
CC it may participate in secretion of other proteins in cells that do not
CC secrete COL7A1. It is also specifically required for the secretion of
CC lipoproteins by participating in their export from the endoplasmic
CC reticulum. Required for correct assembly of COPII coat components at
CC endoplasmic reticulum exit sites (ERES) and for the localization of
CC SEC16A and membrane-bound ER-resident complexes consisting of MIA2 and
CC PREB/SEC12 to ERES. {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SUBUNIT: Interacts with MIA2. Interacts (via SH3 domain) with COL7A1.
CC Interacts with the COPII coat subunits SEC23A, SEC23B and maybe SEC24C.
CC May interact with APOB and MIA2. Interacts with SEC16A.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5JRA6}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5JRA6}. Note=Localizes at endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). SEC16A is required for its proper localization to ERES. After
CC loading of COL7A1 into transport carriers, it is not incorporated into
CC COPII carriers and remains in the endoplasmic reticulum membrane.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BI84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BI84-2; Sequence=VSP_025867, VSP_025868;
CC Name=3;
CC IsoId=Q8BI84-3; Sequence=VSP_025865, VSP_025866;
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during embryogenesis,
CC starting at 8 dpc. {ECO:0000269|PubMed:15183315}.
CC -!- DOMAIN: The proline-rich domain (PRD) contains repeated PPP motifs. A
CC single PPP motif is necessary and sufficient to mediate interaction
CC with the COPII coat subunits SEC23A and SEC23B.
CC {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- DOMAIN: Although 2 transmembrane domains are predicted, it only
CC contains one transmembrane domain. The other predicted transmembrane
CC region is probably a hairpin-type region embedded into the membrane,
CC which does not cross the membrane. It is unclear which of the 2
CC predicted transmembrane regions is the transmembrane or the hairpin-
CC type region. {ECO:0000250|UniProtKB:Q5JRA6}.
CC -!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK044749; BAC32064.1; -; mRNA.
DR EMBL; AK046506; BAC32759.1; -; mRNA.
DR EMBL; AK078951; BAC37474.1; -; mRNA.
DR EMBL; AK084344; BAC39164.1; -; mRNA.
DR EMBL; AK148470; BAE28571.1; ALT_TERM; mRNA.
DR EMBL; CAAA01083517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220252; BAD90177.1; -; mRNA.
DR EMBL; BC125472; AAI25473.1; -; mRNA.
DR RefSeq; NP_796363.2; NM_177389.3.
DR AlphaFoldDB; Q8BI84; -.
DR SMR; Q8BI84; -.
DR BioGRID; 237218; 1.
DR IntAct; Q8BI84; 1.
DR STRING; 10090.ENSMUSP00000064801; -.
DR TCDB; 9.B.113.1.1; the collagen secretory protein, mia3 (mia3) family.
DR GlyConnect; 2505; 4 N-Linked glycans (2 sites).
DR GlyGen; Q8BI84; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q8BI84; -.
DR PhosphoSitePlus; Q8BI84; -.
DR EPD; Q8BI84; -.
DR jPOST; Q8BI84; -.
DR MaxQB; Q8BI84; -.
DR PaxDb; Q8BI84; -.
DR PeptideAtlas; Q8BI84; -.
DR PRIDE; Q8BI84; -.
DR ProteomicsDB; 259376; -. [Q8BI84-1]
DR ProteomicsDB; 259377; -. [Q8BI84-2]
DR ProteomicsDB; 259378; -. [Q8BI84-3]
DR DNASU; 338366; -.
DR GeneID; 338366; -.
DR KEGG; mmu:338366; -.
DR UCSC; uc008icw.1; mouse. [Q8BI84-1]
DR CTD; 375056; -.
DR MGI; MGI:2443183; Mia3.
DR eggNOG; ENOG502QS87; Eukaryota.
DR InParanoid; Q8BI84; -.
DR OrthoDB; 208382at2759; -.
DR PhylomeDB; Q8BI84; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 338366; 0 hits in 19 CRISPR screens.
DR ChiTaRS; Mia3; mouse.
DR PRO; PR:Q8BI84; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BI84; protein.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; ISS:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0035459; P:vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF07653; SH3_2; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW ER-Golgi transport; Exocytosis; Glycoprotein; Membrane; Methylation;
KW Phosphoprotein; Protein transport; Reference proteome; SH3 domain; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1930
FT /note="Transport and Golgi organization protein 1 homolog"
FT /id="PRO_0000288999"
FT TOPO_DOM 25..1171
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 1172..1192
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1203..1223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1224..1930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 144..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1677
FT /note="Mediates interaction with MIA2"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT REGION 1447..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1930
FT /note="Proline-rich domain (PRD); mediates interaction with
FT the COPII coat subunits SEC23A and SEC23B"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT REGION 1801..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1869
FT /note="SEC16A-interacting region (SIR); required for its
FT localization to endoplasmic reticulum exit sites and for
FT its interaction with SEC16A"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT REGION 1840..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1236..1329
FT /evidence="ECO:0000255"
FT COILED 1359..1422
FT /evidence="ECO:0000255"
FT COILED 1514..1662
FT /evidence="ECO:0000255"
FT COMPBIAS 148..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..706
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JRA6"
FT MOD_RES 1805
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1149
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025865"
FT VAR_SEQ 1150..1186
FT /note="GDVQKQLETIAEEPAAVPPLESAFGSLYAFILYLSKM -> MDSLPATVPAV
FT TASPGDPELLGPLSVLYAALIAKLLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025866"
FT VAR_SEQ 1232..1239
FT /note="KSRVYQVT -> SKLNYLIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025867"
FT VAR_SEQ 1240..1930
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025868"
SQ SEQUENCE 1930 AA; 213675 MW; 7C80FC1260136D7F CRC64;
MAAAPGLLFW LFVLGALWWV PGQSDLSHGR RFSDLKVCGD EECSMLMYRG KALEDFTGPD
CRFVNFKKGD DVYVYYKLAG GSLELWAGSV EHSFGYFPKD LIKVLHKYTE EELHIPADET
DFVCFEGGRD DFNSYNVEEL LGSLELEDSV PEESKKAEEV SQHREKSPEE SRGRELDPVP
EPEAFRADSE DGEGAFSEST EGLQGQPSAQ ESHPHTSGPA ANAQGVQSSL DTFEEILHDK
LKVPGSESRT GNSSPASVER EKTDAYKVLK TEMSLDLKTK FGSTADALVS DDEATRLVTS
LEDGFDEALD AEYYPMEEEE EVEEDADSSD ELPLLTFSDK DEKVPGKPMI EKYLTDKDPN
LSEEDKVEPP TWGDAFFSIV TGGEGKPGVV DLERSIEEEE DVSVSSSHQR KPQPAAGYTD
SEDEGDDLFV EEPKTNDVKD SETDPELVIT GEEKDIQESR KGLVQPESQS EDAKSETASA
YRLQGSKLNP LSAAEKGRDF TLKAVFEKKE NGLKESVIHI SKETLHEDKT REIQRDSLES
ELVHRALGSS VTENNKPKSL GVAPLLGNNK PDASKDSTEV PDGSVSGPKA GQQEGFLEPG
LKTQHQPRFS PPEETGPSRE LGGKVPISGR NLSWQQEQDV AAVVGKHANE KTGFPEEESR
EDGTDAEQAR AIRRPQEAES PEVLSVQPGR PDEEEEEEEG DNYPPEGLME DENAVSAQQS
RENSPSARDG RSDMNSQVFE KVILGTLNLN TEKTKQPANM ILETGQESET TSEEAGDVGK
ESGHSVVVDS EESHLADMRA QRPSQVHGLR DETAAQTPGS GEAVLSKNPN DLQKDNPEEE
LVNTLGLEDP GVGEISEGEP EDTKEFGVSE SQGTDAEDLR DDPSRQATPE IPDIVLKSIR
EDLPIINSFF KDDQQSLHRF LKYFDVRELE GLLEDMSIRL RSAHQNSLPY NMEKVLDKVF
RASESRILSM AEKMLDTGVA KNRDLGSKES SPLEEAEVLD DIQDLIYFVR YQYSGVETAP
LVTPPPPEEG WARPGEERQP PQQDSLPQEN TGDLSVQPPE EPELSDQPVT SVQPPEEPEL
SDQPVTSVQP PEEPELSDQP VTSVQPPEEP ELSDQPVTGY TSTSEVSQKP DTKKDIDLGP
VMEGGPVGAG DVQKQLETIA EEPAAVPPLE SAFGSLYAFI LYLSKMLLAT LPDNVQPGPD
FYGLPWQPVI ITAVLGIVSF AIFSWRTILV VKSRVYQVTE KQISEKLENI KKENAELMQK
LSSYEQKIKE SKKYVQETKK QNMILSDEAV KYKDKIKILE ETNVSLGDKA KSLRLQLESE
REQNVKNQDL ILENKKSIEK LKDVISMNAS ELSEVQVALN EAKLSEENVK SECHRVQEEN
ARLKKKKEQL QQQVEEWSKS HAELTGQIKS FEKSQEDLEI ALTHKDDNIS ALTNCITQLN
RLECELESED PDKGGNESDD LANGETGGDR SEKIRNRIKQ MMDVSRTQTA VSIVEEDLKL
LQLKLRASMS TKCNLEDQIK KLEDDRSSLQ TAKAGLEDEC KTLRQKVEIL NELYQQKEMA
LQKKLSQEEY ERQDREQRLT AADEKVVLAA EEVKTYKRRI EEMEEELQKT ERSFKNQIAA
HEKKAHDNWL KARAAERAMA EEKREAANLR HKLLEMTQKM AMRQDEPVIV KPMPGRPNTQ
NPPRRGLLSQ NGSFGPSPVS GGECSPPLPA EPPGRPLSAT LSRRDTPRSE FGSLDRHLPR
PRWPSEASGK HSASDPGPAP VVNSSSRSSS PAKAVDEGKV NMAPKGPPPF PGVPLMGGPV
PPPIRYGPPP QLCGGPFGPR PLPPPFVPGM HPPLGVREYA PGVLPGKRDL PLDPREFLPG
HTPFRPPGSL GPREFFIPGT RLPPPTHGPQ EYPPPPPAVR DSLPSGPREE AKPASPSSVQ
DRSQASKPTP
