SYNPO_MOUSE
ID SYNPO_MOUSE Reviewed; 929 AA.
AC Q8CC35; Q99JI0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Synaptopodin;
GN Name=Synpo; Synonyms=Kiaa1029;
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 3).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203 (ISOFORM 1).
RC TISSUE=Brain;
RG The MGC Project Team;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 392-404; 567-586 AND 751-760, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 863-929 (ISOFORMS 1/3).
RC TISSUE=Skeletal muscle;
RA Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT "Full-length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 921-929 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [6]
RP INTERACTION WITH ACTIN, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9314539; DOI=10.1083/jcb.139.1.193;
RA Mundel P., Heid H.W., Mundel T.M., Krueger M., Reiser J., Kriz W.;
RT "Synaptopodin: an actin-associated protein in telencephalic dendrites and
RT renal podocytes.";
RL J. Cell Biol. 139:193-204(1997).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12357430; DOI=10.1002/cne.10362;
RA Deller T., Haas C.A., Deissenrieder K., Del Turco D., Coulin C.,
RA Gebhardt C., Drakew A., Schwarz K., Mundel P., Frotscher M.;
RT "Laminar distribution of synaptopodin in normal and reeler mouse brain
RT depends on the position of spine-bearing neurons.";
RL J. Comp. Neurol. 453:33-44(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12928494; DOI=10.1073/pnas.1832384100;
RA Deller T., Korte M., Chabanis S., Drakew A., Schwegler H., Stefani G.G.,
RA Zuniga A., Schwarz K., Bonhoeffer T., Zeller R., Frotscher M., Mundel P.;
RT "Synaptopodin-deficient mice lack a spine apparatus and show deficits in
RT synaptic plasticity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10494-10499(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-672, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-833,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 (ISOFORM 2), AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-202; SER-222;
RP SER-258; SER-488; SER-672; SER-689; SER-740; SER-744; THR-769 AND SER-833,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-690; SER-803; SER-819;
RP SER-824; SER-852 AND SER-892 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-848, METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-786; ARG-800 AND ARG-814 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: Actin-associated protein that may play a role in modulating
CC actin-based shape and motility of dendritic spines and renal podocyte
CC foot processes. Seems to be essential for the formation of spine
CC apparatuses in spines of telencephalic neurons, which is involved in
CC synaptic plasticity. {ECO:0000269|PubMed:12928494}.
CC -!- SUBUNIT: Interacts with BAIAP1. Interacts with actin. Interacts (via
CC PPxY motifs) with WWC1 (via WW domains) (By similarity).
CC {ECO:0000250|UniProtKB:Q8N3V7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9314539}. Cell junction, tight junction
CC {ECO:0000269|PubMed:9314539}. Perikaryon {ECO:0000269|PubMed:9314539}.
CC Cell projection, dendritic spine {ECO:0000269|PubMed:12928494,
CC ECO:0000269|PubMed:9314539}. Postsynaptic density
CC {ECO:0000269|PubMed:9314539}. Synapse {ECO:0000269|PubMed:9314539}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N3V7}. Note=Localized at
CC the tight junction of cells. In brain, localized to the postsynaptic
CC densities and in the perikarya. Associated with dendritic spines of a
CC subset of synapses (PubMed:9314539). {ECO:0000269|PubMed:9314539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CC35-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CC35-2; Sequence=VSP_010478, VSP_010479;
CC Name=3;
CC IsoId=Q8CC35-3; Sequence=VSP_010478;
CC -!- TISSUE SPECIFICITY: Expressed in brain, namely in the olfactory bulb,
CC cerebral cortex, striatum, and hippocampus, but not in the cerebellum.
CC Also expressed in the podocytes of kidney glomeruli. In the
CC hippocampus, mainly expressed in the principal cell layer of the
CC dentate gyrus and Ammon's horn. {ECO:0000269|PubMed:12357430,
CC ECO:0000269|PubMed:12928494, ECO:0000269|PubMed:9314539}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
CC -!- MISCELLANEOUS: Synpo deficient mice develop normally, but they lack the
CC spine apparatuses. Adult mice have an impairment of spatial learning in
CC the radial arm maze test.
CC -!- SIMILARITY: Belongs to the synaptopodin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98077.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129267; BAC98077.1; ALT_INIT; mRNA.
DR EMBL; CF539371; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ278123; CAC34581.1; -; mRNA.
DR EMBL; AK034012; BAC28546.1; ALT_INIT; mRNA.
DR CCDS; CCDS37833.1; -. [Q8CC35-2]
DR CCDS; CCDS50298.1; -. [Q8CC35-3]
DR AlphaFoldDB; Q8CC35; -.
DR CORUM; Q8CC35; -.
DR IntAct; Q8CC35; 7.
DR MINT; Q8CC35; -.
DR STRING; 10090.ENSMUSP00000095174; -.
DR iPTMnet; Q8CC35; -.
DR PhosphoSitePlus; Q8CC35; -.
DR EPD; Q8CC35; -.
DR jPOST; Q8CC35; -.
DR MaxQB; Q8CC35; -.
DR PaxDb; Q8CC35; -.
DR PeptideAtlas; Q8CC35; -.
DR PRIDE; Q8CC35; -.
DR ProteomicsDB; 254716; -. [Q8CC35-1]
DR ProteomicsDB; 254717; -. [Q8CC35-2]
DR ProteomicsDB; 254718; -. [Q8CC35-3]
DR Antibodypedia; 16210; 313 antibodies from 35 providers.
DR Ensembl; ENSMUST00000097566; ENSMUSP00000095174; ENSMUSG00000043079. [Q8CC35-2]
DR Ensembl; ENSMUST00000115318; ENSMUSP00000110973; ENSMUSG00000043079. [Q8CC35-3]
DR Ensembl; ENSMUST00000130044; ENSMUSP00000121756; ENSMUSG00000043079. [Q8CC35-2]
DR Ensembl; ENSMUST00000143275; ENSMUSP00000125272; ENSMUSG00000043079. [Q8CC35-1]
DR Ensembl; ENSMUST00000155195; ENSMUSP00000117897; ENSMUSG00000043079. [Q8CC35-3]
DR UCSC; uc008far.2; mouse. [Q8CC35-1]
DR MGI; MGI:1099446; Synpo.
DR VEuPathDB; HostDB:ENSMUSG00000043079; -.
DR eggNOG; ENOG502R7RM; Eukaryota.
DR GeneTree; ENSGT00950000183054; -.
DR HOGENOM; CLU_013103_0_0_1; -.
DR InParanoid; Q8CC35; -.
DR PhylomeDB; Q8CC35; -.
DR TreeFam; TF330867; -.
DR ChiTaRS; Synpo; mouse.
DR PRO; PR:Q8CC35; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CC35; protein.
DR Bgee; ENSMUSG00000043079; Expressed in ascending aorta and 272 other tissues.
DR ExpressionAtlas; Q8CC35; baseline and differential.
DR Genevisible; Q8CC35; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; NAS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0097444; C:spine apparatus; IDA:SynGO.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0030865; P:cortical cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0098886; P:modification of dendritic spine; ISO:MGI.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0099588; P:positive regulation of postsynaptic cytosolic calcium concentration; IDA:SynGO.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:SynGO-UCL.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:1905355; P:spine apparatus assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008542; P:visual learning; IMP:SynGO-UCL.
DR InterPro; IPR028753; Synpo.
DR PANTHER; PTHR24217:SF13; PTHR24217:SF13; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycoprotein;
KW Methylation; Phosphoprotein; Reference proteome; Synapse; Tight junction.
FT CHAIN 1..929
FT /note="Synaptopodin"
FT /id="PRO_0000187671"
FT REGION 54..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 549..552
FT /note="PPxY motif"
FT MOTIF 568..571
FT /note="PPxY motif"
FT COMPBIAS 148..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT MOD_RES 547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z327"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z327"
FT MOD_RES 769
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 848
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3V7"
FT VAR_SEQ 1..239
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010478"
FT VAR_SEQ 921..929
FT /note="VWKPSFCFK -> DRPESLPTSPPWTPAASRPPSSLDGWVSPGPWEPGRGSS
FT MSSPPPLPPPPPMSPSWSERSVSPLRSETEARPPSRQLQALLARNIINAARRKSASPRP
FT APAETLRPFSPPQGPPPPPARMRSPQPASPARNFRGAAFSPIPRSPLPIGPSSCASPRS
FT PQAAPSRPFPYRRSPTDSDVSLDSEDSGLKSPGILGYNICPRGWNGSLRLKRGSLPTEA
FT SCTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010479"
FT CONFLICT 189
FT /note="K -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8CC35-2:690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CC35-2:786
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8CC35-2:789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES Q8CC35-2:800
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8CC35-2:803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CC35-2:814
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8CC35-2:819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CC35-2:824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CC35-2:852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CC35-2:869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES Q8CC35-2:892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 929 AA; 99552 MW; 979CFEE4F9E061A2 CRC64;
MLGAHFPPPP LGASEGRAAP CTFQIPDGSY RCLALEAEES SSEDGLQGEV RLVDLEEEGT
SQSRANHGTP PLSRAPAIIQ PSSCHREARG GFQRSDRPSH DWDVVQARKV MTASGSSSPV
PRVAQKPALG RSTSFTENDL KEAKARSQQI AAQLTTPPSS NSRGVQLFNR RRQRVNEFTL
ESRGQRSPKL NQEALQTGRP LSPIGHAPGP SVKPTSPSKP GSPKHPSPQS PSRGVAGHIM
EGYSEEASLL RHLEKVASEE EEVPLVVYLK ENAALLTANG LHLSQSRETQ QSSPNPPDTE
VPSPAADINQ NPSSPNATLT TLASSSHHSQ PTADINQNPP AAITPVPQNS SQAQCSPNGT
LDSKPGTLCA DDGQSPVPAE EVRSSILLID KVSAPPSAAS TFSREATPLS SSGPPAADLM
SSSLLIDMQP STLVAPAEQE VPGHVAVTTP TKVYSEVHLT LAKPASVVNR TARPFGIQSP
GTSQIEQSPM MGRRQFGEKA WAPPASSMAD RSPQPQRHIM SRSPMVERRL LGQRSPVLER
RPLGNFTPPP TYAETLSTAP VASRVRSPPS YSTLYPSSDP KPSHLKGQVA PANKTGILEE
SMARRGSRKS MFTFVEKPKV TPNPDLLDLV QTADEKRRQR DHGEVGMEEE PFALGAEASN
FQQEPIARDR ASPAAAEEAV PEWASCLKSP RIQAKPKPKP NQNLSEASGK GAELYARRQS
RMEKYVIESS GHAELARCPS PTMSLPSSWK YTTNAPGGFR VASLSPARTP PASLYHGYLP
ENGVLRPEPT KQQPYQMRPS LYALSPVKEP AKASSRATSS RTPSRTVSPR AASPAKPSSL
DLVPNLPRAG LPPSPALPRP SRSSPGLYTA PVQDSLQPTA VSPTYSSDIS PVSPSRAWSP
RAKQAPRPSF STRNAGIEAQ VWKPSFCFK
