ID   SRCN1_MOUSE             Reviewed;        1250 AA.
AC   Q9QWI6; O70298;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   04-NOV-2026, entry version 167.
DE   RecName: Full=SRC kinase signaling inhibitor 1;
DE   AltName: Full=SNAP-25-interacting protein;
DE            Short=SNIP;
DE   AltName: Full=p130Cas-associated protein;
DE   AltName: Full=p140Cap;
GN   Name=Srcin1; Synonyms=Kiaa1684, P140;
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 {ECO:0000312|EMBL:AAC15635.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Croci L., Bossolasco M., Consalez G.G.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-1250 (ISOFORM 3).
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC98232.1};
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] {ECO:0000305}
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=14657239; DOI=10.1091/mbc.e03-09-0689;
RA   Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
RA   Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
RT   "p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
RT   protein involved in cell spreading.";
RL   Mol. Biol. Cell 15:787-800(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-588; SER-1054 AND
RP   SER-1110, AND 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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND TYR-464, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA   Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA   Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA   Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT   "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT   plasticity.";
RL   Neuron 61:85-100(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-52; SER-79; SER-87;
RP   SER-98; SER-211; SER-247; SER-293; TYR-309; SER-366; SER-375; SER-392;
RP   SER-430; SER-432; SER-559; SER-562; SER-566; SER-569; SER-579; SER-581;
RP   SER-583; SER-588; SER-664; SER-688; THR-691; THR-704; SER-911; SER-933;
RP   SER-1054; SER-1110 AND SER-1127, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Kidney;
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-397; ARG-404 AND ARG-567, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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: Acts as a negative regulator of SRC by activating CSK which
CC       inhibits SRC activity and downstream signaling, leading to impaired
CC       cell spreading and migration. Regulates dendritic spine morphology.
CC       Involved in calcium-dependent exocytosis. May play a role in
CC       neurotransmitter release or synapse maintenance (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the N-terminal coiled-coil region of SNAP25.
CC       Interacts with BCAR1/p130Cas and SRC through its C-terminal domain.
CC       Interacts with CSK, CTTN, SORBS3/vinexin, SYP and MAPRE3/EB3 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9QWI6; Q61140: Bcar1; NbExp=2; IntAct=EBI-775592, EBI-77088;
CC       Q9QWI6; P56945: BCAR1; Xeno; NbExp=3; IntAct=EBI-775592, EBI-702093;
CC       Q9QWI6-2; Q14247: CTTN; Xeno; NbExp=2; IntAct=EBI-775607, EBI-351886;
CC       Q9QWI6-2; Q9UPY8: MAPRE3; Xeno; NbExp=5; IntAct=EBI-775607, EBI-726739;
CC       Q9QWI6-2; O60504-2: SORBS3; Xeno; NbExp=4; IntAct=EBI-775607, EBI-1222956;
CC       Q9QWI6-2; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-775607, EBI-848039;
CC       Q9QWI6-2; P07825: Syp; Xeno; NbExp=2; IntAct=EBI-775607, EBI-976085;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QXY2}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXY2}. Cell
CC       projection, axon {ECO:0000250|UniProtKB:Q9QXY2}. Cell projection,
CC       dendrite {ECO:0000250|UniProtKB:Q9QXY2}. Presynapse
CC       {ECO:0000250|UniProtKB:Q9QXY2}. Postsynapse
CC       {ECO:0000250|UniProtKB:Q9QXY2}. Postsynaptic density
CC       {ECO:0000250|UniProtKB:Q9QXY2}. Note=Localized to the perinuclear
CC       region, lamellopodia, cortical actin and actin stress fibers but not to
CC       focal adhesions. Strongly expressed in axons and dendrites of the CA1
CC       and CA3 hippocampal regions and of the dentate gyrus. Detected in both
CC       presynapses and postsynapses and enriched in postsynaptic density
CC       fractions. {ECO:0000250|UniProtKB:Q9QXY2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:14657239}; Synonyms=1a
CC       {ECO:0000303|PubMed:14657239};
CC         IsoId=Q9QWI6-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:14657239}; Synonyms=1b
CC       {ECO:0000303|PubMed:14657239};
CC         IsoId=Q9QWI6-2; Sequence=VSP_050631;
CC       Name=3 {ECO:0000305};
CC         IsoId=Q9QWI6-3; Sequence=VSP_050632;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in central nervous system
CC       with high levels detected in cortex, cerebellum, midbrain and spinal
CC       cord (at protein level). Also expressed in testis and epithelial-rich
CC       tissues such as mammary gland, lung and kidney.
CC       {ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:19146815}.
CC   -!- PTM: Tyrosine-phosphorylated in response to EGF and to cell adhesion to
CC       integrin ligands. {ECO:0000250|UniProtKB:Q9C0H9}.
CC   -!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF040944; AAC15635.1; -; mRNA.
DR   EMBL; U59873; AAD00087.1; -; mRNA.
DR   EMBL; AK129422; BAC98232.1; ALT_FRAME; mRNA.
DR   PIR; T34101; T34101.
DR   RefSeq; NP_061361.2; NM_018873.2.
DR   AlphaFoldDB; Q9QWI6; -.
DR   BioGRID; 207768; 21.
DR   FunCoup; Q9QWI6; 518.
DR   IntAct; Q9QWI6; 371.
DR   STRING; 10090.ENSMUSP00000103222; -.
DR   GlyCosmos; Q9QWI6; 12 sites, 1 glycan.
DR   GlyGen; Q9QWI6; 13 sites, 1 O-linked glycan (11 sites).
DR   iPTMnet; Q9QWI6; -.
DR   PhosphoSitePlus; Q9QWI6; -.
DR   SwissPalm; Q9QWI6; -.
DR   PaxDb; 10090-ENSMUSP00000103222; -.
DR   PeptideAtlas; Q9QWI6; -.
DR   ProteomicsDB; 263337; -. [Q9QWI6-1]
DR   ProteomicsDB; 263338; -. [Q9QWI6-2]
DR   ProteomicsDB; 263339; -. [Q9QWI6-3]
DR   DNASU; 56013; -.
DR   GeneID; 56013; -.
DR   KEGG; mmu:56013; -.
DR   AGR; MGI:1933179; -.
DR   CTD; 80725; -.
DR   MGI; MGI:1933179; Srcin1.
DR   eggNOG; ENOG502QPNH; Eukaryota.
DR   InParanoid; Q9QWI6; -.
DR   PhylomeDB; Q9QWI6; -.
DR   BioGRID-ORCS; 56013; 0 hits in 78 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q9QWI6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9QWI6; protein.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:GO_Central.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030027; C:lamellipodium; ISO:GO_Central.
DR   GO; GO:0098984; C:neuron to neuron synapse; ISO:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:1990708; P:conditioned place preference; ISO:GO_Central.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR   GO; GO:0050709; P:negative regulation of protein secretion; ISO:GO_Central.
DR   GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:GO_Central.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:GO_Central.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0051963; P:regulation of synapse assembly; IDA:SynGO.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   FunFam; 1.20.58.1540:FF:000001; SRC kinase signaling inhibitor 1; 1.
DR   Gene3D; 1.20.58.1540; Actin interacting protein 3, C-terminal domain; 1.
DR   InterPro; IPR022782; AIP3-like_C.
DR   InterPro; IPR051825; SRCIN1.
DR   PANTHER; PTHR22741; P140CAP/SNIP-RELATED; 1.
DR   PANTHER; PTHR22741:SF5; SRC KINASE SIGNALING INHIBITOR 1; 1.
DR   Pfam; PF03915; AIP3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Exocytosis; Methylation; Phosphoprotein; Reference proteome;
KW   Synapse.
FT   CHAIN           1..1250
FT                   /note="SRC kinase signaling inhibitor 1"
FT                   /id="PRO_0000072012"
FT   REGION          19..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..764
FT                   /note="Interaction with SNAP25"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT   REGION          924..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          712..753
FT                   /evidence="ECO:0000255"
FT   COILED          793..813
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        19..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..75
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..374
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..399
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..563
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..607
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..710
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1078
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXY2"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         309
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         397
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         404
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         464
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         566
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         567
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         691
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         704
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         911
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         933
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         951
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT   MOD_RES         1054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..41
FT                   /note="MQPWQCLRRFALAWWERTAEGRARSPREEVGPRDPGGRGEP -> MGNAPSQ
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14657239, ECO:0000303|Ref.1"
FT                   /id="VSP_050631"
FT   VAR_SEQ         1207..1250
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_050632"
FT   CONFLICT        740..741
FT                   /note="NV -> KL (in Ref. 2; BAC98232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        755
FT                   /note="P -> R (in Ref. 2; BAC98232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        759..760
FT                   /note="DV -> EL (in Ref. 2; BAC98232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        821
FT                   /note="M -> V (in Ref. 2; BAC98232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        960
FT                   /note="C -> G (in Ref. 2; BAC98232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1121..1122
FT                   /note="KL -> NV (in Ref. 1; AAD00087)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1250 AA;  134859 MW;  85F394C9523F78C0 CRC64;
     MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
     EYRTLGGGGG GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
     LKSKYPQHAL ALRGQQDRMR EQVGGWTVDP VCLLSSLCSH LHGDSTPSGA GQPAQQPNYW
     SFKTRSSRHT QGAQPGLADQ AAKLSYASAE SLETMSEAEL PLGFSRMNRF RQSLPLSRSA
     SQTKLRSPGV LFLQFGEETR RVHITHEVSS LDTLHALIAH MFPQKLTMGM LKSPNTAILI
     KDEARNVFYE LEDVRDIQDR SIIKIYRKEP LYAAFPGSHL TNGDLRREMV YASRESSPTR
     RLNNLSPASH LASSSPPPGL PSGLPSGLPS GSPSRSRLSY AGGRPPSYAG SPVHHAAERL
     GGAPTGQGVS PSPSAILERR DVKPDEDLAG KAGGMVLVKG EGLYADPYGL LHEGRLSLAA
     AAETHSHTRA RAACTSGVPC ALSAPTPLPR CSPTWRTRCT RRALAALYGD GYGFRLPPSS
     PQKLADVSAP SGGPPPPHSP YSGPPSRGSP VRQSFRKDSG SSSVFAESPG GKARSTGSAS
     TAGAPPSELF PGPGERSLVG FGPPVPAKDT ETRERMEAME KQIASLTGLV QSALLRGSEP
     ETPSEKVEGS NGAATPSAPV CGSGSKSSGA TPVSGPPPPS ASSTPAGQPT AVSRLQMQLH
     LRGLQNSASD LRGQLQQLRN VQLQNQESVR ALLKPTEADV SMRVSEAARR QEDPLQRQRT
     LVEEERLRYL NDEELITQQL NDLEKSVEKI QRDVAHNHRL MPGPELEEKA LVLKQLGETL
     TELKAHFPGL QSKMRVVLRV EVEAVKFLKE EPQRLDGLLK RCRGVTDTLA QIRRQVDEGM
     WPPPNNLLNQ SPKKVAAETD FSKGLDFEIP PPSPPLNLHE LSGPAEGTPL TPKSTNPTKC
     LDASSKRNTD KAVSVEAAER DWEEKRAALT QYSAKDINRL LEETQAELLK AIPDLDCASK
     THPGPAPTPD HKPPKAPHGQ KAAPRTEPSG RRGSDELTVP RYRTEKPSKS PPPPPPRRSF
     PSSHGLTTTR TGEVVVTSKK DSVFIKKAES EELEVQKPQV KLRRAVSEVV RPASTPPIMA
     SAIKDEDDEE RIIAELESGG SSVPPMKVVT PGASRLKAAQ GPAGSPDKGK HGKQRTEYMR
     IQAQQQATKP SKEVSGPNET SSPGSEKPSG SRTSIPVLTS FGARNSSISF
//