MAP6_MOUSE
ID MAP6_MOUSE Reviewed; 906 AA.
AC Q7TSJ2; O55129; O70586; O70587; Q78DV4; Q78DV5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Microtubule-associated protein 6;
DE Short=MAP-6;
DE AltName: Full=Stable tubule-only polypeptide;
DE Short=STOP;
GN Name=Map6; Synonyms=Mtap6;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9501006; DOI=10.1006/bbrc.1998.8179;
RA Denarier E., Aguezzoul M., Jolly C., Vourc'h C., Roure A., Andrieux A.,
RA Bosc C., Job D.;
RT "Genomic structure and chromosomal mapping of the mouse STOP gene
RT (Mtap6).";
RL Biochem. Biophys. Res. Commun. 243:791-796(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Swiss Webster / NIH; TISSUE=Fibroblast;
RX PubMed=9600916; DOI=10.1073/pnas.95.11.6055;
RA Denarier E., Fourest-Lieuvin A., Bosc C., Pirollet F., Chapel A.,
RA Margolis R.L., Job D.;
RT "Nonneuronal isoforms of STOP protein are responsible for microtubule cold
RT stability in mammalian fibroblasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6055-6060(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=12231625; DOI=10.1101/gad.223302;
RA Andrieux A., Salin P.A., Vernet M., Kujala P., Baratier J., Gory-Faure S.,
RA Bosc C., Pointu H., Proietto D., Schweitzer A., Denarier E., Klumperman J.,
RA Job D.;
RT "The suppression of brain cold-stable microtubules in mice induces synaptic
RT defects associated with neuroleptic-sensitive behavioral disorders.";
RL Genes Dev. 16:2350-2364(2002).
RN [5]
RP INTERACTION WITH CALMODULIN.
RX PubMed=14516200; DOI=10.1021/bi034746w;
RA Bouvier D., Vanhaverbeke C., Simorre J.P., Arlaud G.J., Bally I., Forge V.,
RA Margolis R.L., Gans P., Kleman J.P.;
RT "Unusual Ca(2+)-calmodulin binding interactions of the microtubule-
RT associated protein F-STOP.";
RL Biochemistry 42:11484-11493(2003).
RN [6]
RP ALTERNATIVE PROMOTER USAGE, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=12782132; DOI=10.1016/s0888-7543(03)00053-3;
RA Aguezzoul M., Andrieux A., Denarier E.;
RT "Overlap of promoter and coding sequences in the mouse STOP gene (Mtap6).";
RL Genomics 81:623-627(2003).
RN [7]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=15389836; DOI=10.1002/jnr.20260;
RA Galiano M.R., Bosc C., Schweitzer A., Andrieux A., Job D., Hallak M.E.;
RT "Astrocytes and oligodendrocytes express different STOP protein isoforms.";
RL J. Neurosci. Res. 78:329-337(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16837464; DOI=10.1074/jbc.m603380200;
RA Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D., Franck R.,
RA Denarier E., Job D., Andrieux A.;
RT "STOP-like protein 21 is a novel member of the STOP family, revealing a
RT Golgi localization of STOP proteins.";
RL J. Biol. Chem. 281:28387-28396(2006).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-207; SER-632; SER-687
RP AND SER-905, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Lung;
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28521134; DOI=10.1016/j.neuron.2017.04.042;
RA Tortosa E., Adolfs Y., Fukata M., Pasterkamp R.J., Kapitein L.C.,
RA Hoogenraad C.C.;
RT "Dynamic palmitoylation targets MAP6 to the axon to promote microtubule
RT stabilization during neuronal polarization.";
RL Neuron 94:809-825(2017).
CC -!- FUNCTION: Involved in microtubule stabilization in many cell types,
CC including neuronal cells (PubMed:9600916). Specifically has microtubule
CC cold stabilizing activity (PubMed:9600916). Involved in dendrite
CC morphogenesis and maintenance by regulating lysosomal trafficking via
CC its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated
CC axonal cargo transport (By similarity). Regulates axonal growth during
CC neuron polarization (PubMed:28521134). {ECO:0000250|UniProtKB:Q63560,
CC ECO:0000250|UniProtKB:Q96JE9, ECO:0000269|PubMed:28521134,
CC ECO:0000269|PubMed:9600916}.
CC -!- SUBUNIT: Interacts with calmodulin (via C-terminus); the interaction is
CC dependent on Ca(2+) (PubMed:14516200). Interacts with TMEM106B (By
CC similarity). Interacts with ZDHHC13 (via ANK repeats)
CC (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
CC (PubMed:26198635). {ECO:0000250|UniProtKB:Q96JE9,
CC ECO:0000269|PubMed:14516200, ECO:0000269|PubMed:26198635}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9600916}. Golgi apparatus
CC {ECO:0000269|PubMed:16837464}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q63560}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63560}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:Q63560}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q63560}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q63560}. Note=Isoform 1 and isoform 2 associate
CC with axonal microtubules in neurons (PubMed:16837464). Isoform 3
CC associates with microtubules in fibroblasts (PubMed:9600916). Localizes
CC predominantly in the proximal part of the axon (By similarity).
CC Preferentially is concentrated on a portion of the microtubule polymer
CC in which tubulin is modified by detyrosination and acetylation and is
CC also resistant to depolymerization induced by both nocodazole and cold
CC (By similarity). In unpolarized neurons, localizes to the Golgi and to
CC secretory vesicles accumulating transiently at the tips of a subset of
CC neurites (By similarity). Following neuronal polarization and during
CC axon outgrowth, accumulates in the axonal growth cone and subsequently
CC localizes throughout the axon. Partially localizes to dendrites in
CC mature neurons (By similarity). {ECO:0000250|UniProtKB:Q63560,
CC ECO:0000269|PubMed:16837464, ECO:0000269|PubMed:9600916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Comment=Comment: Additional isoforms seem to exist.;
CC Name=1; Synonyms=N-STOP, Neuronal STOP;
CC IsoId=Q7TSJ2-1; Sequence=Displayed;
CC Name=2; Synonyms=E-STOP, Early STOP;
CC IsoId=Q7TSJ2-2; Sequence=VSP_034727;
CC Name=3; Synonyms=F-STOP, Fibroblastic STOP;
CC IsoId=Q7TSJ2-3; Sequence=VSP_034724, VSP_034725, VSP_034726;
CC -!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in adult brain.
CC Isoform 2 is predominantly expressed in embryonic brain; expression
CC persists at low levels in the adult brain. Isoform 3 is expressed at
CC high levels in lung and at lower levels in testis, heart, muscle and
CC kidney (at protein level). Oligodendrocytes express a major isoform of
CC 89 kDa (O-STOP). Astrocytes also express an isoform of 60 kDa (A-STOP).
CC {ECO:0000269|PubMed:12782132, ECO:0000269|PubMed:15389836}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in embryonic brain.
CC {ECO:0000269|PubMed:12782132}.
CC -!- PTM: Palmitoylated. Probably depalmitoylated by ABHD17A, ABHD17B and
CC ABHD17C. During neuronal polarization, palmitoylation and
CC depalmitoylation cycles regulate MAP6 shuttling between secretory
CC vesicles and microtubules, and its polarized distribution in the axon.
CC {ECO:0000250|UniProtKB:Q63560}.
CC -!- DISRUPTION PHENOTYPE: Mice are devoid of cold-stable microtubules and
CC show no detectable defects in brain anatomy but show synaptic defects,
CC with depleted synaptic vesicle pools and impaired synaptic plasticity,
CC associated with severe behavioral disorders, including a disorganized
CC activity with disruption of normal behavioral sequences and episodes of
CC hyperlocomotion or apparent prostration, anxiety, severe social
CC withdrawal and complete nurturing defects (PubMed:12231625). The
CC behavioral defects are alleviated by long-term treatment with
CC neuroleptics (PubMed:12231625). RNAi-mediated knockdown in brain at the
CC 14.5 dpc stage disrupts proper neuron migration resulting in their
CC accumulation in the ventricular and subventricular zones
CC (PubMed:28521134). {ECO:0000269|PubMed:12231625,
CC ECO:0000269|PubMed:28521134}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the STOP family. {ECO:0000305}.
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DR EMBL; Y14754; CAA75049.1; -; Genomic_DNA.
DR EMBL; Y14755; CAA75049.1; JOINED; Genomic_DNA.
DR EMBL; Y14756; CAA75049.1; JOINED; Genomic_DNA.
DR EMBL; Y16008; CAA75930.1; -; Genomic_DNA.
DR EMBL; Y16032; CAA75989.1; -; mRNA.
DR EMBL; BC053039; AAH53039.1; -; mRNA.
DR CCDS; CCDS21479.1; -. [Q7TSJ2-1]
DR CCDS; CCDS40029.1; -. [Q7TSJ2-3]
DR CCDS; CCDS85345.1; -. [Q7TSJ2-2]
DR PIR; JC5963; JC5963.
DR RefSeq; NP_001036820.2; NM_001043355.2. [Q7TSJ2-3]
DR RefSeq; NP_001041632.1; NM_001048167.1. [Q7TSJ2-2]
DR RefSeq; NP_034967.2; NM_010837.3. [Q7TSJ2-1]
DR AlphaFoldDB; Q7TSJ2; -.
DR BioGRID; 201587; 17.
DR IntAct; Q7TSJ2; 6.
DR MINT; Q7TSJ2; -.
DR STRING; 10090.ENSMUSP00000064787; -.
DR iPTMnet; Q7TSJ2; -.
DR PhosphoSitePlus; Q7TSJ2; -.
DR SwissPalm; Q7TSJ2; -.
DR EPD; Q7TSJ2; -.
DR MaxQB; Q7TSJ2; -.
DR PaxDb; Q7TSJ2; -.
DR PeptideAtlas; Q7TSJ2; -.
DR PRIDE; Q7TSJ2; -.
DR ProteomicsDB; 295817; -. [Q7TSJ2-1]
DR ProteomicsDB; 295818; -. [Q7TSJ2-2]
DR ProteomicsDB; 295819; -. [Q7TSJ2-3]
DR Antibodypedia; 17382; 60 antibodies from 18 providers.
DR DNASU; 17760; -.
DR Ensembl; ENSMUST00000068973; ENSMUSP00000064787; ENSMUSG00000055407. [Q7TSJ2-1]
DR Ensembl; ENSMUST00000107100; ENSMUSP00000102717; ENSMUSG00000055407. [Q7TSJ2-3]
DR Ensembl; ENSMUST00000127492; ENSMUSP00000146340; ENSMUSG00000055407. [Q7TSJ2-2]
DR Ensembl; ENSMUST00000207883; ENSMUSP00000146585; ENSMUSG00000055407. [Q7TSJ2-1]
DR Ensembl; ENSMUST00000208605; ENSMUSP00000146897; ENSMUSG00000055407. [Q7TSJ2-3]
DR GeneID; 17760; -.
DR KEGG; mmu:17760; -.
DR UCSC; uc009ilg.1; mouse. [Q7TSJ2-1]
DR UCSC; uc009ili.1; mouse. [Q7TSJ2-3]
DR CTD; 4135; -.
DR MGI; MGI:1201690; Map6.
DR VEuPathDB; HostDB:ENSMUSG00000055407; -.
DR eggNOG; ENOG502QS1F; Eukaryota.
DR GeneTree; ENSGT00530000063947; -.
DR HOGENOM; CLU_018049_1_0_1; -.
DR InParanoid; Q7TSJ2; -.
DR OMA; KKPGPAW; -.
DR OrthoDB; 577082at2759; -.
DR PhylomeDB; Q7TSJ2; -.
DR TreeFam; TF338320; -.
DR BioGRID-ORCS; 17760; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Map6; mouse.
DR PRO; PR:Q7TSJ2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TSJ2; protein.
DR Bgee; ENSMUSG00000055407; Expressed in embryonic brain and 190 other tissues.
DR ExpressionAtlas; Q7TSJ2; baseline and differential.
DR Genevisible; Q7TSJ2; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005798; C:Golgi-associated vesicle; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0099503; C:secretory vesicle; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISO:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR InterPro; IPR007882; MAP6.
DR PANTHER; PTHR14759; PTHR14759; 6.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Calmodulin-binding;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Golgi apparatus; Lipoprotein; Membrane; Microtubule; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..906
FT /note="Microtubule-associated protein 6"
FT /id="PRO_0000344045"
FT REPEAT 222..267
FT /note="Mc-1"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REPEAT 268..313
FT /note="Mc-2"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REPEAT 314..359
FT /note="Mc-3"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REPEAT 360..405
FT /note="Mc-4"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 1..15
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..139
FT /note="Mn 1"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 124..138
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 151..174
FT /note="Mn 2"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 160..174
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 187..201
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 222..405
FT /note="4 X approximate tandem repeat Mc"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 235..249
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 280..294
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 325..339
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 375..389
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 427..450
FT /note="Mn 3"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 435..449
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 441..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..500
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 513..527
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT REGION 674..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q63560"
FT VAR_SEQ 1..203
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9600916"
FT /id="VSP_034724"
FT VAR_SEQ 503..509
FT /note="VEKPSVQ -> EPGQTHQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9600916"
FT /id="VSP_034725"
FT VAR_SEQ 510..906
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9600916"
FT /id="VSP_034726"
FT VAR_SEQ 569..906
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034727"
FT CONFLICT 81
FT /note="P -> L (in Ref. 1; CAA75049)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="V -> G (in Ref. 1; CAA75930)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="E -> K (in Ref. 1; CAA75930 and 2; CAA75989)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> S (in Ref. 1; CAA75049)"
FT /evidence="ECO:0000305"
FT CONFLICT 755..757
FT /note="MVP -> VVH (in Ref. 1; CAA75930)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="M -> V (in Ref. 1; CAA75049)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="P -> S (in Ref. 1; CAA75930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 96450 MW; F3CED1FCF1E2CD83 CRC64;
MAWPCITRAC CIARFWNQLD KADIAVPLVF TKYSEATEHP GAPPQPPAPL QPALAPPSRA
VAIETQPAQG ESDAVARATG PAPGPSVDRE TVAAPGRSGL GLGAASASTS GSGPADSVMR
QDYRAWKVQR PEPSCRPRSE YQPSDAPFER ETQYQKDFRA WPLPRRGDHP WIPKPVQIPA
TSQPSQPVLG VPKRRPQSQE RGPMQLSADA RDPEGAGGAG VLAAGKASGV DQRDTRRKAG
PAWMVTRNEG HEEKPLPPAQ SQTQEGGPAA GKASGADQRD TRRKAGPAWM VTRSEGHEEK
PLPPAQSQTQ EGGPAAGKAS GADQRDTRRK AGPAWMVTRT EGHEETPLPP AQSQTQEGGP
AAGKASGADE RDTRRKAGPA WMVRRSEGHE QTPAAHAQGT GPEGGKGRAV ADALNRQIRE
EVASTVSSSY RNEFRAWTDI KPVKPIKAKP QYKPPDDKMV HETSYSAQFK GEANKPSAAD
NKAMDRRRIR SLYSEPFKEC PKVEKPSVQS SKPKKTSTSH KPPRKAKDKQ VVSGQAAKKK
TTEGPSATKP DDKEQSKEMN NKLAEAKESR VKPTSDASKN RGPVTKEPHK DQGSVAPGLP
KGQEPLKDQG PVVPGLPKDQ VPVVPGSLKG QSPTAPGPTK DQGAVLLGPV KDLGPVAPAP
IKVQDHIASE LLKNKDSVPL APAKAQSPLL PEPLKNQSPV VPASTKDQSF PTPAPRKDPG
PVIPEPEKDR APTVPERRKD QHVSIMASLK NEAPMVPESV KNQGLAGPEL VKDTGTDTTA
PRYLKGHDSV FVAPVKNQGP VIPEPVKSQD PIIPALAKDQ GPMLPEPPKN QSPVVLGPIK
NQDPIIPVPL KGQDPLVPAP TKDQGPTAPD PLKTQGPKGT QLPTVSPSPP VMIPTVPHTE
YIEGSP
