HD_MOUSE
ID HD_MOUSE Reviewed; 3119 AA.
AC P42859;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Huntingtin;
DE AltName: Full=Huntington disease protein homolog;
DE Short=HD protein homolog;
DE Contains:
DE RecName: Full=Huntingtin, myristoylated N-terminal fragment {ECO:0000250|UniProtKB:P42858};
GN Name=Htt; Synonyms=Hd, Hdh;
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] (ISOFORMS LONG AND SHORT).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Spleen;
RX PubMed=8162057; DOI=10.1093/hmg/3.1.85;
RA Lin B., Nasir J., Macdonald H., Hutchinson G., Graham R.K., Rommens J.M.,
RA Hayden M.R.;
RT "Sequence of the murine Huntington disease gene: evidence for conservation,
RT alternate splicing and polymorphism in a triplet (CCG) repeat.";
RL Hum. Mol. Genet. 3:85-92(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RX PubMed=8009370; DOI=10.1007/bf02290678;
RA Barnes G.T., Duyao M.P., Ambrose C.M., McNeil S., Persichetti F.,
RA Srinidhi J., Gusella J.F., Macdonald M.E.;
RT "Mouse Huntington's disease gene homolog (Hdh).";
RL Somat. Cell Mol. Genet. 20:87-97(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7647777; DOI=10.1038/ng0595-104;
RA Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
RA Agid Y., Hirsch E.C., Mandel J.-L.;
RT "Cellular localization of the Huntington's disease protein and
RT discrimination of the normal and mutated form.";
RL Nat. Genet. 10:104-110(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RX PubMed=7759106; DOI=10.1016/0888-7543(95)80014-d;
RA Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P.,
RA Hayden M.R.;
RT "Structural analysis of the 5' region of mouse and human Huntington disease
RT genes reveals conservation of putative promoter region and di- and
RT trinucleotide polymorphisms.";
RL Genomics 25:707-715(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11035034; DOI=10.1074/jbc.m008099200;
RA Peters M.F., Ross C.A.;
RT "Isolation of a 40-kDa Huntingtin-associated protein.";
RL J. Biol. Chem. 276:3188-3194(2001).
RN [6]
RP INTERACTION WITH SH3GLB1.
RX PubMed=12456676; DOI=10.1074/jbc.m208568200;
RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT "Characterization of endophilin B1b, a brain-specific membrane-associated
RT lysophosphatidic acid acyl transferase with properties distinct from
RT endophilin A1.";
RL J. Biol. Chem. 278:4160-4167(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-398; SER-411 AND
RP SER-1853, AND IDENTIFICATION BY MASS 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).
RN [9]
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).
CC -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated
CC transport or vesicle function. {ECO:0000250|UniProtKB:P42858}.
CC -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the
CC formation of autophagic vesicles. {ECO:0000250|UniProtKB:P42858}.
CC -!- SUBUNIT: Interacts with PFN1 (By similarity). Interacts through its N-
CC terminus with PRPF40A (By similarity). Interacts with PQBP1 (By
CC similarity). Interacts with SETD2 (By similarity). Interacts with
CC SH3GLB1 (PubMed:12456676). Interacts with SYVN (By similarity).
CC Interacts with TPR; the interaction is inhibited by forms of Huntingtin
CC with expanded polyglutamine stretch (By similarity). Interacts with
CC ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17
CC (via ANK repeats) (PubMed:26198635). Interacts with F8A1/F8A2/F8A3 (By
CC similarity). Found in a complex with F8A1/F8A2/F8A3, HTT and RAB5A;
CC mediates the recruitment of HTT by RAB5A (By similarity).
CC {ECO:0000250|UniProtKB:P42858, ECO:0000269|PubMed:12456676,
CC ECO:0000269|PubMed:26198635}.
CC -!- INTERACTION:
CC P42859; P70677: Casp3; NbExp=2; IntAct=EBI-5327353, EBI-1790419;
CC P42859; Q02248: Ctnnb1; NbExp=3; IntAct=EBI-5327353, EBI-397872;
CC P42859; Q8CIN4: Pak2; NbExp=2; IntAct=EBI-5327353, EBI-1559317;
CC P42859; O70405: Ulk1; NbExp=4; IntAct=EBI-5327353, EBI-8390771;
CC -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm
CC {ECO:0000269|PubMed:11035034}. Nucleus {ECO:0000250|UniProtKB:P42858}.
CC Note=Shuttles between cytoplasm and nucleus in a Ran GTPase-independent
CC manner. {ECO:0000250|UniProtKB:P42858}.
CC -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]:
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:P42858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P42859-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P42859-2; Sequence=VSP_004282;
CC -!- TISSUE SPECIFICITY: The highest level is seen throughout the brain, but
CC it is also found in the stomach, heart, testis, adipose tissue, muscle,
CC spleen, liver, and kidney.
CC -!- DEVELOPMENTAL STAGE: Predominant expression in neuronal tissues at all
CC developmental stages. In 14.5 day old embryos, it is also detected in
CC non-neuronal tissues. This expression is down-regulated in later stages
CC of development.
CC -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC conformational flexibility and is likely to exist in a fluctuating
CC equilibrium of alpha-helical, random coil, and extended conformations.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: Phosphorylation at Ser-1159 and Ser-1179 by CDK5 in response to
CC DNA damage in nuclei of neurons protects neurons against polyglutamine
CC expansion as well as DNA damage mediated toxicity.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine
CC stretch. {ECO:0000250|UniProtKB:P42858}.
CC -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at
CC Gly-530, following proteolytic cleavage at Asp-529.
CC {ECO:0000250|UniProtKB:P42858}.
CC -!- POLYMORPHISM: The poly-Gln region does not appear to be polymorphic,
CC explaining the absence of a murine HD-like disorder (PubMed:8009370).
CC {ECO:0000269|PubMed:8009370}.
CC -!- MISCELLANEOUS: [Isoform Short]: Cannot be explained by a simple
CC splicing event. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
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DR EMBL; L23312; AAA37799.1; -; mRNA.
DR EMBL; L23313; AAA37800.1; -; mRNA.
DR EMBL; L28827; AAA89100.1; ALT_SEQ; mRNA.
DR EMBL; U24233; AAC52218.1; -; mRNA.
DR EMBL; AH003368; AAA91085.1; -; Genomic_DNA.
DR PIR; I49729; I49729.
DR BMRB; P42859; -.
DR SMR; P42859; -.
DR CORUM; P42859; -.
DR DIP; DIP-41430N; -.
DR IntAct; P42859; 22.
DR MINT; P42859; -.
DR STRING; 10090.ENSMUSP00000078945; -.
DR ChEMBL; CHEMBL1250362; -.
DR iPTMnet; P42859; -.
DR PhosphoSitePlus; P42859; -.
DR SwissPalm; P42859; -.
DR EPD; P42859; -.
DR jPOST; P42859; -.
DR MaxQB; P42859; -.
DR PaxDb; P42859; -.
DR PeptideAtlas; P42859; -.
DR PRIDE; P42859; -.
DR ProteomicsDB; 269778; -. [P42859-1]
DR ProteomicsDB; 269779; -. [P42859-2]
DR MGI; MGI:96067; Htt.
DR eggNOG; ENOG502QR1D; Eukaryota.
DR InParanoid; P42859; -.
DR PhylomeDB; P42859; -.
DR ChiTaRS; Htt; mouse.
DR PRO; PR:P42859; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P42859; protein.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; IDA:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0050809; F:diazepam binding; IMP:MGI.
DR GO; GO:0034452; F:dynactin binding; ISO:MGI.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0005522; F:profilin binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0000052; P:citrulline metabolic process; IMP:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:MGI.
DR GO; GO:0016197; P:endosomal transport; IMP:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0051028; P:mRNA transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0021990; P:neural plate formation; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IMP:MGI.
DR GO; GO:0021988; P:olfactory lobe development; IMP:MGI.
DR GO; GO:0048341; P:paraxial mesoderm formation; IMP:MGI.
DR GO; GO:0030072; P:peptide hormone secretion; IMP:MGI.
DR GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:1904504; P:positive regulation of lipophagy; ISO:MGI.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; IMP:MGI.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IMP:MGI.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; ISO:MGI.
DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1904580; P:regulation of intracellular mRNA localization; ISO:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:ARUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; IMP:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0021756; P:striatum development; IMP:MGI.
DR GO; GO:0000050; P:urea cycle; IMP:MGI.
DR GO; GO:0047496; P:vesicle transport along microtubule; IDA:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000091; Huntingtin.
DR InterPro; IPR028426; Huntingtin_fam.
DR InterPro; IPR024613; Huntingtin_middle-repeat.
DR PANTHER; PTHR10170; PTHR10170; 1.
DR Pfam; PF12372; DUF3652; 1.
DR PRINTS; PR00375; HUNTINGTIN.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Lipoprotein; Myristate; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..3119
FT /note="Huntingtin"
FT /id="PRO_0000083943"
FT CHAIN 530..563
FT /note="Huntingtin, myristoylated N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT /id="PRO_0000447487"
FT REPEAT 183..220
FT /note="HEAT 1"
FT REPEAT 225..262
FT /note="HEAT 2"
FT REPEAT 782..819
FT /note="HEAT 3"
FT REPEAT 882..920
FT /note="HEAT 4"
FT REPEAT 1404..1441
FT /note="HEAT 5"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..481
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT REGION 495..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2610..2637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2372..2381
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 24..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 490..491
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT SITE 507..508
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 529..530
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT SITE 563..564
FT /note="Cleavage; by caspase-6"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1159
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1179
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT MOD_RES 1853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 530
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P42858"
FT VAR_SEQ 1522..2001
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8162057"
FT /id="VSP_004282"
FT CONFLICT 2
FT /note="A -> G (in Ref. 1; AAA37799/AAA37800 and 4;
FT AAA91085)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> P (in Ref. 2; AAA89100)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="N -> D (in Ref. 2; AAA89100 and 4; AAA91085)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="M -> L (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="S -> P (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="A -> P (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="A -> P (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="A -> T (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="D -> E (in Ref. 2; AAA89100)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="S -> R (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="W -> C (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240
FT /note="T -> N (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 1384
FT /note="N -> T (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 1827
FT /note="H -> Y (in Ref. 1; AAA37799)"
FT /evidence="ECO:0000305"
FT CONFLICT 1979..1980
FT /note="PF -> SS (in Ref. 1; AAA37799)"
FT /evidence="ECO:0000305"
FT CONFLICT 2062
FT /note="D -> G (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2570
FT /note="S -> N (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2866
FT /note="E -> V (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2877
FT /note="V -> G (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2882
FT /note="D -> G (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2887
FT /note="Q -> H (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2915
FT /note="A -> T (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 3025
FT /note="P -> S (in Ref. 3; AAC52218)"
FT /evidence="ECO:0000305"
FT CONFLICT 3062..3063
FT /note="QV -> LM (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
FT CONFLICT 3095..3096
FT /note="VV -> EE (in Ref. 1; AAA37799/AAA37800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3119 AA; 344690 MW; ECA42B5916F50F4F CRC64;
MATLEKLMKA FESLKSFQQQ QQQQPPPQAP PPPPPPPPQP PQPPPQGQPP PPPPPLPGPA
EEPLHRPKKE LSATKKDRVN HCLTICENIV AQSLRNSPEF QKLLGIAMEL FLLCSNDAES
DVRMVADECL NKVIKALMDS NLPRLQLELY KEIKKNGAPR SLRAALWRFA ELAHLVRPQK
CRPYLVNLLP CLTRTSKRPE ESVQETLAAA VPKIMASFGN FANDNEIKVL LKAFIANLKS
SSPTVRRTAA GSAVSICQHS RRTQYFYNWL LNVLLGLLVP MEEEHSTLLI LGVLLTLRCL
VPLLQQQVKD TSLKGSFGVT RKEMEVSPST EQLVQVYELT LHHTQHQDHN VVTGALELLQ
QLFRTPPPEL LQALTTPGGL GQLTLVQEEA RGRGRSGSIV ELLAGGGSSC SPVLSRKQKG
KVLLGEEEAL EDDSESRSDV SSSAFAASVK SEIGGELAAS SGVSTPGSVG HDIITEQPRS
QHTLQADSVD LSGCDLTSAA TDGDEEDILS HSSSQFSAVP SDPAMDLNDG TQASSPISDS
SQTTTEGPDS AVTPSDSSEI VLDGADSQYL GMQIGQPQED DEEGAAGVLS GEVSDVFRNS
SLALQQAHLL ERMGHSRQPS DSSIDKYVTR DEVAEASDPE SKPCRIKGDI GQPNDDDSAP
LVHCVRLLSA SFLLTGEKKA LVPDRDVRVS VKALALSCIG AAVALHPESF FSRLYKVPLN
TTESTEEQYV SDILNYIDHG DPQVRGATAI LCGTLVYSIL SRSRLRVGDW LGNIRTLTGN
TFSLVDCIPL LQKTLKDESS VTCKLACTAV RHCVLSLCSS SYSDLGLQLL IDMLPLKNSS
YWLVRTELLD TLAEIDFRLV SFLEAKAESL HRGAHHYTGF LKLQERVLNN VVIYLLGDED
PRVRHVAATS LTRLVPKLFY KCDQGQADPV VAVARDQSSV YLKLLMHETQ PPSHFSVSTI
TRIYRGYSLL PSITDVTMEN NLSRVVAAVS HELITSTTRA LTFGCCEALC LLSAAFPVCT
WSLGWHCGVP PLSASDESRK SCTVGMASMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS
APKSLRSSWT SEEEANSAAT RQEEIWPALG DRTLVPLVEQ LFSHLLKVIN ICAHVLDDVT
PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASTPMSP KKVGEASAAS RQSDTSGPVT
ASKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST EKFGGFLRSA LDVLSQILEL
ATLQDIGKCV EEVLGYLKSC FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQC
RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQERDASGW FDVLQKVSAQ
LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT SVQLQKQVLD LLAQLVQLRV
NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF LVLLSYERYH SKQIIGIPKI
IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA GKELETQKEV VVSMLLRLIQ
YHQVLEMFIL VLQQCHKENE DKWKRLSRQV ADIILPMLAK QQMHIDSHEA LGVLNTLFEI
LAPSSLRPVD MLLRSMFITP STMASVSTVQ LWISGILAIL RVLISQSTED IVLCRIQELS
FSPHLLSCPV INRLRGGGGN VTLGECSEGK QKSLPEDTFS RFLLQLVGIL LEDIVTKQLK
VDMSEQQHTF YCQELGTLLM CLIHIFKSGM FRRITAAATR LFTSDGCEGS FYTLESLNAR
VRSMVPTHPA LVLLWCQILL LINHTDHRWW AEVQQTPKRH SLSCTKSLNP QKSGEEEDSG
SAAQLGMCNR EIVRRGALIL FCDYVCQNLH DSEHLTWLIV NHIQDLISLS HEPPVQDFIS
AIHRNSAASG LFIQAIQSRC ENLSTPTTLK KTLQCLEGIH LSQSGAVLTL YVDRLLGTPF
RALARMVDTL ACRRVEMLLA ANLQSSMAQL PEEELNRIQE HLQNSGLAQR HQRLYSLLDR
FRLSTVQDSL SPLPPVTSHP LDGDGHTSLE TVSPDKDWYL QLVRSQCWTR SDSALLEGAE
LVNRIPAEDM NDFMMSSEFN LSLLAPCLSL GMSEIANGQK SPLFEAARGV ILNRVTSVVQ
QLPAVHQVFQ PFLPIEPTAY WNKLNDLLGD TTSYQSLTIL ARALAQYLVV LSKVPAHLHL
PPEKEGDTVK FVVMTVEALS WHLIHEQIPL SLDLQAGLDC CCLALQVPGL WGVLSSPEYV
THACSLIHCV RFILEAIAVQ PGDQLLGPES RSHTPRAVRK EEVDSDIQNL SHVTSACEMV
ADMVESLQSV LALGHKRNST LPSFLTAVLK NIVISLARLP LVNSYTRVPP LVWKLGWSPK
PGGDFGTVFP EIPVEFLQEK EILKEFIYRI NTLGWTNRTQ FEETWATLLG VLVTQPLVME
QEESPPEEDT ERTQIHVLAV QAITSLVLSA MTVPVAGNPA VSCLEQQPRN KPLKALDTRF
GRKLSMIRGI VEQEIQEMVS QRENTATHHS HQAWDPVPSL LPATTGALIS HDKLLLQINP
EREPGNMSYK LGQVSIHSVW LGNNITPLRE EEWDEEEEEE SDVPAPTSPP VSPVNSRKHR
AGVDIHSCSQ FLLELYSRWI LPSSAARRTP VILISEVVRS LLVVSDLFTE RTQFEMMYLT
LTELRRVHPS EDEILIQYLV PATCKAAAVL GMDKTVAEPV SRLLESTLRS SHLPSQIGAL
HGILYVLECD LLDDTAKQLI PVVSDYLLSN LKGIAHCVNI HSQQHVLVMC ATAFYLMENY
PLDVGPEFSA SVIQMCGVML SGSEESTPSI IYHCALRGLE RLLLSEQLSR LDTESLVKLS
VDRVNVQSPH RAMAALGLML TCMYTGKEKA SPGRASDPSP ATPDSESVIV AMERVSVLFD
RIRKGFPCEA RVVARILPQF LDDFFPPQDV MNKVIGEFLS NQQPYPQFMA TVVYKVFQTL
HSAGQSSMVR DWVMLSLSNF TQRTPVAMAM WSLSCFLVSA STSPWVSAIL PHVISRMGKL
EQVDVNLFCL VATDFYRHQI EEEFDRRAFQ SVFEVVAAPG SPYHRLLACL QNVHKVTTC
