MTAP2_RAT
ID MTAP2_RAT Reviewed; 1861 AA.
AC P15146;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 25-MAY-2022, entry version 179.
DE RecName: Full=Microtubule-associated protein 2;
DE Short=MAP-2;
GN Name=Map2; Synonyms=Mtap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=2339070; DOI=10.1093/nar/18.9.2822;
RA Kindler S., Schwanke B., Schulz B., Garner C.C.;
RT "Complete cDNA sequence encoding rat high and low molecular weight MAP2.";
RL Nucleic Acids Res. 18:2822-2822(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=2174050; DOI=10.1016/s0021-9258(17)45425-1;
RA Kindler S., Schulz B., Goedert M., Garner C.C.;
RT "Molecular structure of microtubule-associated protein 2b and 2c from rat
RT brain.";
RL J. Biol. Chem. 265:19679-19684(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=2326166; DOI=10.1093/nar/18.2.361;
RA Doll T., Papandrikopoulou A., Matus A.;
RT "Nucleotide and amino acid sequences of embryonic rat MAP2c.";
RL Nucleic Acids Res. 18:361-361(1990).
RN [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2770869; DOI=10.1038/340650a0;
RA Papandrikopoulou A., Doll T., Tucker R.P., Garner C.C., Matus A.;
RT "Embryonic MAP2 lacks the cross-linking sidearm sequences and dendritic
RT targeting signal of adult MAP2.";
RL Nature 340:650-652(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1695-1725 (ISOFORM 1).
RX PubMed=8282767; DOI=10.1242/jcs.106.2.633;
RA Doll T., Meichsner M., Riederer B.M., Honegger P., Matus A.;
RT "An isoform of microtubule-associated protein 2 (MAP2) containing four
RT repeats of the tubulin-binding motif.";
RL J. Cell Sci. 106:633-640(1993).
RN [6]
RP PHOSPHORYLATION AT SER-1682.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9108484; DOI=10.1016/s0092-8674(00)80208-1;
RA Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.;
RT "MARK - a novel family of protein kinases that phosphorylate microtubule-
RT associated proteins and trigger microtubule disruption.";
RL Cell 89:297-308(1997).
RN [7]
RP PHOSPHORYLATION AT SER-319; SER-350 AND SER-382 (ISOFORM 3).
RX PubMed=11029056; DOI=10.1091/mbc.11.10.3573;
RA Ozer R.S., Halpain S.;
RT "Phosphorylation-dependent localization of microtubule-associated protein
RT MAP2c to the actin cytoskeleton.";
RL Mol. Biol. Cell 11:3573-3587(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-136; SER-140;
RP SER-221; SER-224; SER-348; SER-498; SER-522; SER-610; SER-628; SER-741;
RP SER-884; SER-893; SER-939; SER-1051; SER-1140; SER-1141; THR-1161;
RP SER-1162; SER-1353; THR-1359; SER-1541; THR-1611; THR-1622; THR-1625;
RP THR-1652; SER-1656; SER-1816; SER-1824; SER-1829 AND SER-1842, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize
CC the microtubules against depolymerization. They also seem to have a
CC stiffening effect on microtubules.
CC -!- SUBUNIT: Interacts with KNDC1 (via KIND2); the interaction enhances
CC MAP2 phosphorylation and localizes KNDC1 to dendrites. Interacts with
CC DPYSL5 (By similarity). {ECO:0000250|UniProtKB:P11137,
CC ECO:0000250|UniProtKB:P20357}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:P20357}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=MAP2x;
CC IsoId=P15146-1; Sequence=Displayed;
CC Name=2; Synonyms=MAP2b;
CC IsoId=P15146-2; Sequence=VSP_003199;
CC Name=3; Synonyms=MAP2c;
CC IsoId=P15146-3; Sequence=VSP_003198, VSP_003199;
CC Name=4; Synonyms=MAP2d;
CC IsoId=P15146-4; Sequence=VSP_003198;
CC -!- DEVELOPMENTAL STAGE: Isoform 3/MAP2c is expressed during embryonic
CC brain development and until postanatal day 10. Isoform 2 is expressed
CC throughout brain development.
CC -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
CC MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing
CC detachment from microtubules, and their disassembly. Isoform 3/MAP2c is
CC probably phosphorylated by PKA at Ser-319, Ser-350 and Ser-382 and by
CC FYN at Tyr-67. The interaction with KNDC1 enhances MAP2 threonine
CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:P20357,
CC ECO:0000269|PubMed:11029056, ECO:0000269|PubMed:9108484}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51842; CAA36135.1; -; mRNA.
DR EMBL; X17682; CAA35667.1; -; mRNA.
DR EMBL; X71487; CAA50588.1; -; mRNA.
DR PIR; A37981; A37981.
DR PIR; I55502; S33176.
DR RefSeq; XP_008765430.1; XM_008767208.2. [P15146-3]
DR AlphaFoldDB; P15146; -.
DR SASBDB; P15146; -.
DR BioGRID; 247625; 7.
DR IntAct; P15146; 6.
DR MINT; P15146; -.
DR STRING; 10116.ENSRNOP00000050877; -.
DR iPTMnet; P15146; -.
DR PhosphoSitePlus; P15146; -.
DR SwissPalm; P15146; -.
DR PaxDb; P15146; -.
DR PRIDE; P15146; -.
DR GeneID; 25595; -.
DR UCSC; RGD:3044; rat. [P15146-1]
DR CTD; 4133; -.
DR RGD; 3044; Map2.
DR eggNOG; KOG2418; Eukaryota.
DR InParanoid; P15146; -.
DR PhylomeDB; P15146; -.
DR PRO; PR:P15146; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IMP:CAFA.
DR GO; GO:0097440; C:apical dendrite; ISO:RGD.
DR GO; GO:0150014; C:apical distal dendrite; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043203; C:axon hillock; IDA:ARUK-UCL.
DR GO; GO:0043194; C:axon initial segment; IDA:ARUK-UCL.
DR GO; GO:0097441; C:basal dendrite; IDA:ARUK-UCL.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0044307; C:dendritic branch; IDA:ARUK-UCL.
DR GO; GO:1902737; C:dendritic filopodium; IDA:ARUK-UCL.
DR GO; GO:0044294; C:dendritic growth cone; IDA:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; IDA:ARUK-UCL.
DR GO; GO:0150002; C:distal dendrite; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IMP:CAFA.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0034399; C:nuclear periphery; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0150001; C:primary dendrite; IDA:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:1990635; C:proximal dendrite; IDA:ARUK-UCL.
DR GO; GO:1990769; C:proximal neuron projection; IDA:ARUK-UCL.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; IMP:CAFA.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IMP:CAFA.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IMP:CAFA.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0021954; P:central nervous system neuron development; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:ARUK-UCL.
DR GO; GO:1904527; P:negative regulation of microtubule binding; IDA:ARUK-UCL.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:CAFA.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IMP:ARUK-UCL.
DR GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; IMP:ARUK-UCL.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IMP:ARUK-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR DisProt; DP00122; -.
DR InterPro; IPR030797; MAP2.
DR InterPro; IPR013588; MAP2_projctn.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR PANTHER; PTHR11501:SF15; PTHR11501:SF15; 2.
DR Pfam; PF08377; MAP2_projctn; 1.
DR Pfam; PF00418; Tubulin-binding; 4.
DR PROSITE; PS00229; TAU_MAP_1; 3.
DR PROSITE; PS51491; TAU_MAP_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1861
FT /note="Microtubule-associated protein 2"
FT /id="PRO_0000072749"
FT REPEAT 1664..1694
FT /note="Tau/MAP 1"
FT REPEAT 1695..1725
FT /note="Tau/MAP 2"
FT REPEAT 1726..1756
FT /note="Tau/MAP 3"
FT REPEAT 1757..1788
FT /note="Tau/MAP 4"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..747
FT /note="Interaction with KNDC1"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT REGION 766..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1474
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 1816..1835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 736
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1359
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1608
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1611
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1622
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1625
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1682
FT /note="Phosphoserine; by MARK1"
FT /evidence="ECO:0000269|PubMed:9108484"
FT MOD_RES 1816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20357"
FT MOD_RES 1824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 152..1514
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:2326166"
FT /id="VSP_003198"
FT VAR_SEQ 1695..1725
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:2174050,
FT ECO:0000303|PubMed:2326166, ECO:0000303|PubMed:2339070"
FT /id="VSP_003199"
FT MOD_RES P15146-3:319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11029056"
FT MOD_RES P15146-3:350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11029056"
FT MOD_RES P15146-3:382
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11029056"
SQ SEQUENCE 1861 AA; 202411 MW; 42DCF116D21EF54E CRC64;
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGSGEG LSRSANGFPY REEEEGAFGE
HGSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQP
AALPLAAEET VNLPPSPPPS PASEQTAALE EDLLTASKME FPEQQKLPSS FAEPLDKEET
EFKMQSKPGE DFEHAALVPQ PDTSKTPQDK KDPQDMEGEK SPASPFAQTF GTNLEDIKQI
TEPSITVPSI GLSAEPLAPK DQKDWFIEMP VESKKDEWGL AAPISPGPLT PMREKDVLED
IPRWEGKQFD SPMPSPFHGG SFTLPLDTVK DERVTEGSQP FAPVFFQSDD KMSLQDTSGS
ATSKESSKDE EPQKDKADKV ADVPVSEATT VLGDVHSPAV EGFVGENISG EEKGTTDQEK
KETSTPSVQE PTLTETEPQT KLEETSKVSI EETVAKEEES LKLKDDKAGV IQTSTEQSFS
KEDQKGQEQT IEALKQDSFP ISLEQAVTDA AMATKTLEKV TSEPEAVSEK REIQGLFEED
IADKSKLEGA GSATVAEVEM PFYEDKSGMS KYFETSALKE DVTRSTGLGS DYYELSDSRG
NAQESLDTVS PKNQQDEKEL LAKASQPSPP AHEAGYSTLA QSYTSDHPSE LPEEPSSPQE
RMFTIDPKVY GEKRDLHSKN KDDLTLSRSL GLGGRSAIEQ RSMSINLPMS CLDSIALGFN
FGRGHDLSPL ASDILTNTSG SMDEGDDYLP PTTPAVEKIP CFPIESKEEE DKTEQAKVTG
GQTTQVETSS ESPFPAKEYY KNGTVMAPDL PEMLDLAGTR SRLASVSADA EVARRKSVPS
EAVVAESSTG LPPVADDSQP VKPDSQLEDM GYCVFNKYTV PLPSPVQDSE NLSGESGSFY
EGTDDKVRRD LATDLSLIEV KLAAAGRVKD EFTAEKEASP PSSADKSGLS REFDQDRKAN
DKLDTVLEKS EEHVDSKEHA KESEEVGDKV ELFGLGVTYE QTSAKELITT KETAPERAEK
GLSSVPEVAE VETTTKADQG LDVAAKKDDQ SPLDIKVSDF GQMASGMSVD AGKTIELKFE
VDQQLTLSSE APQETDSFMG IESSHVKDGA KVSETEVKEK VAKPDLVHQE AVDKEESYES
SGEHESLTME SLKPDEGKKE TSPETSLIQD EVALKLSVEI PCPPPVSEAD SSIDEKAEVQ
MEFIQLPKEE STETPDIPAI PSDVTQPQPE AVVSEPAEVR GEEEEIEAEG EYDKLLFRSD
TLQITDLLVP GSREEFVETC PGEHKGVVES VVTIEDDFIT VVQTTTDEGE LGSHSVRFAA
PVQPEEERRP YPHDEELEVL MAAEAQAEPK DGSPDAPATP EKEEVPFSEY KTETYDDYKD
ETTIDDSIMD ADSLWVDTQD DDRSILTEQL ETIPKEERAE KEARRPSLEK HRKEKPFKTG
RGRISTPERR EVAKKEPSTV SRDEVRRKKA VYKKAELAKE SEVQAHSPSR KLILKPAIKY
TRPTHLSCVK RKTTATSGES AQAPSAFKQA KDKVTDGITK SPEKRSSLPR PSSILPPRRG
VSGDREENSF SLNSSISSAR RTTRSEPIRR AGKSGTSTPT TPGSTAITPG TPPSYSSRTP
GTPGTPSYPR TPGTPKSGIL VPSEKKVAII RTPPKSPATP KQLRLINQPL PDLKNVKSKI
GSTDNIKYQP KGGQVRILNK KMDFSKVQSR CGSKDNIKHS AGGGNVQIVT KKIDLSHVTS
KCGSLKNIRH RPGGGRVKIE SVKLDFKEKA QAKVGSLDNA HHVPGGGNVK IDSQKLNFRE
HAKARVDHGA EIITQSPSRS SVASPRRLSN VSSSGSINLL ESPQLATLAE DVTAALAKQG
L
