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Runt-related transcription factor 2 (Acute myeloid leukemia 3 protein) (Core-binding factor subunit alpha-1) (CBF-alpha-1) (Oncogene AML-3) (Osteoblast-specific transcription factor 2) (OSF-2) (Polyomavirus enhancer-binding protein 2 alpha A subunit) (PEA2-alpha A) (PEBP2-alpha A) (SL3-3 enhancer factor 1 alpha A subunit) (SL3/AKV core-binding factor alpha A subunit)

 RUNX2_MOUSE             Reviewed;         607 AA.
Q08775; O35183; Q08776; Q9JLN0; Q9QUQ6; Q9QY29; Q9R0U4; Q9Z2J7;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
25-OCT-2017, entry version 178.
RecName: Full=Runt-related transcription factor 2;
AltName: Full=Acute myeloid leukemia 3 protein;
AltName: Full=Core-binding factor subunit alpha-1;
Short=CBF-alpha-1;
AltName: Full=Oncogene AML-3;
AltName: Full=Osteoblast-specific transcription factor 2;
Short=OSF-2;
AltName: Full=Polyomavirus enhancer-binding protein 2 alpha A subunit;
Short=PEA2-alpha A;
Short=PEBP2-alpha A;
AltName: Full=SL3-3 enhancer factor 1 alpha A subunit;
AltName: Full=SL3/AKV core-binding factor alpha A subunit;
Name=Runx2; Synonyms=Aml3, Cbfa1, Osf2, Pebp2a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
PubMed=8341710; DOI=10.1073/pnas.90.14.6859;
Ogawa E., Maruyama M., Kagoshima H., Inuzuka M., Lu J., Satake M.,
Shigesada K., Ito Y.;
"PEBP2/PEA2 represents a family of transcription factors homologous to
the products of the Drosophila runt gene and the human AML1 gene.";
Proc. Natl. Acad. Sci. U.S.A. 90:6859-6863(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Osteoblast;
PubMed=9182762; DOI=10.1016/S0092-8674(00)80257-3;
Ducy P., Zhang R., Geoffroy V., Ridall A.L., Karsenty G.;
"Osf2/Cbfa1: a transcriptional activator of osteoblast
differentiation.";
Cell 89:747-754(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9).
STRAIN=CD2-MYC;
PubMed=9238031; DOI=10.1073/pnas.94.16.8646;
Stewart M., Terry A., Hu M., O'Hara M., Blyth K., Baxter E.,
Cameron E., Onions D.E., Neil J.C.;
"Proviral insertions induce the expression of bone-specific isoforms
of PEBP2alphaA (CBFA1): evidence for a new myc collaborating
oncogene.";
Proc. Natl. Acad. Sci. U.S.A. 94:8646-8651(1997).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 6),
AND ALTERNATIVE SPLICING.
PubMed=9651525; DOI=10.1016/S0378-1119(98)00227-3;
Xiao Z.S., Thomas R., Hinson T.K., Quarles L.D.;
"Genomic structure and isoform expression of the mouse, rat and human
Cbfa1/Osf2 transcription factor.";
Gene 214:187-197(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 (ISOFORMS 1 AND 2).
PubMed=10524201; DOI=10.1016/S0167-4781(99)00113-X;
Fujiwara M., Tagashira S., Harada H., Ogawa S., Katsumata T.,
Nakatsuka M., Komori T., Takada H.;
"Isolation and characterization of the distal promoter region of mouse
Cbfa1.";
Biochim. Biophys. Acta 1446:265-272(1999).
[6]
PROTEIN SEQUENCE OF 263-277 AND 305-319.
PubMed=8386878; DOI=10.1006/viro.1993.1262;
Ogawa E., Inuzuka M., Maruyama M., Satake M., Naito-Fujimoto M.,
Ito Y., Shigesada K.;
"Molecular cloning and characterization of PEBP2 beta, the
heterodimeric partner of a novel Drosophila runt-related DNA binding
protein PEBP2 alpha.";
Virology 194:314-331(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
STRAIN=129;
Chi X.-Z., Bae S.-C.;
"Analysis of the two PEBP2aA/cbfa1 promoter regions.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION.
PubMed=9182763; DOI=10.1016/S0092-8674(00)80258-5;
Komori T., Yagi H., Nomura S., Yamaguchi A., Sasaki K., Deguchi K.,
Shimizu Y., Bronson R.T., Gao Y.-H., Inada M., Sato M., Okamoto R.,
Kitamura Y., Yoshiki S., Kishimoto T.;
"Targeted disruption of Cbfa1 results in a complete lack of bone
formation owing to maturational arrest of osteoblasts.";
Cell 89:755-764(1997).
[9]
PHOSPHORYLATION.
PubMed=10660618; DOI=10.1074/jbc.275.6.4453;
Xiao G., Jiang D., Thomas P., Benson M.D., Guan K., Karsenty G.,
Franceschi R.T.;
"MAPK pathways activate and phosphorylate the osteoblast-specific
transcription factor, Cbfa1.";
J. Biol. Chem. 275:4453-4459(2000).
[10]
INTERACTION WITH IFI204.
PubMed=15557274; DOI=10.1074/jbc.M412604200;
Liu C.-J., Chang E., Yu J., Carlson C.S., Prazak L., Yu X.-P.,
Ding B., Lengyel P., Di Cesare P.E.;
"The interferon-inducible p204 protein acts as a transcriptional
coactivator of Cbfa1 and enhances osteoblast differentiation.";
J. Biol. Chem. 280:2788-2796(2005).
[11]
INTERACTION WITH SATB2.
PubMed=16751105; DOI=10.1016/j.cell.2006.05.012;
Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B.,
Farinas I., Karsenty G., Grosschedl R.;
"SATB2 is a multifunctional determinant of craniofacial patterning and
osteoblast differentiation.";
Cell 125:971-986(2006).
[12]
INTERACTION WITH HIVEP3.
PubMed=16728642; DOI=10.1126/science.1126313;
Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
Glimcher L.H.;
"Regulation of adult bone mass by the zinc finger adapter protein
Schnurri-3.";
Science 312:1223-1227(2006).
[13]
INTERACTION WITH DDX5.
PubMed=17960593; DOI=10.1002/jcb.21526;
Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S.,
Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.;
"p68 (Ddx5) interacts with Runx2 and regulates osteoblast
differentiation.";
J. Cell. Biochem. 103:1438-1451(2008).
[14]
FUNCTION, PHOSPHORYLATION BY HIPK3, AND INTERACTION WITH HIPK3.
PubMed=20484411; DOI=10.1210/me.2010-0029;
Sierra O.L., Towler D.A.;
"Runx2 trans-activation mediated by the MSX2-interacting nuclear
target requires homeodomain interacting protein kinase-3.";
Mol. Endocrinol. 24:1478-1497(2010).
[15]
INTERACTION WITH TMEM119.
PubMed=21239498; DOI=10.1074/jbc.M110.179127;
Hisa I., Inoue Y., Hendy G.N., Canaff L., Kitazawa R., Kitazawa S.,
Komori T., Sugimoto T., Seino S., Kaji H.;
"Parathyroid hormone-responsive Smad3-related factor, Tmem119,
promotes osteoblast differentiation and interacts with the bone
morphogenetic protein-Runx2 pathway.";
J. Biol. Chem. 286:9787-9796(2011).
[16]
INTERACTION WITH FOXO1.
PubMed=21471200; DOI=10.1074/jbc.M110.197905;
Yang S., Xu H., Yu S., Cao H., Fan J., Ge C., Fransceschi R.T.,
Dong H.H., Xiao G.;
"Foxo1 mediates insulin-like growth factor 1 (IGF1)/insulin regulation
of osteocalcin expression by antagonizing Runx2 in osteoblasts.";
J. Biol. Chem. 286:19149-19158(2011).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-353, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Transcription factor involved in osteoblastic
differentiation and skeletal morphogenesis. Essential for the
maturation of osteoblasts and both intramembranous and
endochondral ossification. CBF binds to the core site, 5'-
PYGPYGGT-3', of a number of enhancers and promoters, including
murine leukemia virus, polyomavirus enhancer, T-cell receptor
enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I)
collagen, LCK, IL-3 and GM-CSF promoters. Inhibits KAT6B-dependent
transcriptional activation (By similarity). In osteoblasts,
supports transcription activation: synergizes with SPEN/MINT to
enhance FGFR2-mediated activation of the osteocalcin FGF-
responsive element (OCFRE). {ECO:0000250,
ECO:0000269|PubMed:20484411, ECO:0000269|PubMed:9182763}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit binds DNA as a monomer and through the Runt domain. DNA-
binding is increased by heterodimerization. Interacts with XRCC6
(Ku70) and XRCC5 (Ku80). Interacts with CCNB1, KAT6A and KAT6B (By
similarity). Interacts with HIVEP3. Interacts with IFI204.
Interaction with SATB2; the interaction results in enhanced DNA
binding and transactivation by these transcription factors. Binds
to HIPK3. Interacts (isoform 3) with DDX5. Interacts with FOXO1
(via a C-terminal region); the interaction inhibits RUNX2
transcriptional activity towards BGLAP. Interacts with FOXP3 (By
similarity). Interacts with TMEM119 (PubMed:21239498).
{ECO:0000250|UniProtKB:Q13950, ECO:0000269|PubMed:15557274,
ECO:0000269|PubMed:16728642, ECO:0000269|PubMed:16751105,
ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:20484411,
ECO:0000269|PubMed:21239498, ECO:0000269|PubMed:21471200}.
-!- INTERACTION:
P17844:DDX5 (xeno); NbExp=2; IntAct=EBI-6119991, EBI-351962;
Q6AYI1:Ddx5 (xeno); NbExp=2; IntAct=EBI-903354, EBI-931635;
Q6NZM9:Hdac4; NbExp=3; IntAct=EBI-903354, EBI-646397;
Q9D030:Twist2; NbExp=2; IntAct=EBI-903354, EBI-2903190;
P25976:Ubtf; NbExp=4; IntAct=EBI-903354, EBI-7364139;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q08775-1; Sequence=Displayed;
Name=2;
IsoId=Q08775-2; Sequence=VSP_005941;
Name=3; Synonyms=PEBP2-alpha A1;
IsoId=Q08775-3; Sequence=VSP_005940, VSP_005942;
Name=4; Synonyms=PEBP2-alpha A2;
IsoId=Q08775-4; Sequence=VSP_005940, VSP_005942, VSP_005944,
VSP_005945;
Name=5; Synonyms=G1;
IsoId=Q08775-5; Sequence=VSP_005939;
Name=6; Synonyms=G2;
IsoId=Q08775-6; Sequence=VSP_005939, VSP_005943;
Name=7; Synonyms=U1;
IsoId=Q08775-7; Sequence=VSP_005939, VSP_005946, VSP_005948;
Name=8; Synonyms=Y1;
IsoId=Q08775-8; Sequence=VSP_005939, VSP_005947;
Name=9; Synonyms=Y2;
IsoId=Q08775-9; Sequence=VSP_005939, VSP_005943, VSP_005947;
-!- TISSUE SPECIFICITY: Found in thymus and testis, T-cell lines but
not in B-cell lines. Isoform 2 is exclusively found in bone,
particularly in osteoblasts; isoforms 3 and 4 are expressed in T-
cell lines; isoforms 5, 6, 7, 8 and 9 can be found in osteoblasts
and osteosarcoma cell lines.
-!- DEVELOPMENTAL STAGE: Expression occurs early during skeletal
development and is restricted to cells of the mesenchymal
condensations and of the osteoblast lineage. Expression of isoform
2 in the embryo reaches a peak at 12.5 dpc.
-!- DOMAIN: A proline/serine/threonine rich region at the C-terminus
is necessary for transcriptional activation of target genes and
contains the phosphorylation sites.
-!- PTM: Phosphorylated; probably by MAP kinases (MAPK).
Phosphorylation by HIPK3 is required for the SPEN/MINT and FGF2
transactivation during osteoblastic differentiation.
Phosphorylation at Ser-537 by CDK1 promotes endothelial cell
proliferation required for tumor angiogenesis probably by
facilitating cell cycle progression (By similarity).
{ECO:0000250}.
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EMBL; D14636; BAA03485.1; -; mRNA.
EMBL; D14637; BAA03486.1; -; mRNA.
EMBL; AF010284; AAB65409.1; -; mRNA.
EMBL; AF005936; AAB82419.1; -; mRNA.
EMBL; AF053948; AAC77440.1; -; Genomic_DNA.
EMBL; AF053951; AAC78623.1; -; mRNA.
EMBL; AF053956; AAC78626.1; -; mRNA.
EMBL; AF134836; AAF22568.1; -; Genomic_DNA.
EMBL; AF134836; AAF22569.1; -; Genomic_DNA.
EMBL; AB013129; BAA85345.1; -; Genomic_DNA.
EMBL; AB013129; BAA85346.1; -; Genomic_DNA.
EMBL; AH009404; AAF73290.1; -; Genomic_DNA.
CCDS; CCDS37624.2; -. [Q08775-5]
PIR; A48233; A48233.
RefSeq; NP_001139510.1; NM_001146038.2. [Q08775-5]
RefSeq; NP_001258556.1; NM_001271627.1. [Q08775-5]
RefSeq; NP_033950.2; NM_009820.5. [Q08775-5]
RefSeq; XP_006523607.1; XM_006523544.2. [Q08775-1]
RefSeq; XP_006523608.1; XM_006523545.2. [Q08775-2]
UniGene; Mm.391013; -.
UniGene; Mm.391017; -.
UniGene; Mm.491666; -.
ProteinModelPortal; Q08775; -.
SMR; Q08775; -.
BioGrid; 198518; 22.
CORUM; Q08775; -.
DIP; DIP-36316N; -.
ELM; Q08775; -.
IntAct; Q08775; 13.
MINT; MINT-4133380; -.
STRING; 10090.ENSMUSP00000109201; -.
ChEMBL; CHEMBL1681609; -.
iPTMnet; Q08775; -.
PhosphoSitePlus; Q08775; -.
MaxQB; Q08775; -.
PaxDb; Q08775; -.
PeptideAtlas; Q08775; -.
PRIDE; Q08775; -.
Ensembl; ENSMUST00000113571; ENSMUSP00000109201; ENSMUSG00000039153. [Q08775-5]
Ensembl; ENSMUST00000159943; ENSMUSP00000124918; ENSMUSG00000039153. [Q08775-5]
Ensembl; ENSMUST00000160673; ENSMUSP00000123743; ENSMUSG00000039153. [Q08775-2]
GeneID; 12393; -.
KEGG; mmu:12393; -.
UCSC; uc008cpy.3; mouse. [Q08775-6]
UCSC; uc008cqa.3; mouse. [Q08775-1]
CTD; 860; -.
MGI; MGI:99829; Runx2.
eggNOG; KOG3982; Eukaryota.
eggNOG; ENOG4111J4Y; LUCA.
GeneTree; ENSGT00390000016964; -.
HOVERGEN; HBG060268; -.
InParanoid; Q08775; -.
KO; K09278; -.
OMA; SDPRQFT; -.
OrthoDB; EOG091G0CXB; -.
PhylomeDB; Q08775; -.
Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
ChiTaRS; Runx2; mouse.
PRO; PR:Q08775; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000039153; -.
CleanEx; MM_RUNX2; -.
ExpressionAtlas; Q08775; baseline and differential.
Genevisible; Q08775; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0070491; F:repressing transcription factor binding; IPI:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
GO; GO:0002063; P:chondrocyte development; IMP:MGI.
GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0002076; P:osteoblast development; IGI:MGI.
GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
GO; GO:0030217; P:T cell differentiation; IDA:MGI.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.770.10; -; 1.
InterPro; IPR000040; AML1_Runt.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd.
InterPro; IPR013524; Runt_dom.
InterPro; IPR027384; Runx_central_dom.
InterPro; IPR013711; RunxI_C_dom.
InterPro; IPR011990; TPR-like_helical_dom.
PANTHER; PTHR11950; PTHR11950; 2.
Pfam; PF00853; Runt; 1.
Pfam; PF08504; RunxI; 1.
PRINTS; PR00967; ONCOGENEAML1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51062; RUNT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 607 Runt-related transcription factor 2.
/FTId=PRO_0000174660.
DOMAIN 187 315 Runt. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
REGION 1 88 Interaction with IFI204.
{ECO:0000269|PubMed:15557274}.
REGION 242 258 Required for interaction with FOXO1.
{ECO:0000269|PubMed:21471200}.
REGION 422 525 Interaction with KAT6A. {ECO:0000250}.
REGION 460 554 Interaction with KAT6B. {ECO:0000250}.
COMPBIAS 128 156 Poly-Gln.
COMPBIAS 158 175 Poly-Ala.
COMPBIAS 323 607 Pro/Ser/Thr-rich.
MOD_RES 353 353 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 537 537 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q13950}.
CROSSLNK 324 324 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13950}.
VAR_SEQ 1 98 MLHSPHKQPQNHKCGANFLQEDCKKALAFKWLISAGHYQPP
RPTESVSALTTVHAGIFKAASSIYNRGHKFYLEKKGGTMAS
NSLFSAVTPCQQSFFW -> MRIPV (in isoform 3
and isoform 4).
{ECO:0000303|PubMed:8341710,
ECO:0000303|PubMed:9238031}.
/FTId=VSP_005940.
VAR_SEQ 1 79 Missing (in isoform 5, isoform 6, isoform
7, isoform 8 and isoform 9).
{ECO:0000303|PubMed:9238031}.
/FTId=VSP_005939.
VAR_SEQ 47 57 Missing (in isoform 2).
{ECO:0000303|PubMed:9182762,
ECO:0000303|PubMed:9238031}.
/FTId=VSP_005941.
VAR_SEQ 156 156 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:8341710,
ECO:0000303|PubMed:9238031}.
/FTId=VSP_005942.
VAR_SEQ 316 373 Missing (in isoform 6 and isoform 9).
{ECO:0000303|PubMed:9238031}.
/FTId=VSP_005943.
VAR_SEQ 399 400 PS -> LS (in isoform 4).
{ECO:0000303|PubMed:8341710,
ECO:0000303|PubMed:9238031}.
/FTId=VSP_005944.
VAR_SEQ 401 607 Missing (in isoform 4).
{ECO:0000303|PubMed:8341710,
ECO:0000303|PubMed:9238031}.
/FTId=VSP_005945.
VAR_SEQ 427 439 DDDTATSDFCLWP -> GFCGTTTTTTTKL (in
isoform 7). {ECO:0000303|PubMed:9238031}.
/FTId=VSP_005946.
VAR_SEQ 428 607 DDTATSDFCLWPSSLSKKSQAGASELGPFSDPRQFPSISSL
TESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLP
PPYPGSSQSQSGPFQTSSTPYLYYGTSSASYQFPMVPGGDR
SPSRMVPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPT
VLNSSGRMDESVWRPY -> SEPSTLDSQSSTTLFLSSEEP
GPSTAALPSPSSSCEPQPFSPSPMLPPLLQPLSTASTVPAP
CVPRRTGLYTIVTSSPEAAPHLVDWMPSCPTATSPGVRGKD
HERPQTMMAPAPALASERGHSQHAGPARDDHAEHPGTSPKP
CAPPAAAATLEASVGDILVELRTMNGHLDIIAKALTKLASS
LVPQSQPVPEAPDAN (in isoform 8 and isoform
9). {ECO:0000303|PubMed:9238031}.
/FTId=VSP_005947.
VAR_SEQ 440 607 Missing (in isoform 7).
{ECO:0000303|PubMed:9238031}.
/FTId=VSP_005948.
CONFLICT 266 266 A -> S (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 280 280 G -> S (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 373 373 D -> N (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 375 375 R -> T (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 396 396 M -> L (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 459 459 P -> L (in Ref. 4; AAC78626).
{ECO:0000305}.
CONFLICT 472 472 R -> P (in Ref. 4; AAC78626).
{ECO:0000305}.
SEQUENCE 607 AA; 66205 MW; E87A4497ED19EE0E CRC64;
MLHSPHKQPQ NHKCGANFLQ EDCKKALAFK WLISAGHYQP PRPTESVSAL TTVHAGIFKA
ASSIYNRGHK FYLEKKGGTM ASNSLFSAVT PCQQSFFWDP STSRRFSPPS SSLQPGKMSD
VSPVVAAQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQEAAA AAAAAAAAAA AAAAAVPRLR
PPHDNRTMVE IIADHPAELV RTDSPNFLCS VLPSHWRCNK TLPVAFKVVA LGEVPDGTVV
TVMAGNDENY SAELRNASAV MKNQVARFND LRFVGRSGRG KSFTLTITVF TNPPQVATYH
RAIKVTVDGP REPRRHRQKL DDSKPSLFSD RLSDLGRIPH PSMRVGVPPQ NPRPSLNSAP
SPFNPQGQSQ ITDPRQAQSS PPWSYDQSYP SYLSQMTSPS IHSTTPLSST RGTGLPAITD
VPRRISDDDT ATSDFCLWPS SLSKKSQAGA SELGPFSDPR QFPSISSLTE SRFSNPRMHY
PATFTYTPPV TSGMSLGMSA TTHYHTYLPP PYPGSSQSQS GPFQTSSTPY LYYGTSSASY
QFPMVPGGDR SPSRMVPPCT TTSNGSTLLN PNLPNQNDGV DADGSHSSSP TVLNSSGRMD
ESVWRPY


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