[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH PARD6B. TISSUE=Kidney; DOI=10.1038/35019573; PubMed=10934474 [NCBI, ExPASy, EBI, Israel, Japan] Joberty G., Petersen C., Gao L., Macara I.G.; "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."; Nat. Cell Biol. 2:531-539(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 7; 8 AND 9). DOI=10.1038/sj.cr.7290090; PubMed=11642408 [NCBI, ExPASy, EBI, Israel, Japan] Fang C.M., Xu Y.H.; "Down-regulated expression of atypical PKC-binding domain deleted asip isoforms in human hepatocellular carcinomas."; Cell Res. 11:223-229(2001).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). DOI=10.1016/S0006-291X(02)02698-0; PubMed=12459187 [NCBI, ExPASy, EBI, Israel, Japan] Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.; "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions."; Biochem. Biophys. Res. Commun. 299:641-646(2002).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH PARD6B AND PRKCZ, AND TISSUE SPECIFICITY. DOI=10.1016/S0378-1119(02)00681-9; PubMed=12234671 [NCBI, ExPASy, EBI, Israel, Japan] Gao L., Macara I.G., Joberty G.; "Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties."; Gene 294:99-99(2002).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10). TISSUE=Hepatoma, and Ovarian carcinoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 313-992. TISSUE=Testis; DOI=10.1073/pnas.021386498; PubMed=11149944 [NCBI, ExPASy, EBI, Israel, Japan] Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.; "Serological detection of cutaneous T-cell lymphoma-associated antigens."; Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1356. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	INTERACTION WITH PARD6A. PubMed=10954424 [NCBI, ExPASy, EBI, Israel, Japan] Johansson A.-S., Driessens M., Aspenstroem P.; "The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."; J. Cell Sci. 113:3267-3275(2000).
[9]	SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI. TISSUE=Kidney; DOI=10.1083/jcb.152.6.1183; PubMed=11257119 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S.; "Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures."; J. Cell Biol. 152:1183-1196(2001).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1127, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.; "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."; Mol. Cell. Proteomics 4:1240-1250(2005).
[12]	IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH ARHGAP17; AMOT; MPP5 AND INADL. DOI=10.1016/j.cell.2006.02.045; PubMed=16678097 [NCBI, ExPASy, EBI, Israel, Japan] Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.; "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."; Cell 125:535-548(2006).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1127, MASS SPECTROMETRY, INTERACTION WITH LIMK2, AND MUTAGENESIS OF TYR-1127. DOI=10.1038/sj.emboj.7601384; PubMed=17053785 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.; "Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."; EMBO J. 25:5058-5070(2006).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-144; SER-383; SER-695; SER-715; SER-717 AND SER-728, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).

Comments

FUNCTION: Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins.
SUBUNIT: Interacts with PARD6A and PARD6B. Isoform 2, but not at least isoform 3 interacts with PRKCZ. Interacts with PRCKI (By similarity). Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Interacts with F11R/JAM1 (By similarity). Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with LIMK2.
INTERACTION:
Q9NPB6:PARD6A; NbExp=2; IntAct=EBI-81968, EBI-81876;
Q9BYG5:PARD6B; NbExp=1; IntAct=EBI-81968, EBI-295391;
Q9JK83:Pard6b (xeno); NbExp=2; IntAct=EBI-81968, EBI-81861;
Q8ND90:PNMA1; NbExp=1; IntAct=EBI-81968, EBI-302345;
P41743:PRKCI; NbExp=1; IntAct=EBI-81968, EBI-286199;
P31946:YWHAB; NbExp=1; IntAct=EBI-81968, EBI-359815;
P61981:YWHAG; NbExp=1; IntAct=EBI-81968, EBI-359832;
Q04917:YWHAH; NbExp=1; IntAct=EBI-81968, EBI-306940;
P63104:YWHAZ; NbExp=1; IntAct=EBI-81968, EBI-347088;
SUBCELLULAR LOCATION: Intracytoplasmic membrane. Cell junction, tight junction. Cell membrane. Note=Partially localized along the cell-cell contact region. Colocalizes with PARD6A and PRKCI at epithelial tight junctions.

ALTERNATIVE PRODUCTS: 10 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	A
Isoform ID	Q8TEW0-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	B, La
Isoform ID	Q8TEW0-2
Features which should be applied to build the isoform sequence: VSP_007464.

Name	3
Synonyms	C
Isoform ID	Q8TEW0-3
Features which should be applied to build the isoform sequence: VSP_007462, VSP_007463, VSP_007464, VSP_007465.

Name	4
Synonyms	D
Isoform ID	Q8TEW0-4
Features which should be applied to build the isoform sequence: VSP_007469.

Name	5
Synonyms	E
Isoform ID	Q8TEW0-5
Features which should be applied to build the isoform sequence: VSP_007462, VSP_007463, VSP_007464, VSP_007466, VSP_007468, VSP_007469.

Name	6
Synonyms	F
Isoform ID	Q8TEW0-6
Features which should be applied to build the isoform sequence: VSP_007463, VSP_007464, VSP_007465.

Name	7
Synonyms	Lb
Isoform ID	Q8TEW0-7
Features which should be applied to build the isoform sequence: VSP_007463, VSP_007464, VSP_007465, VSP_007469.

Name	8
Synonyms	Sa
Isoform ID	Q8TEW0-8
Features which should be applied to build the isoform sequence: VSP_007464, VSP_007470, VSP_007471.

Name	9
Synonyms	Sb
Isoform ID	Q8TEW0-9
Features which should be applied to build the isoform sequence: VSP_007463, VSP_007464, VSP_007465, VSP_007470, VSP_007471.

Name	10
Isoform ID	Q8TEW0-10
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_007464, VSP_007465, VSP_007467, VSP_007470, VSP_007471.

TISSUE SPECIFICITY: Widely expressed.
PTM: Phosphorylated by PRKCZ. EGF-induced Tyr-1127 phosphorylation mediates dissociation from LIMK2.
MISCELLANEOUS: Antibodies against PARD3 are present in sera from patients with cutaneous T-cell lymphomas.
SIMILARITY: Belongs to the PAR3 family.
SIMILARITY: Contains 3 PDZ (DHR) domains.
SEQUENCE CAUTION:
- Sequence=AAG33676.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF252293; AAF71530.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF196185; AAK27891.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF196186; AAK27892.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF332592; AAK69192.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF332593; AAK69193.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB073671; BAC54037.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467002; AAL76042.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467003; AAL76043.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467004; AAL76044.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467005; AAL76045.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467006; AAL76046.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000761; BAA91366.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027735; BAB55330.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177228; AAG33676.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011711; AAH11711.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_062565.2; -.

UniGene

Hs.131489

3D structure databases

SMR

Q8TEW0; 583-683.

ModBase

Q8TEW0.

Protein-protein interaction databases

IntAct

Q8TEW0; -.

PTM databases

PhosphoSite

Q8TEW0; -.

Organism-specific databases

H-InvDB

HIX0008758; -.
HIX0035395; -.

HGNC:16051; PARD3.

PARD3; Homo sapiens.

606745; gene. [NCBI / EBI]

PharmGKB

PA32936; -.

GeneCards

Q8TEW0.

Gene expression databases

ArrayExpress

Q8TEW0; -.

GermOnline

ENSG00000148498; Homo sapiens.

Ontologies

GO:0005923;	Cellular component: tight junction (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0007205;	Biological process: activation of protein kinase C activity (traceable author statement from UniProtKB).
GO:0008356;	Biological process: asymmetric cell division (traceable author statement from ProtInc).
GO:0007409;	Biological process: axonogenesis (traceable author statement from UniProtKB).
GO:0007163;	Biological process: establishment and/or maintenance of cell polarity (traceable author statement from UniProtKB).
GO:0006461;	Biological process: protein complex assembly (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001478; PDZ.
Graphical view of domain structure.

Pfam

PF00595; PDZ; 2.
Pfam graphical view of domain structure.

SMART

SM00228; PDZ; 3.
SMART graphical view of domain structure.

PROSITE

PS50106; PDZ; 3.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q8TEW0.

Genome annotation databases

Ensembl

ENSG00000148498; Homo sapiens. [Contig view]

GeneID

56288; -.

KEGG

hsa:56288; -.

Phylogenomic databases

HOVERGEN

Q8TEW0; -.

Other

Q8TEW0; -.

PARD3; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cell cycle; Cell division; Cell junction; Coiled coil; Membrane; Phosphoprotein; Polymorphism; Repeat; Tight junction.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1356`	`1356`	`Partitioning-defective 3 homolog.`	`PRO_0000185069`
`DOMAIN`	`271 359`	`89`	`PDZ 1.`
`DOMAIN`	`461 546`	`86`	`PDZ 2.`
`DOMAIN`	`590 677`	`88`	`PDZ 3.`
`REGION`	`712 936`	`225`	`Interacts with PRKCZ (By similarity).`
`COILED`	`1049 1077`	`29`	`Potential.`
`COILED`	`1151 1174`	`24`	`Potential.`
`COILED`	`1201 1224`	`24`	`Potential.`
`COILED`	`1280 1301`	`22`	`Potential.`
`COMPBIAS`	`984 1042`	`59`	`Lys-rich.`
`MOD_RES`	`143 143`		`Phosphoserine.`
`MOD_RES`	`144 144`		`Phosphoserine.`
`MOD_RES`	`383 383`		`Phosphoserine.`
`MOD_RES`	`695 695`		`Phosphoserine.`
`MOD_RES`	`715 715`		`Phosphoserine.`
`MOD_RES`	`717 717`		`Phosphoserine.`
`MOD_RES`	`728 728`		`Phosphoserine.`
`MOD_RES`	`827 827`		`Phosphoserine (By similarity).`
`MOD_RES`	`852 852`		`Phosphoserine.`
`MOD_RES`	`1080 1080`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`1127 1127`		`Phosphotyrosine.`
`VAR_SEQ`	`195 238`		`Missing (in isoform 3 and isoform 5).`	`VSP_007462`
`VAR_SEQ`	`557 569`		`Missing (in isoform 3, isoform 5, isoform 6, isoform 7 and isoform 9).`	`VSP_007463`
`VAR_SEQ`	`740 742`		`Missing (in isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10).`	`VSP_007464`
`VAR_SEQ`	`827 856`		`Missing (in isoform 3, isoform 6, isoform 7, isoform 9 and isoform 10).`	`VSP_007465`
`VAR_SEQ`	`857 858`		`IA -> T (in isoform 10).`	`VSP_007467`
`VAR_SEQ`	`857 857`		`I -> S (in isoform 5).`	`VSP_007466`
`VAR_SEQ`	`858 872`		`Missing (in isoform 5).`	`VSP_007468`
`VAR_SEQ`	`1025 1061`		`Missing (in isoform 4, isoform 5 and isoform 7).`	`VSP_007469`
`VAR_SEQ`	`1025 1034`		`RFGKHRKDDK -> SLAKLKPEKR (in isoform 8, isoform 9 and isoform 10).`	`VSP_007470`
`VAR_SEQ`	`1035 1356`		`Missing (in isoform 8, isoform 9 and isoform 10).`	`VSP_007471`
`VARIANT`	`107 107`	`1`	`E -> D (in dbSNP:rs1436731 [NCBI]).`	`VAR_015663`
`MUTAGEN`	`1127 1127`		`Y->F: Delayed epithelial tight junction assembly.`
`CONFLICT`	`190 190`		`T -> A (in Ref. 5; BAB55330).`
`CONFLICT`	`233 233`		`L -> Q (in Ref. 5; BAB55330).`
`CONFLICT`	`594 594`		`N -> S (in Ref. 5; BAB55330).`
`CONFLICT`	`996 1000`		`GKEKK -> VELHE (in Ref. 5; BAA91366).`

Sequence information

Length: 1356 AA [This is the length of the unprocessed precursor]

Molecular weight: 151423 Da [This is the MW of the unprocessed precursor]

CRC64: A4FD3F4F9AD8B92A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVTVCFGRT RVVVPCGDGH MKVFSLIQQA VTRYRKAIAK DPNYWIQVHR LEHGDGGILD 

        70         80         90        100        110        120 
LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS PEIFGSELGT NNVSAFQPYQ 

       130        140        150        160        170        180 
ATSEIEVTPS VLRANMPLHV RRSSDPALIG LSTSVSDSNF SSEEPSRKNP TRWSTTAGFL 

       190        200        210        220        230        240 
KQNTAGSPKT CDRKKDENYR SLPRDTSNWS NQFQRDNARS SLSASHPMVG KWLEKQEQDE 

       250        260        270        280        290        300 
DGTEEDNSRV EPVGHADTGL EHIPNFSLDD MVKLVEVPND GGPLGIHVVP FSARGGRTLG 

       310        320        330        340        350        360 
LLVKRLEKGG KAEHENLFRE NDCIVRINDG DLRNRRFEQA QHMFRQAMRT PIIWFHVVPA 

       370        380        390        400        410        420 
ANKEQYEQLS QSEKNNYYSS RFSPDSQYID NRSVNSAGLH TVQRAPRLNH PPEQIDSHSR 

       430        440        450        460        470        480 
LPHSAHPSGK PPSAPASAPQ NVFSTTVSSG YNTKKIGKRL NIQLKKGTEG LGFSITSRDV 

       490        500        510        520        530        540 
TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLV GKSQEEVVSL LRSTKMEGTV 

       550        560        570        580        590        600 
SLLVFRQEDA FHPRELNAEP SQMQIPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG 

       610        620        630        640        650        660 
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKTNQDAME 

       670        680        690        700        710        720 
TLRRSMSTEG NKRGMIQLIV ARRISKCNEL KSPGSPPGPE LPIETALDDR ERRISHSLYS 

       730        740        750        760        770        780 
GIEGLDESPS RNAALSRIMG ESGKYQLSPT VNMPQDDTVI IEDDRLPVLP PHLSDQSSSS 

       790        800        810        820        830        840 
SHDDVGFVTA DAGTWAKAAI SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSDAS 

       850        860        870        880        890        900 
QLDFVKTRKS KSMDLGIADE TKLNTVDDQK AGSPSRDVGP SLGLKKSSSL ESLQTAVAEV 

       910        920        930        940        950        960 
TLNGDIPFHR PRPRIIRGRG CNESFRAAID KSYDKPAVDD DDEGMETLEE DTEESSRSGR 

       970        980        990       1000       1010       1020 
ESVSTASDQP SHSLERQMNG NQEKGDKTDR KKDKTGKEKK KDRDKEKDKM KAKKGMLKGL 

      1030       1040       1050       1060       1070       1080 
GDMFRFGKHR KDDKIEKTGK IKIQESFTSE EERIRMKQEQ ERIQAKTREF RERQARERDY 

      1090       1100       1110       1120       1130       1140 
AEIQDFHRTF GCDDELMYGG VSSYEGSMAL NARPQSPREG HMMDALYAQV KKPRNSKPSP 

      1150       1160       1170       1180       1190       1200 
VDSNRSTPSN HDRIQRLRQE FQQAKQDEDV EDRRRTYSFE QPWPNARPAT QSGRHSVSVE 

      1210       1220       1230       1240       1250       1260 
VQMQRQRQEE RESSQQAQRQ YSSLPRQSRK NASSVSQDSW EQNYSPGEGF QSAKENPRYS 

      1270       1280       1290       1300       1310       1320 
SYQGSRNGYL GGHGFNARVM LETQELLRQE QRRKEQQMKK QPPSEGPSNY DSYKKVQDPS 

      1330       1340       1350 
YAPPKGPFRQ DVPPSPSQVA RLNRLQTPEK GRPFYS

Q8TEW0 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools