LOCUS NP_001032358 345 aa linear PRI 12-OCT-2008
DEFINITION par-6 partitioning defective 6 homolog alpha isoform 2 [Homo
sapiens].
ACCESSION NP_001032358
VERSION NP_001032358.1 GI:82659097
DBSOURCE REFSEQ: accession NM_001037281.1
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 345)
AUTHORS Hartleben,B., Schweizer,H., Lubben,P., Bartram,M.P., Moller,C.C.,
Herr,R., Wei,C., Neumann-Haefelin,E., Schermer,B., Zentgraf,H.,
Kerjaschki,D., Reiser,J., Walz,G., Benzing,T. and Huber,T.B.
TITLE Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C
(aPKC) complex to regulate podocyte cell polarity
JOURNAL J. Biol. Chem. 283 (34), 23033-23038 (2008)
PUBMED 18562307
REMARK GeneRIF: Neph1-Nephrin proteins bind the Par3-Par6-atypical protein
kinase C (aPKC) complex to regulate podocyte cell polarity
REFERENCE 2 (residues 1 to 345)
AUTHORS Rudolph,J.L., Shi,G.X., Erdogan,E., Fields,A.P. and Andres,D.A.
TITLE Rit mutants confirm role of MEK/ERK signaling in neuronal
differentiation and reveal novel Par6 interaction
JOURNAL Biochim. Biophys. Acta 1773 (12), 1793-1800 (2007)
PUBMED 17976838
REMARK GeneRIF: In vivo binding studies identified a novel mechanism of
Par6 interaction, suggesting that the cell polarity machinery may
serve to spatially restrict Rit signaling.
REFERENCE 3 (residues 1 to 345)
AUTHORS Simmers,M.B., Pryor,A.W. and Blackman,B.R.
TITLE Arterial shear stress regulates endothelial cell-directed
migration, polarity, and morphology in confluent monolayers
JOURNAL Am. J. Physiol. Heart Circ. Physiol. 293 (3), H1937-H1946 (2007)
PUBMED 17586613
REMARK GeneRIF: Shear stress-induced directed migratory polarity is
modulated by exogenous growth factors and dependent on Par6
activity and shear stress direction in endothelial cells
REFERENCE 4 (residues 1 to 345)
AUTHORS Cline,E.G. and Nelson,W.J.
TITLE Characterization of mammalian Par 6 as a dual-location protein
JOURNAL Mol. Cell. Biol. 27 (12), 4431-4443 (2007)
PUBMED 17420281
REMARK GeneRIF: Par6 was characterized as a dual-location protein.
REFERENCE 5 (residues 1 to 345)
AUTHORS Weyrich,P., Neuscheler,D., Melzer,M., Hennige,A.M., Haring,H.U. and
Lammers,R.
TITLE The Par6alpha/aPKC complex regulates Akt1 activity by
phosphorylating Thr34 in the PH-domain
JOURNAL Mol. Cell. Endocrinol. 268 (1-2), 30-36 (2007)
PUBMED 17335965
REMARK GeneRIF: Par6alpha-mediated inhibition of insulin-dependent
glycogen synthesis in C2C12 cells depends on the direct interaction
of Par6alpha with aPKC and on aPKC-mediated T34 phosphorylation of
Akt1.
REFERENCE 6 (residues 1 to 345)
AUTHORS Suzuki,A., Yamanaka,T., Hirose,T., Manabe,N., Mizuno,K.,
Shimizu,M., Akimoto,K., Izumi,Y., Ohnishi,T. and Ohno,S.
TITLE Atypical protein kinase C is involved in the evolutionarily
conserved par protein complex and plays a critical role in
establishing epithelia-specific junctional structures
JOURNAL J. Cell Biol. 152 (6), 1183-1196 (2001)
PUBMED 11257119
REFERENCE 7 (residues 1 to 345)
AUTHORS Johansson,A., Driessens,M. and Aspenstrom,P.
TITLE The mammalian homologue of the Caenorhabditis elegans polarity
protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
Rac1
JOURNAL J. Cell. Sci. 113 (PT 18), 3267-3275 (2000)
PUBMED 10954424
REFERENCE 8 (residues 1 to 345)
AUTHORS Joberty,G., Petersen,C., Gao,L. and Macara,I.G.
TITLE The cell-polarity protein Par6 links Par3 and atypical protein
kinase C to Cdc42
JOURNAL Nat. Cell Biol. 2 (8), 531-539 (2000)
PUBMED 10934474
REFERENCE 9 (residues 1 to 345)
AUTHORS Qiu,R.G., Abo,A. and Steven Martin,G.
TITLE A human homolog of the C. elegans polarity determinant Par-6 links
Rac and Cdc42 to PKCzeta signaling and cell transformation
JOURNAL Curr. Biol. 10 (12), 697-707 (2000)
PUBMED 10873802
REFERENCE 10 (residues 1 to 345)
AUTHORS Rousset,R., Fabre,S., Desbois,C., Bantignies,F. and Jalinot,P.
TITLE The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
with the PDZ domain of cellular proteins
JOURNAL Oncogene 16 (5), 643-654 (1998)
PUBMED 9482110
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AF252292.1 and BC015626.2.
Summary: This gene is a member of the PAR6 family and encodes a
protein with a PSD95/Discs-large/ZO1 (PDZ) domain and a
semi-Cdc42/Rac interactive binding (CRIB) domain. This cell
membrane protein is involved in asymmetrical cell division and cell
polarization processes as a member of a multi-protein complex. The
protein also has a role in the epithelial-to-mesenchymal transition
(EMT) that characterizes the invasive phenotype associated with
metastatic carcinomas. Alternate transcriptional splice variants,
encoding different isoforms, have been characterized. [provided by
RefSeq].
Transcript Variant: This variant (2) uses an alternate in-frame
splice site in the coding region, compared to variant 1, resulting
in a protein (isoform 2) that is one amino acid shorter than
isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..345
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="16"
/map="16q22.1"
Protein 1..345
/product="par-6 partitioning defective 6 homolog alpha
isoform 2"
/note="Tax-interacting protein 40; partitioning
defective-6 homolog alpha; partitioning-defective protein
6"
/calculated_mol_wt=37186
CDS 1..345
/gene="PARD6A"
/gene_synonym="PAR6"
/gene_synonym="PAR6C"
/gene_synonym="TAX40"
/gene_synonym="PAR-6A"
/gene_synonym="TIP-40"
/gene_synonym="PAR6alpha"
/coded_by="NM_001037281.1:92..1129"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="GeneID:50855"
/db_xref="HGNC:15943"
/db_xref="HPRD:06316"
/db_xref="MIM:607484"
ORIGIN
1 marpqrtpar spdsivevks kfdaefrrfa lprasvsgfq efsrllravh qipgldvllg
61 ytdahgdllp ltnddslhra lasgppplrl lvqkreadss glafasnslq rrkkglllrp
121 vaplrtrppl lislpqdfrq vssvidvdll pethrrvrlh khgsdrplgf yirdgmsvrv
181 apqglervpg ifisrlvrgg laestgllav sdeilevngi evagktldqv tdmmvanshn
241 livtvkpanq rnnvvrgasg rltgppsagp gpaepdsddd ssdlvienrq ppssnglsqg
301 ppcwdlhpgc rhpgtrsslp slddqeqass gwgsrirgdg sgfsl
//