ID   AXN1_HUMAN     STANDARD;      PRT;   862 AA.
AC   O15169; Q96S28; Q8WVW6;
DT   16-OCT-2001 (Rel. 40, Created)
DT   15-JUN-2002 (Rel. 41, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Axin 1 (Axis inhibition protein 1) (hAxin).
GN   AXIN1 OR AXIN.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=97373830; PubMed=9230313;
RA   Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III,
RA   Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.;
RT   "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling
RT   pathway that regulates embryonic axis formation.";
RL   Cell 90:181-192(1997).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=21096910; PubMed=11157797;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA   Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA   Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2
RT   Mb of the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [3]
RP   SEQUENCE OF 471-862 FROM N.A.
RC   TISSUE=Kidney;
RA   Strausberg R.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DISEASE.
RX   PubMed=10700176;
RA   Satoh S., Daigo Y., Furukawa Y., Kato T., Miwa N., Nishiwaki T.,
RA   Kawasoe T., Ishiguro H., Fujita M., Tokino T., Sasaki Y., Imaoka S.,
RA   Murata M., Shimano T., Yamaoka Y., Nakamura Y.;
RT   "AXIN1 mutations in hepatocellular carcinomas, and growth suppression
RT   in cancer cells by virus-mediated transfer of AXIN1.";
RL   Nat. Genet. 24:245-250(2000).
CC   -!- FUNCTION: INHIBITOR OF THE WNT SIGNALING PATHWAY. DOWN-REGULATES
CC       BETA-CATENIN. PROBABLY FACILITATE THE PHOSPHORYLATION OF BETA-
CC       CATENIN AND APC BY GSK-3B. LIKELY TO FUNCTION AS A TUMOR
CC       SUPPRESSOR. WILD-TYPE AXIN 1 CAN INDUCE APOPTOSIS IN
CC       HEPATOCELLULAR AND COLORECTAL CANCER CELLS.
CC   -!- SUBUNIT: INTERACTS WITH GLYCOGEN SYNTHASE KINASE-3 BETA (GSK-3B)
CC       AND BETA-CATENIN. THE INTERACTION BETWEEN AXIN AND BETA-CATENIN
CC       OCCURS VIA THE ARMADILLO REPEATS CONTAINED IN BETA-CATENIN.
CC       TERNARY COMPLEX. MAY ALSO BINDS TO PLAKOGLOBIN (GAMMA-CATENIN),
CC       APC, DVL AND PP2A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED.
CC   -!- PTM: PROBABLY PHOSPHORYLATED BY GSK-3B AND DEPHOSPHORYLATED BY
CC       PP2A.
CC   -!- DISEASE: Defects in AXIN1 are a cause of hepatocellular carcinoma.
CC   -!- SIMILARITY: CONTAINS 1 RGS DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 DIX DOMAIN.
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; AF009674; AAC51624.1; ALT_INIT.
DR   EMBL; AE006463; AAK61224.1; -.
DR   EMBL; BC017447; AAH17447.1; -.
DR   HSSP; P49799; 1AGR.
DR   MIM; 603816; -.
DR   MIM; 114550; -.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR000342; Regl_Gprotein.
DR   Pfam; PF00615; RGS; 2.
DR   Pfam; PF00778; DIX; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   ProDom; PD001580; Reg_of_prG; 1.
DR   ProDom; PD003639; DIX; 1.
DR   SMART; SM00021; DAX; 1.
DR   SMART; SM00315; RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
KW   Developmental protein; Phosphorylation; Anti-oncogene.
FT   DOMAIN       88    211       RGS.
FT   DOMAIN      348    433       GSK-3B BINDING SITE (BY SIMILARITY).
FT   DOMAIN      434    502       BETA-CATENIN BINDING SITE (BY
FT                                SIMILARITY).
FT   DOMAIN      780    862       DIX.
FT   CONFLICT    360    360       V -> A (IN REF. 1).
FT   CONFLICT    451    455       CVDMG -> LCWTWA (IN REF. 1).
FT   CONFLICT    482    482       P -> T (IN REF. 1).
SQ   SEQUENCE   862 AA;  95634 MW;  10779173F5092F3F CRC64;
     MNIQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGV GIKGETSTAT
     PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA
     CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL DNNGIVSRQT KPATKSFIKG CIMKQLIDPA
     MFDQAQTEIQ ATMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT
     LNEDEEWKCD QDMDEDDGRD AAPPGRLPQK LLLETAAPRV SSSRRYSEGR EFRYGSWREP
     VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESV
     QVNGRVPLPH IPRTYRVPKE VRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE
     EGEDGDPSSG PPGPCHKLPP APAWHHFPPR CVDMGCAGLR DAHEENPESI LDEHVQRVLR
     TPGRQSPGPG HRSPDSGHVA KMPVALGGAA SGHGKHVPKS GAKLDAAGLH HHRHVHHHVH
     HSTARPKEQV EAEATRRAQS SFAWGLEPHS HGARSRGYSE SVGAAPNASD GLAHSGKVGV
     ACKRNAKKAE SGKSASTEVP GASEDAEKNQ KIMQWIIEGE KEISRHRRTG HGSSGTRKPQ
     PHENSRPLSL EHPWAGPQLR TSVQPSHLFI QDPTMPPHPA PNPLTQLEEA RRRLEEEEKR
     ASRAPSKQRY VQEVMRRGRA CVRPACAPVL HVVPAVSDME LSETETRSQR KVGGGSAQPC
     DSIVVAYYFC GEPIPYRTLV RGRAVTLGQF KELLTKKGSY RYYFKKVSDE FDCGVVFEEV
     REDEAVLPVF EEKIIGKVEK VD
//