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DIX1A_DANRE
ID   DIX1A_DANRE             Reviewed;         443 AA.
AC   Q804T6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Dixin-A;
DE   AltName: Full=Coiled-coil protein DIX1-A;
DE            Short=Coiled-coil-DIX1-A;
DE   AltName: Full=DIX domain-containing protein 1-A;
GN   Name=dixdc1a; Synonyms=ccd1, dixdc1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, OLIGOMERIZATION,
RP   AND INTERACTION WITH DISHEVELLED AND AXIN1.
RX   PubMed=12526749; DOI=10.1016/s0960-9822(02)01398-2;
RA   Shiomi K., Uchida H., Keino-Masu K., Masu M.;
RT   "Ccd1, a novel protein with a DIX domain, is a positive regulator in the
RT   Wnt signaling during zebrafish neural patterning.";
RL   Curr. Biol. 13:73-77(2003).
CC   -!- FUNCTION: Functions as a positive effector of the Wnt signaling pathway
CC       regulating antero-posterior neural patterning.
CC       {ECO:0000269|PubMed:12526749}.
CC   -!- SUBUNIT: Homomers. Interacts with dishevelled and axin1.
CC       {ECO:0000269|PubMed:12526749}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo including the
CC       shield. Strongly expressed in notochord and head regions from the bud
CC       to somite stages. Expressed in early born neurons in the telencephalic
CC       nucleus, the nuclei of the tract of the post-optic commissure and of
CC       the medial longitudinal fasciculus, and in segmental clusters of
CC       neurons in the hindbrain. {ECO:0000269|PubMed:12526749}.
CC   -!- DOMAIN: The DIX domain mediates self-interaction and interaction with
CC       dishevelled and axin1.
CC   -!- SIMILARITY: Belongs to the DIXDC1 family. {ECO:0000305}.
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DR   EMBL; AF502143; AAO31595.1; -; mRNA.
DR   RefSeq; NP_878304.1; NM_182884.1.
DR   PDB; 5Y3C; X-ray; 1.96 A; A=356-438.
DR   PDBsum; 5Y3C; -.
DR   AlphaFoldDB; Q804T6; -.
DR   SMR; Q804T6; -.
DR   STRING; 7955.ENSDARP00000073184; -.
DR   PaxDb; Q804T6; -.
DR   PRIDE; Q804T6; -.
DR   GeneID; 360137; -.
DR   KEGG; dre:360137; -.
DR   CTD; 360137; -.
DR   ZFIN; ZDB-GENE-030721-2; dixdc1a.
DR   eggNOG; ENOG502RD5G; Eukaryota.
DR   InParanoid; Q804T6; -.
DR   OrthoDB; 949210at2759; -.
DR   PhylomeDB; Q804T6; -.
DR   SignaLink; Q804T6; -.
DR   PRO; PR:Q804T6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:ZFIN.
DR   GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:ZFIN.
DR   GO; GO:0030900; P:forebrain development; IMP:ZFIN.
DR   Gene3D; 2.40.240.130; -; 1.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR038207; DIX_dom_sf.
DR   InterPro; IPR029800; Dixin.
DR   InterPro; IPR015506; Dsh/Dvl-rel.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10878; PTHR10878; 1.
DR   PANTHER; PTHR10878:SF22; PTHR10878:SF22; 1.
DR   Pfam; PF00778; DIX; 1.
DR   SMART; SM00021; DAX; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50841; DIX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Coiled coil; Cytoplasm; Developmental protein;
KW   Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..443
FT                   /note="Dixin-A"
FT                   /id="PRO_0000287226"
FT   DOMAIN          357..439
FT                   /note="DIX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          71..240
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          360..368
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   STRAND          373..379
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   TURN            381..383
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   HELIX           386..393
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   STRAND          400..407
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   TURN            408..410
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   STRAND          411..416
FT                   /evidence="ECO:0007829|PDB:5Y3C"
FT   STRAND          430..436
FT                   /evidence="ECO:0007829|PDB:5Y3C"
SQ   SEQUENCE   443 AA;  50439 MW;  F828E90318BD096E CRC64;
     MGAKQMKCLS SSSPSHTPKE EYIIAKSEDS GELVGNHTEQ PQSLEDVVKS SATDPYPGPE
     HVVKEESSTW EEQLCAQQEQ LEKEMQETRK MVSRLQALLL HGSLPEDEQT STLSFGDTAS
     SEQQLILTRS RLDQSMEESL DLKRELLRYK QEARNLQAVK DALQQRMSVQ EDSVLQLKQE
     LLRSSMTREE LEGQNVELER KLSERNRLLS EYKKELGQKD RLLQQQQTKL DDALRRISES
     YHRLSGCENN GYSHMMDTSS AVFQHRMGDE LQLVRDALRS LRDSFSGHDP QHHTLDTLEQ
     GVASLVDRLH TSDTKKRPER KGSTRSPGRK ANHTDRESWP STSKIAHSHS SPVLSAAAST
     KVLYYTDRSL TPFLVNIPKR LGDVTLQDFK AAVDRHGSFR YHFKSLDPEF GTVKEEVFQD
     DAVIPGWEGK IVAWVEEDHG EGR
 
 
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