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MESD_DANRE
ID   MESD_DANRE              Reviewed;         206 AA.
AC   A1L243;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=LRP chaperone MESD {ECO:0000305};
DE   AltName: Full=LDLR chaperone MESD;
DE   AltName: Full=Mesoderm development candidate 2;
DE   AltName: Full=Mesoderm development protein;
DE   Flags: Precursor;
GN   Name=mesd; Synonyms=mesdc2; ORFNames=zgc:158636;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Tuebingen; TISSUE=Embryo;
RA   Mathavan S., Yao F., Wong E., Thoreau H., Nayudu M., Govindarajan K.R.,
RA   Ruan Y., Wei C.;
RT   "Zebrafish transcriptome characterization.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone specifically assisting the folding of beta-
CC       propeller/EGF modules within the family of low-density lipoprotein
CC       receptors (LDLRs). Acts as a modulator of the Wnt pathway, since some
CC       LDLRs are coreceptors for the canonical Wnt pathway (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9ERE7, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A1L243-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A1L243-2; Sequence=VSP_038093;
CC   -!- SIMILARITY: Belongs to the MESD family. {ECO:0000305}.
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DR   EMBL; EH610226; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC129340; AAI29341.1; -; mRNA.
DR   RefSeq; NP_001074173.1; NM_001080704.1. [A1L243-2]
DR   RefSeq; XP_005166421.1; XM_005166364.3. [A1L243-1]
DR   AlphaFoldDB; A1L243; -.
DR   SMR; A1L243; -.
DR   STRING; 7955.ENSDARP00000093291; -.
DR   PaxDb; A1L243; -.
DR   PeptideAtlas; A1L243; -.
DR   Ensembl; ENSDART00000172796; ENSDARP00000142197; ENSDARG00000063030. [A1L243-1]
DR   GeneID; 791222; -.
DR   KEGG; dre:791222; -.
DR   CTD; 23184; -.
DR   ZFIN; ZDB-GENE-070112-2142; mesd.
DR   eggNOG; KOG4357; Eukaryota.
DR   GeneTree; ENSGT00390000000993; -.
DR   InParanoid; A1L243; -.
DR   OMA; NRATKQR; -.
DR   OrthoDB; 1590303at2759; -.
DR   PhylomeDB; A1L243; -.
DR   TreeFam; TF315614; -.
DR   PRO; PR:A1L243; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000063030; Expressed in tail and 24 other tissues.
DR   ExpressionAtlas; A1L243; baseline.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR019330; MESD.
DR   PANTHER; PTHR17600; PTHR17600; 1.
DR   Pfam; PF10185; Mesd; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chaperone; Endoplasmic reticulum; Reference proteome;
KW   Signal; Wnt signaling pathway.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..206
FT                   /note="LRP chaperone MESD"
FT                   /id="PRO_0000385020"
FT   REGION          93..166
FT                   /note="Structured core"
FT                   /evidence="ECO:0000250"
FT   REGION          171..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           203..206
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        173..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..51
FT                   /note="MASSVGCRTLSVLFLLVLFITVHCTDTKPKKKKDIRDYNDADMARLLEEWE
FT                   -> MFEC (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_038093"
SQ   SEQUENCE   206 AA;  23307 MW;  7F3E8C76841FA15A CRC64;
     MASSVGCRTL SVLFLLVLFI TVHCTDTKPK KKKDIRDYND ADMARLLEEW EKDDDIEEGD
     LPEHKRSPPP IDFSKIDASK PEELLKMSKK GKTLMVFASV SGNPTEKETE EITGLWQGSL
     FNANYDVQRF VVGSNRVIFM LRDGSYAWEI KDFLVSQDRC EDVTVEGQVF PGKNAKKDAK
     GKEQNETKKK GDKKAANRAN KGKQEL
 
 
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