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PDLI3_PIG
ID   PDLI3_PIG               Reviewed;         365 AA.
AC   Q6QGC0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=PDZ and LIM domain protein 3;
DE   AltName: Full=Actinin-associated LIM protein;
DE   AltName: Full=Alpha-actinin-2-associated LIM protein;
GN   Name=PDLIM3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Longissimus dorsi muscle;
RA   Tian X., Li J., Wang C., Chen Y.;
RT   "The cloning and expression of alpha-actinin-2-associated LIM protein gene
RT   in pig.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in the organization of actin filament arrays
CC       within muscle cells. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ACTN2 (By similarity). Forms a heterodimer with
CC       PDLIM4 (via LIM domain) (By similarity). {ECO:0000250|UniProtKB:O70209,
CC       ECO:0000250|UniProtKB:Q66HS7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000250}. Note=Localizes to myofiber Z-lines. {ECO:0000250}.
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DR   EMBL; AY543095; AAS55866.1; -; mRNA.
DR   RefSeq; NP_001001637.1; NM_001001637.1.
DR   AlphaFoldDB; Q6QGC0; -.
DR   SMR; Q6QGC0; -.
DR   STRING; 9823.ENSSSCP00000016738; -.
DR   PaxDb; Q6QGC0; -.
DR   PeptideAtlas; Q6QGC0; -.
DR   PRIDE; Q6QGC0; -.
DR   Ensembl; ENSSSCT00000017199; ENSSSCP00000016738; ENSSSCG00000015796.
DR   Ensembl; ENSSSCT00005056527; ENSSSCP00005034788; ENSSSCG00005034876.
DR   Ensembl; ENSSSCT00005056559; ENSSSCP00005034807; ENSSSCG00005034876.
DR   Ensembl; ENSSSCT00015040998; ENSSSCP00015016205; ENSSSCG00015030376.
DR   Ensembl; ENSSSCT00025049163; ENSSSCP00025021020; ENSSSCG00025036042.
DR   Ensembl; ENSSSCT00030103959; ENSSSCP00030048109; ENSSSCG00030074128.
DR   Ensembl; ENSSSCT00035018380; ENSSSCP00035006422; ENSSSCG00035014492.
DR   Ensembl; ENSSSCT00040046658; ENSSSCP00040019555; ENSSSCG00040034605.
DR   Ensembl; ENSSSCT00050027919; ENSSSCP00050011546; ENSSSCG00050020686.
DR   Ensembl; ENSSSCT00055030210; ENSSSCP00055024065; ENSSSCG00055015298.
DR   Ensembl; ENSSSCT00060084157; ENSSSCP00060036458; ENSSSCG00060060611.
DR   Ensembl; ENSSSCT00060084186; ENSSSCP00060036471; ENSSSCG00060060611.
DR   Ensembl; ENSSSCT00065093889; ENSSSCP00065041086; ENSSSCG00065068360.
DR   Ensembl; ENSSSCT00070054507; ENSSSCP00070046233; ENSSSCG00070027183.
DR   GeneID; 414421; -.
DR   KEGG; ssc:414421; -.
DR   CTD; 27295; -.
DR   VGNC; VGNC:95945; PDLIM3.
DR   eggNOG; KOG1703; Eukaryota.
DR   GeneTree; ENSGT00940000156741; -.
DR   InParanoid; Q6QGC0; -.
DR   OrthoDB; 840552at2759; -.
DR   TreeFam; TF106408; -.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Proteomes; UP000314985; Chromosome 15.
DR   Bgee; ENSSSCG00000015796; Expressed in muscle tissue and 44 other tissues.
DR   ExpressionAtlas; Q6QGC0; baseline and differential.
DR   Genevisible; Q6QGC0; SS.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR031847; DUF4749.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR006643; Zasp-like_motif.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF15936; DUF4749; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00735; ZM; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; LIM domain; Metal-binding; Phosphoprotein; Reference proteome;
KW   Zinc.
FT   CHAIN           1..365
FT                   /note="PDZ and LIM domain protein 3"
FT                   /id="PRO_0000075869"
FT   DOMAIN          1..84
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          293..352
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          126..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66HS7"
SQ   SEQUENCE   365 AA;  39546 MW;  B66EE3A4CF35FCAA CRC64;
     MPQNVILPGP APWGFRLSGG IDFNQPLIIT RITPGSKAAA ANLCPGDVIL AIDGYGTESM
     THADAQDRIK AAAHQLCLKI DRAETRLWSP QVTEDGKAHP FKINLESEPQ DVNYFEHKHN
     IRPKPFIIPG RSSGCSTPSG IDGGSGRSTP SSVSTLSTIC PGDLKVAAKM APNIPLEMEL
     PGVKIVHAQF NTPMQLYSDD NIMETLQGQV STALGETPSM SEPTTASVPP QSDVYRMLHD
     NRNEPTQPRQ SGSFRVLQEL VNDGPDDRPA GTRSVRAPVT KIHGGAGGTQ KMPLCDKCGS
     GIVGAVVKAR DKYRHPECFV CADCNLNLKQ KGYFFVEGEL YCETHARARM RPPEGYDTVT
     LYPKA
 
 
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