PDLI7_XENLA
ID PDLI7_XENLA Reviewed; 421 AA.
AC Q6INU3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=PDZ and LIM domain protein 7;
GN Name=pdlim7;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a scaffold on which the coordinated assembly
CC of proteins can occur. May play a role as an adapter that, via its PDZ
CC domain, localizes LIM-binding proteins to actin filaments of both
CC skeletal muscle and nonmuscle tissues (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding 3 (LIM 3) domain provides the structural
CC basis for recognition of tyrosine-containing tight turn structures.
CC {ECO:0000250}.
CC -!- DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain.
CC {ECO:0000250}.
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; BC072179; AAH72179.1; -; mRNA.
DR AlphaFoldDB; Q6INU3; -.
DR SMR; Q6INU3; -.
DR IntAct; Q6INU3; 1.
DR OMA; ESQRICH; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..421
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075886"
FT DOMAIN 1..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 244..302
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 303..362
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 363..421
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 115..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46427 MW; 75EB7169099CBB27 CRC64;
MEEYKVTLDG PAPWGFRLQG GKDFNMPLSI SRLTPGGKSE LAGVNVGDWL LQIEGDSTAS
MTHIEAQNKI RASSNKLGLV LSRFAVGANH PKGVHTPESQ GRKYNFAPST ALNKIARPFG
SGTPPPDNSR PVQVTKPVAY NPPPTSYPSS QMPQGQLQNG QKSRTVSNVS GKDTTDHPIP
PAPSTGPAVR PPWTTDPTFA DRYAPDKTTT VMTKHTQPAT PTPAQSRNSI LQAAQVPSSG
DKTPVCSQCN KIIRGRFLLA LGRYYHPEEF TCSQCHKVLE EGGFFEEKGS IFCPCCYDAR
FAPNCAKCKK KITGEIMHAL KMTWHVPCFT CAYCKTPIRN RAFYMEDGKP YCEKDYEQMF
GTKCRGCDFK IDAGDRFLEA LGFSWHDTCF VCAICQINLE GKTFYSKKDK PLCKTHAFSN
V