PDLI7_CHICK
ID PDLI7_CHICK Reviewed; 416 AA.
AC Q679P3; Q5ZJY4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=PDZ and LIM domain protein 7;
DE AltName: Full=LIM mineralization protein;
DE Short=LMP;
GN Name=PDLIM7; Synonyms=LMP; ORFNames=RCJMB04_14g20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH TBX4 AND TBX5.
RX PubMed=15302601; DOI=10.1016/j.ydbio.2004.05.024;
RA Krause A., Zacharias W., Camarata T., Linkhart B., Law E., Lischke A.,
RA Miljan E., Simon H.-G.;
RT "Tbx5 and Tbx4 transcription factors interact with a new chicken PDZ-LIM
RT protein in limb and heart development.";
RL Dev. Biol. 273:106-120(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. May be involved in bone
CC formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with various PKC isoforms through the LIM zinc-
CC binding domains. Interacts with TPM2 (By similarity). Interacts with
CC TBX4 and TBX5. {ECO:0000250, ECO:0000269|PubMed:15302601}.
CC -!- INTERACTION:
CC Q679P3; O93288: TBX4; NbExp=3; IntAct=EBI-6693710, EBI-6663926;
CC Q679P3; Q9PWE8: TBX5; NbExp=4; IntAct=EBI-6693710, EBI-6663870;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15302601}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:15302601}. Note=Colocalizes with TPM2 near the Z
CC line in muscle (By similarity). Colocalizes with TBX4 and TBX5 to actin
CC filaments. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the presumptive fore- and hindlimb.
CC Continues to be expressed in the limb mesenchyme throughout forelimb
CC and hindlimb bud outgrowth. Expressed in the developing heart and eye.
CC {ECO:0000269|PubMed:15302601}.
CC -!- DOMAIN: The LIM zinc-binding 2 (LIM 2) interacts with TBX4.
CC -!- DOMAIN: The LIM zinc-binding 3 (LIM 3) domain provides the structural
CC basis for recognition of tyrosine-containing tight turn structures (By
CC similarity). This domain is necessary and sufficient for interaction
CC with TBX5. {ECO:0000250}.
CC -!- DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain.
CC {ECO:0000250}.
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DR EMBL; AY376690; AAR24913.1; -; mRNA.
DR EMBL; AJ720300; CAG31959.1; -; mRNA.
DR RefSeq; NP_001005345.2; NM_001005345.1.
DR AlphaFoldDB; Q679P3; -.
DR SMR; Q679P3; -.
DR IntAct; Q679P3; 2.
DR STRING; 9031.ENSGALP00000042621; -.
DR GeneID; 416362; -.
DR KEGG; gga:416362; -.
DR CTD; 9260; -.
DR VEuPathDB; HostDB:geneid_416362; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q679P3; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q679P3; -.
DR PRO; PR:Q679P3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:AgBase.
DR GO; GO:0005884; C:actin filament; IDA:AgBase.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0031941; C:filamentous actin; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:AgBase.
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:0008134; F:transcription factor binding; IPI:AgBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:AgBase.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:AgBase.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IDA:AgBase.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW LIM domain; Metal-binding; Osteogenesis; Reference proteome; Repeat; Zinc.
FT CHAIN 1..416
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075884"
FT DOMAIN 1..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 239..297
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 298..357
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 358..416
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 145..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45724 MW; E668BEB3D4D75F62 CRC64;
MESYKVMLNG PAPWGFRLQG GKDFSMPLSI SRLTPGGKAA QAGVGVGDWV LYIDGESTGT
MTHIEAQNRI RACGDRLCLT LSRAQNHLGK PQKDSLPCSE PPKYNFAPST ALNKTARPFG
ASSPPNPRPG LVTKPVTYVP LAPACTPQHN GQVSVPDPSP GAAMKTEPGL APRTPAATPG
PTSRPPWAVD PSFAERYAPD KTSTVLSKHS QPATPTPMQN RSSIVQAAQQ APESPGRTPL
CYKCNKIIRG RYLVALGHYY HPEEFTCCQC RKVLDEGGFF EEKGSIFCPK CYDTRYAPSC
AKCKKKITGE VMHALKMTWH VQCFTCAACK TPIRNRAFYM EEGQPYCERD YEKMFGTKCR
GCDFKIDAGD RFLEALGFSW HDTCFVCAIC QTNLEGKTFY SKKDKPLCKS HAFSHV
