LOCUS NP_005442 457 aa linear PRI 04-JAN-2024
DEFINITION PDZ and LIM domain protein 7 isoform 1 [Homo sapiens].
ACCESSION NP_005442
VERSION NP_005442.2
DBSOURCE REFSEQ: accession NM_005451.5
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 457)
AUTHORS Rood K, Yamauchi CR, Sharma U, Laxa RT, Robins C, Lanza G,
Sanchez-Ruiz K, Khan A, Kim HS, Shields A, Kennedy K, Mirshahidi S,
Perez MC, Firek A, Munir I, Simental AA and Khan S.
TITLE Regulatory and Interacting Partners of PDLIM7 in Thyroid Cancer
JOURNAL Curr Oncol 30 (12), 10450-10462 (2023)
PUBMED 38132395
REMARK GeneRIF: Regulatory and Interacting Partners of PDLIM7 in Thyroid
Cancer.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 457)
AUTHORS Santos ERCD, Silva MSDME, Canedo NHS, Gaui MFD, Britto ALVL, Silva
WMVD, Carvalho MDGDC and Bravo Neto GP.
TITLE Epstein-Barr virus in gastric cancer and association with 30 bp
del-latent membrane protein 1 polymorphism
JOURNAL Rev Assoc Med Bras (1992) 69 (5), e20221571 (2023)
PUBMED 37222327
REMARK GeneRIF: Epstein-Barr virus in gastric cancer and association with
30 bp del-latent membrane protein 1 polymorphism.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 457)
AUTHORS Nilsson G, Leppert J and Ohrvik J.
TITLE Enigma of the cholesterol paradox in acute myocardial infarction:
lessons from an 8-year follow-up of all-cause mortality in an
age-matched and sex-matched case-control study with controls from
the patients' recruitment area
JOURNAL BMJ Open 12 (7), e057562 (2022)
PUBMED 35896296
REMARK GeneRIF: Enigma of the cholesterol paradox in acute myocardial
infarction: lessons from an 8-year follow-up of all-cause mortality
in an age-matched and sex-matched case-control study with controls
from the patients' recruitment area.
Publication Status: Online-Only
REFERENCE 4 (residues 1 to 457)
AUTHORS Benz C, Ali M, Krystkowiak I, Simonetti L, Sayadi A, Mihalic F,
Kliche J, Andersson E, Jemth P, Davey NE and Ivarsson Y.
TITLE Proteome-scale mapping of binding sites in the unstructured regions
of the human proteome
JOURNAL Mol Syst Biol 18 (1), e10584 (2022)
PUBMED 35044719
REFERENCE 5 (residues 1 to 457)
AUTHORS Liu Y, Zhou W, Chen FF, Xiao F, Zhu HY, Zhou Y and Guo GC.
TITLE Overexpression of LMP-1 Decreases Apoptosis in Human Nucleus
Pulposus Cells via Suppressing the NF-kappaB Signaling Pathway
JOURNAL Oxid Med Cell Longev 2020, 8189706 (2020)
PUBMED 33414896
REMARK GeneRIF: Overexpression of LMP-1 Decreases Apoptosis in Human
Nucleus Pulposus Cells via Suppressing the NF-kappaB Signaling
Pathway.
Publication Status: Online-Only
REFERENCE 6 (residues 1 to 457)
AUTHORS Bach I.
TITLE The LIM domain: regulation by association
JOURNAL Mech Dev 91 (1-2), 5-17 (2000)
PUBMED 10704826
REMARK Review article
REFERENCE 7 (residues 1 to 457)
AUTHORS Guy PM, Kenny DA and Gill GN.
TITLE The PDZ domain of the LIM protein enigma binds to beta-tropomyosin
JOURNAL Mol Biol Cell 10 (6), 1973-1984 (1999)
PUBMED 10359609
REFERENCE 8 (residues 1 to 457)
AUTHORS Durick K, Gill GN and Taylor SS.
TITLE Shc and Enigma are both required for mitogenic signaling by
Ret/ptc2
JOURNAL Mol Cell Biol 18 (4), 2298-2308 (1998)
PUBMED 9528800
REFERENCE 9 (residues 1 to 457)
AUTHORS Kuroda S, Tokunaga C, Kiyohara Y, Higuchi O, Konishi H, Mizuno K,
Gill GN and Kikkawa U.
TITLE Protein-protein interaction of zinc finger LIM domains with protein
kinase C
JOURNAL J Biol Chem 271 (49), 31029-31032 (1996)
PUBMED 8940095
REFERENCE 10 (residues 1 to 457)
AUTHORS Wu RY and Gill GN.
TITLE LIM domain recognition of a tyrosine-containing tight turn
JOURNAL J Biol Chem 269 (40), 25085-25090 (1994)
PUBMED 7929196
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from HY026171.1 and BC001093.2.
On Dec 1, 2000 this sequence version replaced NP_005442.1.
Summary: The protein encoded by this gene is representative of a
family of proteins composed of conserved PDZ and LIM domains. LIM
domains are proposed to function in protein-protein recognition in
a variety of contexts including gene transcription and development
and in cytoskeletal interaction. The LIM domains of this protein
bind to protein kinases, whereas the PDZ domain binds to actin
filaments. The gene product is involved in the assembly of an actin
filament-associated complex essential for transmission of ret/ptc2
mitogenic signaling. The biological function is likely to be that
of an adapter, with the PDZ domain localizing the LIM-binding
proteins to actin filaments of both skeletal muscle and nonmuscle
tissues. Alternative splicing of this gene results in multiple
transcript variants. [provided by RefSeq, Jul 2008].
Transcript Variant: This variant (1) encodes the longest isoform
(1).
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC001093.2, SRR3476690.573383.1
[ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000355841.7/ ENSP00000348099.2
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..457
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="5"
/map="5q35.3"
Protein 1..457
/product="PDZ and LIM domain protein 7 isoform 1"
/note="LIM domain protein; 1110003B01Rik; PDZ and LIM
domain protein 7; LMP; protein enigma; Lim mineralization
protein 3; PDZ and LIM domain 7 (enigma)"
/calculated_mol_wt=49714
Region 5..79
/region_name="PDZ_signaling"
/note="PDZ domain found in a variety of Eumetazoan
signaling molecules, often in tandem arrangements. May be
responsible for specific protein-protein interactions, as
most PDZ domains bind C-terminal polypeptides, and binding
to internal (non-C-terminal)...; cd00992"
/db_xref="CDD:238492"
Site order(13..16,18,66..67,70..71)
/site_type="other"
/note="protein binding site [polypeptide binding]"
/db_xref="CDD:238492"
Site 78
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9NR12.1)"
Region <81..254
/region_name="PHA03247"
/note="large tegument protein UL36; Provisional"
/db_xref="CDD:223021"
Region 82..142
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9NR12.1)"
Site 103
/site_type="methylation"
/note="Asymmetric dimethylarginine.
/evidence=ECO:0007744|PubMed:24129315; propagated from
UniProtKB/Swiss-Prot (Q9NR12.1)"
Site 111
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q9NR12.1)"
Region <120..189
/region_name="DUF4749"
/note="Domain of unknown function (DUF4749); pfam15936"
/db_xref="CDD:435028"
Region 176..226
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9NR12.1)"
Region 239..258
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9NR12.1)"
Site 247
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (Q9NR12.1)"
Region 282..333
/region_name="LIM1_Enigma"
/note="The first LIM domain of Enigma; cd09452"
/db_xref="CDD:188836"
Site order(282,285,302,305,308,311,329,332)
/site_type="other"
/note="Zn binding site [ion binding]"
/db_xref="CDD:188836"
Region 341..392
/region_name="LIM2_Enigma"
/note="The second LIM domain of Enigma; cd09456"
/db_xref="CDD:188840"
Site order(341,344,361,364,367,370,388,391)
/site_type="other"
/note="Zn binding site [ion binding]"
/db_xref="CDD:188840"
Region 400..454
/region_name="LIM3_Enigma"
/note="The third LIM domain of Enigma; cd09458"
/db_xref="CDD:188842"
Site order(400,403,422,425,428,431,449,452)
/site_type="other"
/note="Zn binding site [ion binding]"
/db_xref="CDD:188842"
CDS 1..457
/gene="PDLIM7"
/gene_synonym="LMP1; LMP3"
/coded_by="NM_005451.5:89..1462"
/note="isoform 1 is encoded by transcript variant 1"
/db_xref="CCDS:CCDS4422.1"
/db_xref="GeneID:9260"
/db_xref="HGNC:HGNC:22958"
/db_xref="MIM:605903"
ORIGIN
1 mdsfkvvleg papwgfrlqg gkdfnvplsi srltpggkaa qagvavgdwv lsidgenags
61 lthieaqnki racgerlslg lsraqpvqsk pqkasapaad pprytfapsv slnktarpfg
121 apppadsapq qngqplrplv pdaskqrlme ntedwrprpg tgqsrsfril ahltgtefmq
181 dpdeehlkks sqvprteapa passtpqepw pgptapspts rppwavdpaf aeryapdkts
241 tvltrhsqpa tptplqsrts ivqaaaggvp gggsnngktp vchqchkvir grylvalgha
301 yhpeefvcsq cgkvleeggf feekgaifcp pcydvryaps cakckkkitg eimhalkmtw
361 hvhcftcaac ktpirnrafy meegvpycer dyekmfgtkc hgcdfkidag drflealgfs
421 whdtcfvcai cqinlegktf yskkdrplck shafshv
//
