PDLI7_BOVIN
ID PDLI7_BOVIN Reviewed; 424 AA.
AC Q3SX40; Q5E9L1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=PDZ and LIM domain protein 7;
GN Name=PDLIM7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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. Involved in both of the two
CC fundamental mechanisms of bone formation, direct bone formation (e.g.
CC embryonic flat bones mandible and cranium), and endochondral bone
CC formation (e.g. embryonic long bone development). Plays a role during
CC fracture repair. Involved in BMP6 signaling pathway (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds via its LIM zinc-binding 3 domain (LIM 3) domain to
CC endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or
CC EGFR. Interacts with various PKC isoforms through the LIM zinc-binding
CC domains. Binds to RET in a phosphorylation-independent manner via its
CC LIM zinc-binding 2 domain (LIM 2). Probably part of a complex with SHC
CC and the RET dimer. Interacts with TPM2, TBX4 and TBX5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in
CC some cytoskeletal components. Colocalizes with TPM2 near the Z line in
CC muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3SX40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SX40-2; Sequence=VSP_016506, VSP_016507, VSP_016508;
CC -!- DOMAIN: The LIM zinc-binding 2 (LIM 2) interacts with TBX4.
CC {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 This domain is necessary and sufficient for interaction with TBX5 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain.
CC {ECO:0000250}.
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DR EMBL; BT020909; AAX08926.1; -; mRNA.
DR EMBL; BC104521; AAI04522.1; -; mRNA.
DR RefSeq; NP_001017947.1; NM_001017947.1. [Q3SX40-2]
DR RefSeq; NP_001106722.1; NM_001113251.1. [Q3SX40-1]
DR RefSeq; XP_005209262.1; XM_005209205.3. [Q3SX40-2]
DR RefSeq; XP_010805461.1; XM_010807159.2. [Q3SX40-2]
DR AlphaFoldDB; Q3SX40; -.
DR SMR; Q3SX40; -.
DR STRING; 9913.ENSBTAP00000024902; -.
DR PRIDE; Q3SX40; -.
DR Ensembl; ENSBTAT00000009662; ENSBTAP00000009662; ENSBTAG00000011400. [Q3SX40-2]
DR GeneID; 533851; -.
DR KEGG; bta:533851; -.
DR CTD; 9260; -.
DR VEuPathDB; HostDB:ENSBTAG00000011400; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159431; -.
DR HOGENOM; CLU_001357_8_1_1; -.
DR InParanoid; Q3SX40; -.
DR Reactome; R-BTA-8853659; RET signaling.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000011400; Expressed in aorta and 107 other tissues.
DR ExpressionAtlas; Q3SX40; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; 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 Alternative splicing; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; LIM domain; Metal-binding; Osteogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..424
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075880"
FT DOMAIN 1..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 247..305
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 306..365
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 366..424
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 81..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR12"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z9"
FT VAR_SEQ 94..99
FT /note="VQTPDK -> ALAPAADPPRYTFAPSASLNKTARPFGANPPADSAPQQNG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_016506"
FT VAR_SEQ 157..188
FT /note="SQVPRTEAPTPASATPQEPWPGPTTPSPTSRP -> REKYVLELQSPRYTRL
FT RDWHHQRSAHVLNVQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_016507"
FT VAR_SEQ 189..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_016508"
SQ SEQUENCE 424 AA; 46433 MW; AEEC4F553090BE05 CRC64;
MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGG
LTHIEAQNKI RACGERLSLS LSRAQPAQSK PQKVQTPDKQ PLRPLVPDAS KQRLMEDTED
WRPRPGTGQS RSFRILAHLT GTEFMQDPDE EHLKKSSQVP RTEAPTPASA TPQEPWPGPT
TPSPTSRPPW AVDPAFAERY APDKTSTVLT RHTQPATPTP MQNRTSIVQA AAGGGHGGGG
GSNGKTPVCH QCHKVIRGRY LVALGRAYHP EEFVCSQCGK VLEEGGFFEE KGAIFCPPCY
DVRYAPSCAK CKKKITGEVM HALKTTWHVH CFTCAACKAP IRNRAFYMEE GAPYCEPDYE
KMFGTKCRGC DFKIDAGDRF LEALGFSWHD TCFVCAICQI NLEGKTFYSK KDKPLCKSHA
FSHV
