LPP_CHICK
ID LPP_CHICK Reviewed; 604 AA.
AC Q5F464;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Lipoma-preferred partner homolog;
GN Name=LPP; ORFNames=RCJMB04_2l20;
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 [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 play a structural role at sites of cell adhesion in
CC maintaining cell shape and motility. May be involved in signal
CC transduction from cell adhesion sites to the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell junction {ECO:0000250}. Note=Found in the nucleus, in the
CC cytoplasm and at cell adhesion sites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; AJ851436; CAH65070.1; -; mRNA.
DR RefSeq; NP_001026738.1; NM_001031567.1.
DR RefSeq; XP_015146918.1; XM_015291432.1.
DR RefSeq; XP_015146919.1; XM_015291433.1.
DR RefSeq; XP_015146921.1; XM_015291435.1.
DR RefSeq; XP_015146922.1; XM_015291436.1.
DR RefSeq; XP_015146923.1; XM_015291437.1.
DR RefSeq; XP_015146924.1; XM_015291438.1.
DR RefSeq; XP_015146925.1; XM_015291439.1.
DR RefSeq; XP_015146926.1; XM_015291440.1.
DR AlphaFoldDB; Q5F464; -.
DR SMR; Q5F464; -.
DR STRING; 9031.ENSGALP00000011857; -.
DR PaxDb; Q5F464; -.
DR Ensembl; ENSGALT00000011871; ENSGALP00000011857; ENSGALG00000007337.
DR Ensembl; ENSGALT00000105031; ENSGALP00000066879; ENSGALG00000007337.
DR GeneID; 429148; -.
DR KEGG; gga:429148; -.
DR CTD; 4026; -.
DR VEuPathDB; HostDB:geneid_429148; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000156022; -.
DR HOGENOM; CLU_001357_10_0_1; -.
DR InParanoid; Q5F464; -.
DR OMA; FNPYKQM; -.
DR OrthoDB; 483341at2759; -.
DR PhylomeDB; Q5F464; -.
DR TreeFam; TF320310; -.
DR PRO; PR:Q5F464; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000007337; Expressed in skeletal muscle tissue and 9 other tissues.
DR ExpressionAtlas; Q5F464; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR InterPro; IPR028771; LPP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24207:SF0; PTHR24207:SF0; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 2: Evidence at transcript level;
KW Activator; Cell adhesion; Cell junction; Cytoplasm; LIM domain;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT CHAIN 1..604
FT /note="Lipoma-preferred partner homolog"
FT /id="PRO_0000075835"
FT DOMAIN 406..465
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 466..526
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 527..595
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 31..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65139 MW; E3DBF28A196F4C43 CRC64;
MSHPSWLPPK STNEPVGHVT ARMETTHAFG TPSISVSTQQ TPKKFAPVVA PKPKYNPYKQ
PGGDGDFLPP PPPPVDDLGN ITSQGAFPPP PPLDDVAFNV QVNPGGKTLE ERRSSLDAEI
DSLTSILADL ESSSPYKPRI QQGSGTSSSA ATTPSVSTPV TGHKRMIIPN QPPLTATKKS
TAKGPGQPAP IPVTPIGTLK PQPVPASYTT ASTPSRPTFN VQVRTAQPSP HYQPPGPQPT
HYGSLGPGQP YAAPPARPPG AQQYGSPQPR GPDYGYAPPP ARPSEPSYGY APQQGRYQDP
YYGGYGGRNG SEAPYMPQST WKVEPAYPSS NTVGQAPPGM YQHPGPKKTY ITDPVLAPQP
LQQKSGYPSS GPTSSTPAFR PEDELEHLTK KMLYDMENPP SDDYFGRCAR CGENVVGEGT
GCTAMDQVFH VECFTCMMCN NKLRGQPFYA VEKKAYCEPC YINTLEQCSV CAKPIMERIL
RATGKAYHPH CFTCVMCHRS LDGIPFTVDA GGNIHCIEDF HKKFAPRCSV CKEPIMPAPG
QEETVRIVAL DRDFHVQCYR CEDCGGLLSE GDNQGCYPLD GHILCKTCNS ARIQALTAKA
STDL
