PLSI_CHICK
ID PLSI_CHICK Reviewed; 630 AA.
AC P19179;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Plastin-1;
DE AltName: Full=Fimbrin;
GN Name=PLS1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Intestine;
RX PubMed=2391360; DOI=10.1083/jcb.111.3.1069;
RA de Arruda M.V., Watson S., Lin C.-S., Leavitt J., Matsudaira P.;
RT "Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has
RT domains homologous with calmodulin and actin gelation proteins.";
RL J. Cell Biol. 111:1069-1079(1990).
CC -!- FUNCTION: Actin-bundling protein. In the inner ear, it is required for
CC stereocilia formation. Mediates liquid packing of actin filaments that
CC is necessary for stereocilia to grow to their proper dimensions.
CC {ECO:0000250|UniProtKB:Q3V0K9}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3V0K9}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:Q3V0K9}.
CC -!- PTM: The N-terminus is blocked.
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; X52562; CAA36796.1; -; mRNA.
DR PIR; A37097; A37097.
DR RefSeq; NP_990678.1; NM_205347.1.
DR RefSeq; XP_015132331.1; XM_015276845.1.
DR AlphaFoldDB; P19179; -.
DR SMR; P19179; -.
DR BioGRID; 676550; 1.
DR STRING; 9031.ENSGALP00000004164; -.
DR PaxDb; P19179; -.
DR Ensembl; ENSGALT00000004173; ENSGALP00000004164; ENSGALG00000002647.
DR Ensembl; ENSGALT00000078701; ENSGALP00000056193; ENSGALG00000002647.
DR Ensembl; ENSGALT00000098713; ENSGALP00000070144; ENSGALG00000002647.
DR GeneID; 396291; -.
DR KEGG; gga:396291; -.
DR CTD; 5357; -.
DR VEuPathDB; HostDB:geneid_396291; -.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR HOGENOM; CLU_015284_2_0_1; -.
DR InParanoid; P19179; -.
DR OMA; KDDPDCK; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; P19179; -.
DR TreeFam; TF300680; -.
DR PRO; PR:P19179; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000002647; Expressed in colon and 7 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; TAS:AgBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:AgBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR InterPro; IPR030235; PLS1.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR PANTHER; PTHR19961:SF27; PTHR19961:SF27; 1.
DR Pfam; PF00307; CH; 4.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00033; CH; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 2.
DR PROSITE; PS00020; ACTININ_2; 2.
DR PROSITE; PS50021; CH; 4.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell projection; Cytoplasm;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..630
FT /note="Plastin-1"
FT /id="PRO_0000073751"
FT DOMAIN 11..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..238
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 266..377
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 396..505
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 517..626
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..114
FT /note="Fimbrin headpiece"
FT REGION 108..375
FT /note="Actin-binding 1"
FT REGION 115..630
FT /note="Fimbrin core"
FT REGION 376..624
FT /note="Actin-binding 2"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 630 AA; 70939 MW; F616F228A86E8F1E CRC64;
MENNVTTISR EELEELREAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIIEKIF
AVTDSNKDGK INFEEFVSLI QELKSKDVSK SYRKSINKKL GITALGGTSS ISTEGTQHSY
SEEEKVAFVN WINKALQDDP DCKHILPMNP SDASLFKSLA DGILLCKMIN FSQPDTIDER
AINKKKLTPF TISENLNLAL NSASAIGCTV VNIGSQDLQE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLNEGEEL DQLMKLSPEE LLLRWVNYHL ANAGWQKISN FSQDIRDSRA
YYHLLNQIAP KGDDFDEIHV EIDFSGFNDK NDLRRAECML QQADKLGCRQ FVTPADVVAG
NPKLNLAFVA NLFNTYPALH KPDNSSYDLT LLEGESNEER TFRNWMNSLG VSPYVNHLYS
DLSDALIIFQ LYEMTRVPVD WTHVNKRPYP LLGGNMKKIE NCNYAVELGK TKAKFSLVGI
AGHDLNEGNP TLTLALIWQL MRRYTLNVLS DLGEGEKVND EIIIKWVNQT LANANKKTSI
TSFKDKSIST SLPVLDLIDA IAPKAVRQEM VKREDLSYQD KLNNAKYAIS VARKIGARIY
ALPDDLVEVK PKMVMTVFAC LMGRGLNKIK
