PLSI_BOVIN
ID PLSI_BOVIN Reviewed; 630 AA.
AC A6H742;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Plastin-1;
GN Name=PLS1;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3V0K9}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:Q3V0K9}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC146105; AAI46106.1; -; mRNA.
DR RefSeq; NP_001096769.1; NM_001103299.2.
DR RefSeq; XP_010799858.1; XM_010801556.2.
DR RefSeq; XP_010799860.1; XM_010801558.2.
DR RefSeq; XP_015328779.1; XM_015473293.1.
DR AlphaFoldDB; A6H742; -.
DR SMR; A6H742; -.
DR STRING; 9913.ENSBTAP00000053019; -.
DR PaxDb; A6H742; -.
DR PeptideAtlas; A6H742; -.
DR PRIDE; A6H742; -.
DR Ensembl; ENSBTAT00000049695; ENSBTAP00000053019; ENSBTAG00000023429.
DR GeneID; 616560; -.
DR KEGG; bta:616560; -.
DR CTD; 5357; -.
DR VEuPathDB; HostDB:ENSBTAG00000023429; -.
DR VGNC; VGNC:33051; PLS1.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR HOGENOM; CLU_015284_2_0_1; -.
DR InParanoid; A6H742; -.
DR OMA; KDDPDCK; -.
DR OrthoDB; 312506at2759; -.
DR TreeFam; TF300680; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000023429; Expressed in abomasum and 87 other tissues.
DR ExpressionAtlas; A6H742; baseline and differential.
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; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:1990357; C:terminal web; IEA:Ensembl.
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 GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:0001951; P:intestinal D-glucose absorption; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0032532; P:regulation of microvillus length; IEA:Ensembl.
DR GO; GO:1902896; P:terminal web assembly; IEA:Ensembl.
DR GO; GO:0060121; P:vestibular receptor cell stereocilium organization; ISS:UniProtKB.
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; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Calcium; Cell projection; Cytoplasm;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..630
FT /note="Plastin-1"
FT /id="PRO_0000364187"
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 108..381
FT /note="Actin-binding 1"
FT REGION 382..626
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="3"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14651"
SQ SEQUENCE 630 AA; 70532 MW; 2495079DEADB208D CRC64;
MENSTTTISR EELEELQEAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIVEKIL
AVADNNKDSR ISFEEFVSLM QELKSKDISK TFRKIINKRE GITAIGGTSS ISSEGTQHSY
SEEEKVAFVN WINKALENDP DCKHLIPMNP NDDSLFKSLA DGILLCKMIN LSEPDTIDER
AINKKKLTPF TISENLNLAL NSASAIGCTV VNIGAQDLTE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLKEGEDL EELMRLSPEE LLLQWVNYHL TNAGWPTISN FSHDIKDSRA
YFHLLNQIAP KGDRDDGPAI AIDLTGFSEK NDLKRAEFML QEADKLGCRQ FVTPADVVSG
NPKLNLAFVA NLFNTYPGLH KPDNNDIDVN LLEGESKEER TFRNWMNSLG VNPYINHLYS
DLADALVIFQ LYEMIRVPVD WSHVNKPPYP ALGGNMKKIE NCNYAVELGK NKAKFSLVGI
AGQDLNEGNS TLTLALVWQL MRRYTLNVLS DLGEGEKVND AIIIEWVNQT LKSANKNTFI
SSFKDKSIST SLPVLDLIDA IAPNAVRQEM IKREDLSDED KLNNAKYAIS VARKIGARIY
ALPDDLVEVK PKMVMTVFAC LMGKGLNKIK
