PLST_RAT
ID PLST_RAT Reviewed; 630 AA.
AC Q63598;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Plastin-3;
DE AltName: Full=T-plastin;
GN Name=Pls3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Saedi M.S., Kerjaschki D., Farquhar M.;
RT "Nucleotide sequence of rat kidney T-plastin.";
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Actin-bundling protein.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X70706; CAA50037.1; ALT_INIT; mRNA.
DR PIR; S31765; S31765.
DR AlphaFoldDB; Q63598; -.
DR SMR; Q63598; -.
DR IntAct; Q63598; 1.
DR STRING; 10116.ENSRNOP00000056912; -.
DR iPTMnet; Q63598; -.
DR PhosphoSitePlus; Q63598; -.
DR jPOST; Q63598; -.
DR PaxDb; Q63598; -.
DR PRIDE; Q63598; -.
DR RGD; 621409; Pls3.
DR eggNOG; KOG0046; Eukaryota.
DR InParanoid; Q63598; -.
DR PhylomeDB; Q63598; -.
DR ChiTaRS; Plscr3; rat.
DR PRO; PR:Q63598; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098699; F:structural constituent of presynaptic actin cytoskeleton; ISO:RGD.
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:0060348; P:bone development; ISO:RGD.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IEP:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
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; IPR039956; PLS2/3.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR PANTHER; PTHR19961:SF32; PTHR19961:SF32; 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; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..630
FT /note="Plastin-3"
FT /id="PRO_0000073749"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..239
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 267..378
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 397..506
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 518..627
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 109..382
FT /note="Actin-binding 1"
FT REGION 383..627
FT /note="Actin-binding 2"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13797"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13797"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13797"
SQ SEQUENCE 630 AA; 70680 MW; 6F3F987D095E3B9B CRC64;
MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL
MLDGDRNKDG KISFNEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS
YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE
RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF
ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK
AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS
GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY
VDLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KNQAKFSLVG
IGGQDLNDGN PTLTLAVVWQ LMRRYTLNVM EDLGEGQKAT DDIIVNWVNG TLSEAGKSTS
IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKTGNLTEE DKHNNAKYAV SMARRIGARV
YALPEDLVEV KPKMVMTVFA CLMGRGMKSV
