PLSL_DANRE
ID PLSL_DANRE Reviewed; 624 AA.
AC Q6P698; Q9W746;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Plastin-2;
DE AltName: Full=L-plastin;
DE AltName: Full=Lymphocyte cytosolic plastin 1;
GN Name=lcp1 {ECO:0000312|EMBL:AAH62381.1}; Synonyms=pls2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAH62381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH62381.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD40680.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 423-624, AND DEVELOPMENTAL STAGE.
RX PubMed=10433904; DOI=10.1242/dev.126.17.3735;
RA Herbomel P., Thisse B., Thisse C.;
RT "Ontogeny and behaviour of early macrophages in the zebrafish embryo.";
RL Development 126:3735-3745(1999).
CC -!- FUNCTION: Actin-binding protein. Plays a role in the activation of T-
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P13796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P13796}. Cell junction
CC {ECO:0000250|UniProtKB:P13796}. Cell projection
CC {ECO:0000250|UniProtKB:P13796}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P13796, ECO:0000250|UniProtKB:Q61233};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q61233}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q61233}.
CC -!- DEVELOPMENTAL STAGE: Expressed in macrophage precursors as they migrate
CC from the midline to the yolksac during somatogenesis. Prior to blood
CC circulation, continues to be expressed in maturing macrophage
CC precursors in the yolksac and in those that have migrated to the
CC mesenchyme of the head. At 28 hours post-fertilization (hpf), also
CC expressed in the caudal part of the axial vein and the surrounding
CC mesenchyme. {ECO:0000269|PubMed:10433904}.
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DR EMBL; BC062381; AAH62381.1; -; mRNA.
DR EMBL; AF157110; AAD40680.1; -; mRNA.
DR AlphaFoldDB; Q6P698; -.
DR SMR; Q6P698; -.
DR STRING; 7955.ENSDARP00000108316; -.
DR PaxDb; Q6P698; -.
DR PRIDE; Q6P698; -.
DR ZFIN; ZDB-GENE-991213-5; lcp1.
DR eggNOG; KOG0046; Eukaryota.
DR InParanoid; Q6P698; -.
DR PhylomeDB; Q6P698; -.
DR PRO; PR:Q6P698; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
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; 3.
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 2: Evidence at transcript level;
KW Actin-binding; Calcium; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..624
FT /note="Plastin-2"
FT /id="PRO_0000073745"
FT DOMAIN 9..44
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 118..234
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 262..373
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 392..501
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 513..621
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 118..373
FT /note="Actin-binding 1"
FT /evidence="ECO:0000255"
FT REGION 392..621
FT /note="Actin-binding 2"
FT /evidence="ECO:0000255"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 423..424
FT /note="VI -> HE (in Ref. 2; AAD40680)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="D -> G (in Ref. 2; AAD40680)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="K -> E (in Ref. 2; AAD40680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 69900 MW; F78D17B8BF1D4D6F CRC64;
MAAAQISAEE MEELREAFTK VDVDGNGHIS TDELNALFKA ANLPLPGYRV REIIQEISRT
MDLNQDGKIT FDEFAKVVHD LKSSEVAKTF RKAINKKEGI CSVAGTSEQS GTQHSYSEEE
KVAFVNWVNK ALEKDPDCQH VLPMDPSTDD LFTAVGDGIV LCKMINLSVP DTIDERTINK
KKLTPFTIQE NLNLALNSAS AIGCHVVNIG AEDLKEGRQH LVLGLLWQVI KIGLFADIEI
SRNEALIALL RDGESLEDLV KLSPEELLLR WANYHLEEAG CPKINNFSSD IKDSKAYYNI
LNQVAPKRDE EGIPAIPIDI SGIREKDDLK RAECMLEQAD RLGCRQFVTA TDVVRGNPKL
NLAYVANLFN KYPALKKPEN QDIDWSSIEG ETREERTFRN WMNSLGVNPR VNHLYVDLAD
ALVIFQLYEK IKVPVDWDKV NKPPYPKLGS NMKKLENCNY AVELGKKEAK FSLVGIAGQD
LNEGNRTLTL ALLWQLMRRY TLNILEDLGD GQKIIDETIV QWVNETLTQA GKGTISGFKD
GSISSSMPVL DLIDAIQPGS IRYDLLKAED LTDEKKLNNA KYAISMARKI GARVYALPED
LVEVKPKMVM TVFACLMARG MRRI
