PLSI_MOUSE
ID PLSI_MOUSE Reviewed; 630 AA.
AC Q3V0K9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Plastin-1;
GN Name=Pls1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25124451; DOI=10.1093/hmg/ddu417;
RA Taylor R., Bullen A., Johnson S.L., Grimm-Guenter E.M., Rivero F.,
RA Marcotti W., Forge A., Daudet N.;
RT "Absence of plastin 1 causes abnormal maintenance of hair cell stereocilia
RT and a moderate form of hearing loss in mice.";
RL Hum. Mol. Genet. 24:37-49(2015).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27811163; DOI=10.1083/jcb.201606036;
RA Krey J.F., Krystofiak E.S., Dumont R.A., Vijayakumar S., Choi D.,
RA Rivero F., Kachar B., Jones S.M., Barr-Gillespie P.G.;
RT "Plastin 1 widens stereocilia by transforming actin filament packing from
RT hexagonal to liquid.";
RL J. Cell Biol. 215:467-482(2016).
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 (PubMed:27811163). {ECO:0000269|PubMed:25124451,
CC ECO:0000269|PubMed:27811163}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC stereocilium {ECO:0000269|PubMed:25124451,
CC ECO:0000269|PubMed:27811163}.
CC -!- TISSUE SPECIFICITY: In the inner ear, it is expressed in the organ of
CC Corti (PubMed:25124451). Abundant in the utricle (at protein level)
CC (PubMed:27811163). {ECO:0000269|PubMed:25124451,
CC ECO:0000269|PubMed:27811163}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Knockout animals have a progressive form of
CC hearing loss at all frequencies. Hearing loss is moderate in young
CC adult mice, progresses to severe deafness with age, and is associated
CC with defects in stereocilia morphology. Stereocilia are shorter and
CC narrower than those of wild-type mice. {ECO:0000269|PubMed:25124451,
CC ECO:0000269|PubMed:27811163}.
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DR EMBL; AK133070; BAE21495.1; -; mRNA.
DR EMBL; CH466560; EDL20943.1; -; Genomic_DNA.
DR EMBL; BC139068; AAI39069.1; -; mRNA.
DR EMBL; BC139069; AAI39070.1; -; mRNA.
DR CCDS; CCDS23412.1; -.
DR RefSeq; NP_001028382.1; NM_001033210.3.
DR RefSeq; XP_006510809.1; XM_006510746.3.
DR RefSeq; XP_006510810.1; XM_006510747.2.
DR AlphaFoldDB; Q3V0K9; -.
DR SMR; Q3V0K9; -.
DR BioGRID; 221886; 1.
DR IntAct; Q3V0K9; 3.
DR MINT; Q3V0K9; -.
DR STRING; 10090.ENSMUSP00000091317; -.
DR iPTMnet; Q3V0K9; -.
DR PhosphoSitePlus; Q3V0K9; -.
DR jPOST; Q3V0K9; -.
DR MaxQB; Q3V0K9; -.
DR PaxDb; Q3V0K9; -.
DR PeptideAtlas; Q3V0K9; -.
DR PRIDE; Q3V0K9; -.
DR ProteomicsDB; 289627; -.
DR Antibodypedia; 33495; 155 antibodies from 25 providers.
DR DNASU; 102502; -.
DR Ensembl; ENSMUST00000093800; ENSMUSP00000091317; ENSMUSG00000049493.
DR GeneID; 102502; -.
DR KEGG; mmu:102502; -.
DR UCSC; uc009rbk.2; mouse.
DR CTD; 5357; -.
DR MGI; MGI:104809; Pls1.
DR VEuPathDB; HostDB:ENSMUSG00000049493; -.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR HOGENOM; CLU_015284_2_0_1; -.
DR InParanoid; Q3V0K9; -.
DR OMA; KDDPDCK; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q3V0K9; -.
DR TreeFam; TF300680; -.
DR BioGRID-ORCS; 102502; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Pls1; mouse.
DR PRO; PR:Q3V0K9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3V0K9; protein.
DR Bgee; ENSMUSG00000049493; Expressed in intestinal villus and 172 other tissues.
DR ExpressionAtlas; Q3V0K9; baseline and differential.
DR Genevisible; Q3V0K9; MM.
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; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:1990357; C:terminal web; IDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0001951; P:intestinal D-glucose absorption; IGI:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; IGI:UniProtKB.
DR GO; GO:1902896; P:terminal web assembly; IMP:MGI.
DR GO; GO:0060121; P:vestibular receptor cell stereocilium organization; IMP: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; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein 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_0000364188"
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="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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14651"
SQ SEQUENCE 630 AA; 70408 MW; 1F7254CB97780742 CRC64;
MENSTTTISR EELEELQEAF NKIDIDNSGY VSDYELQDLF KEASLPLPGY KVREIVEKIL
VVADNNKDGK ISFEEFVSLM QELKSKDISK TFRKIINKRE GITAIGGTSS ISSEGTQHSY
SEEEKVAFVN WINKALENDA DCSHLLPMNP NDGSLFKSLA DGILLCKMIN LSEPDTIDER
AINKKKLTPF TVSENLNLAL NSASAIGCTV VNIGAQDLKE GKPHLVLGLL WQIIKVGLFA
DIEISRNEAL IALLKDGEDL EELMKLSPEE LLLRWVNYHL TNAGWRTINN FSQDIKDSKA
YFHLLNQIAP KGDRDDGPAV AIDLSGFNEK NDLKRAGFML QEADKLGCRQ FVTPADVVSG
NPKLNLAFVA NLFNTYPCLH KPDNNDIDLN LLEGESKEER TFRNWMNSLG VNPYINHLYS
DLADALVIFQ LYEMIRVPVN WSQVNKPPYP ALGGNMKKIE NCNYAVELGK NEAKFSLVGI
AGQDLNEGNA TLTLALVWQL MRRYTLKVLS DLGEGEKVTD DIIIKWVNQT LKSANKSTSI
SSFKDKSIST SLPVLDLIDA IAPNAVRQEM IKREHLTDED KLNNAKYAIS VARKIGARIY
ALPDDLVEVK PKMVMTVFAC LMGKGLNRLK
