LASP1_MOUSE
ID LASP1_MOUSE Reviewed; 263 AA.
AC Q61792; Q62416;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=LIM and SH3 domain protein 1;
DE Short=LASP-1;
DE AltName: Full=Metastatic lymph node gene 50 protein;
DE Short=MLN 50;
GN Name=Lasp1; Synonyms=Mln50;
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 [MRNA].
RX PubMed=9511759; DOI=10.1016/s0378-1119(97)00622-7;
RA Schreiber V., Masson R., Linares J.L., Mattei M.-G., Tomasetto C.,
RA Rio M.-C.;
RT "Chromosomal assignment and expression pattern of the murine Lasp-1 gene.";
RL Gene 207:171-175(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 59-263.
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [5]
RP PHOSPHORYLATION AT THR-156.
RX PubMed=15465019; DOI=10.1016/j.bbrc.2004.08.235;
RA Keicher C., Gambaryan S., Schulze E., Marcus K., Meyer H.E., Butt E.;
RT "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-
RT dependent protein kinase.";
RL Biochem. Biophys. Res. Commun. 324:308-316(2004).
RN [6]
RP INTERACTION WITH ANKRD54.
RX PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA Samuels A.L., Klinken S.P., Ingley E.;
RT "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT influences erythropoietin-induced differentiation.";
RL Blood 113:3845-3856(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Plays an important role in the regulation of dynamic actin-
CC based, cytoskeletal activities. Agonist-dependent changes in LASP1
CC phosphorylation may also serve to regulate actin-associated ion
CC transport activities, not only in the parietal cell but also in certain
CC other F-actin-rich secretory epithelial cell types (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with KBTBD10 (By
CC similarity). Interacts with ANKRD54. {ECO:0000250,
CC ECO:0000269|PubMed:19064729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich
CC cortical cytoskeleton. {ECO:0000250}.
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DR EMBL; X96973; CAA65659.1; -; mRNA.
DR EMBL; AK078445; BAC37278.1; -; mRNA.
DR EMBL; BC010840; AAH10840.1; -; mRNA.
DR EMBL; U58882; AAC52639.1; -; mRNA.
DR CCDS; CCDS25332.1; -.
DR RefSeq; NP_034818.1; NM_010688.4.
DR RefSeq; XP_006532404.1; XM_006532341.1.
DR AlphaFoldDB; Q61792; -.
DR SMR; Q61792; -.
DR BioGRID; 201111; 14.
DR ELM; Q61792; -.
DR IntAct; Q61792; 4.
DR MINT; Q61792; -.
DR STRING; 10090.ENSMUSP00000042123; -.
DR iPTMnet; Q61792; -.
DR PhosphoSitePlus; Q61792; -.
DR SwissPalm; Q61792; -.
DR EPD; Q61792; -.
DR jPOST; Q61792; -.
DR MaxQB; Q61792; -.
DR PaxDb; Q61792; -.
DR PRIDE; Q61792; -.
DR ProteomicsDB; 264842; -.
DR Antibodypedia; 1894; 408 antibodies from 38 providers.
DR DNASU; 16796; -.
DR Ensembl; ENSMUST00000043843; ENSMUSP00000042123; ENSMUSG00000038366.
DR GeneID; 16796; -.
DR KEGG; mmu:16796; -.
DR UCSC; uc007lew.1; mouse.
DR CTD; 3927; -.
DR MGI; MGI:109656; Lasp1.
DR VEuPathDB; HostDB:ENSMUSG00000038366; -.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000154775; -.
DR HOGENOM; CLU_026811_0_1_1; -.
DR InParanoid; Q61792; -.
DR OMA; QIEYVEY; -.
DR OrthoDB; 1549538at2759; -.
DR PhylomeDB; Q61792; -.
DR TreeFam; TF319104; -.
DR BioGRID-ORCS; 16796; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Lasp1; mouse.
DR PRO; PR:Q61792; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61792; protein.
DR Bgee; ENSMUSG00000038366; Expressed in pigmented layer of retina and 255 other tissues.
DR ExpressionAtlas; Q61792; baseline and differential.
DR Genevisible; Q61792; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR CDD; cd11934; SH3_Lasp1_C; 1.
DR InterPro; IPR035630; Lasp1_SH3.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00880; Nebulin; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00227; NEBU; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51216; NEBULIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Ion transport;
KW LIM domain; Metal-binding; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Transport; Zinc.
FT CHAIN 1..263
FT /note="LIM and SH3 domain protein 1"
FT /id="PRO_0000075762"
FT DOMAIN 5..56
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 61..95
FT /note="Nebulin 1"
FT REPEAT 97..131
FT /note="Nebulin 2"
FT DOMAIN 204..263
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 123..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 75
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 156
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:15465019"
SQ SEQUENCE 263 AA; 29994 MW; A6CA2FC2E451433E CRC64;
MNPNCARCGK IVYPTEKVNC LDKYWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGVE PERREAQDSS SYRRPTEQQQ PQPHHIPTSA PVYQQPQQQQ
MTSSYGGYKE PAAPVSIQRS APGGGGKRYR AVYDYSAADE DEVSFQDGDT IVNVQQIDDG
WMYGTVERTG DTGMLPANYV EAI
