LSP1_MOUSE
ID LSP1_MOUSE Reviewed; 330 AA.
AC P19973; A2A6J5; A2A6J6; P97339; Q04950; Q62022; Q62023; Q62024; Q8CD28;
AC Q99L65;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Lymphocyte-specific protein 1;
DE AltName: Full=52 kDa phosphoprotein;
DE Short=pp52;
DE AltName: Full=Lymphocyte-specific antigen WP34;
DE AltName: Full=S37 protein;
GN Name=Lsp1; Synonyms=Pp52, S37, Wp34;
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 (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=3263441;
RA Jongstra J., Tidmarsh G.F., Jongstra-Bilen J., Davis M.M.;
RT "A new lymphocyte-specific gene which encodes a putative Ca2+-binding
RT protein is not expressed in transformed T lymphocyte lines.";
RL J. Immunol. 141:3999-4004(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8417117;
RA Gimble J.M., Dorheim M.-A., Youkhana K., Hudson J., Nead M., Gilly M.,
RA Wood W.J. Jr., Hermanson G.G., Kuehl M., Wall R., Kincade P.W.;
RT "Alternatively spliced pp52 mRNA in nonlymphoid stromal cells.";
RL J. Immunol. 150:115-121(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=7935501; DOI=10.1016/0161-5890(94)90026-4;
RA Jongstra J., Ittel M.E., Iscove N.N., Brady G.;
RT "The LSP1 gene is expressed in cultured normal and transformed mouse
RT macrophages.";
RL Mol. Immunol. 31:1125-1131(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
RC STRAIN=ICR; TISSUE=Thymus;
RX PubMed=7775393; DOI=10.1093/oxfordjournals.jbchem.a124714;
RA Matsumoto N., Kojima S., Osawa T., Toyoshima S.;
RT "Protein kinase C phosphorylates p50 LSP1 and induces translocation of p50
RT LSP1 in T lymphocytes.";
RL J. Biochem. 117:222-229(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC STRAIN=ICR; TISSUE=Thymus;
RX PubMed=8537319; DOI=10.1093/oxfordjournals.jbchem.a124885;
RA Matsumoto N., Kita K., Kojima S., Yamamoto K., Irimura T., Miyagi M.,
RA Tsunasawa S., Toyoshima S.;
RT "Lymphocyte isoforms of mouse p50 LSP1, which are phosphorylated in
RT mitogen-activated T cells, are formed through alternative splicing and
RT phosphorylation.";
RL J. Biochem. 118:237-243(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; 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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-124 (ISOFORMS 1 AND 2), AND
RP ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Leukocyte, and Stromal cell;
RX PubMed=8838798; DOI=10.1006/geno.1996.0129;
RA Thompson A.A., Omori S.A., Gilly M.J., May W., Gordon M.S., Wood W.J. Jr.,
RA Miyoshi E., Malone C.S., Gimble J., Denny C.T., Wall R.;
RT "Alternatively spliced exons encode the tissue-specific 5' termini of
RT leukocyte pp52 and stromal cell S37 mRNA isoforms.";
RL Genomics 32:352-357(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127 (ISOFORM 2).
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 [10]
RP PROTEIN SEQUENCE OF 55-81; 131-144; 211-229; 238-255 AND 311-330, AND
RP PHOSPHORYLATION.
RC TISSUE=T-cell;
RX PubMed=8340356; DOI=10.1093/oxfordjournals.jbchem.a124094;
RA Matsumoto N., Toyoshima S., Osawa T.;
RT "Characterization of the 50 kDa protein phosphorylated in concanavalin A-
RT stimulated mouse T cells.";
RL J. Biochem. 113:630-636(1993).
RN [11]
RP PHOSPHORYLATION AT SER-243 BY MAPKAPK2, MUTAGENESIS OF SER-195 AND SER-243,
RP AND FUNCTION.
RX PubMed=17481585; DOI=10.1016/j.bbrc.2007.04.104;
RA Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K., Madri J.A.;
RT "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil
RT polarization.";
RL Biochem. Biophys. Res. Commun. 358:170-175(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166; SER-168; SER-180;
RP SER-184 AND SER-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, 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).
CC -!- FUNCTION: May play a role in mediating neutrophil activation and
CC chemotaxis. {ECO:0000269|PubMed:17481585}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19973-2; Sequence=VSP_004313;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in normal mouse B and T-
CC lymphocytes and in transformed B-cells but not (or in smaller amounts)
CC in nine T-lymphoma lines tested. Isoform 2 is expressed in non-lymphoid
CC cell lines (myocytes, stromal cells, fibroblasts).
CC -!- PTM: Phosphorylated by casein kinase II, protein kinase C and MAPKAPK2.
CC Phosphorylation by PKC induces translocation from membrane to
CC cytoplasm. Phosphorylation by MAPKAPK2 may regulate neutrophil
CC chemotaxis. {ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:7775393,
CC ECO:0000269|PubMed:8340356}.
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DR EMBL; M90316; AAA65108.1; -; mRNA.
DR EMBL; S74179; AAB32257.1; -; mRNA.
DR EMBL; M89956; AAB48537.1; -; mRNA.
DR EMBL; D49691; BAA08541.1; -; mRNA.
DR EMBL; AL603651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003796; AAH03796.1; -; mRNA.
DR EMBL; U30942; AAB37542.1; -; Genomic_DNA.
DR EMBL; U30939; AAB37542.1; JOINED; Genomic_DNA.
DR EMBL; U30941; AAB37542.1; JOINED; Genomic_DNA.
DR EMBL; U30942; AAB37543.1; -; Genomic_DNA.
DR EMBL; U30940; AAB37543.1; JOINED; Genomic_DNA.
DR EMBL; U30941; AAB37543.1; JOINED; Genomic_DNA.
DR EMBL; AK031587; BAC27463.1; -; mRNA.
DR CCDS; CCDS40193.1; -. [P19973-2]
DR CCDS; CCDS52450.1; -. [P19973-1]
DR PIR; A30533; A30533.
DR PIR; A46521; A46521.
DR RefSeq; NP_001129543.1; NM_001136071.2. [P19973-1]
DR RefSeq; NP_001258437.1; NM_001271508.1.
DR RefSeq; NP_001258439.1; NM_001271510.1. [P19973-1]
DR RefSeq; NP_062264.1; NM_019391.3. [P19973-2]
DR AlphaFoldDB; P19973; -.
DR SMR; P19973; -.
DR BioGRID; 201211; 4.
DR IntAct; P19973; 2.
DR MINT; P19973; -.
DR STRING; 10090.ENSMUSP00000018963; -.
DR iPTMnet; P19973; -.
DR PhosphoSitePlus; P19973; -.
DR CPTAC; non-CPTAC-3471; -.
DR EPD; P19973; -.
DR jPOST; P19973; -.
DR MaxQB; P19973; -.
DR PaxDb; P19973; -.
DR PeptideAtlas; P19973; -.
DR PRIDE; P19973; -.
DR ProteomicsDB; 292121; -. [P19973-1]
DR ProteomicsDB; 292122; -. [P19973-2]
DR Antibodypedia; 4493; 663 antibodies from 40 providers.
DR DNASU; 16985; -.
DR Ensembl; ENSMUST00000018963; ENSMUSP00000018963; ENSMUSG00000018819. [P19973-1]
DR Ensembl; ENSMUST00000038946; ENSMUSP00000040637; ENSMUSG00000018819. [P19973-2]
DR Ensembl; ENSMUST00000105968; ENSMUSP00000101588; ENSMUSG00000018819. [P19973-1]
DR GeneID; 16985; -.
DR KEGG; mmu:16985; -.
DR UCSC; uc009knb.3; mouse. [P19973-1]
DR UCSC; uc009knf.2; mouse. [P19973-2]
DR CTD; 4046; -.
DR MGI; MGI:96832; Lsp1.
DR VEuPathDB; HostDB:ENSMUSG00000018819; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000153901; -.
DR InParanoid; P19973; -.
DR OMA; RAPQTRW; -.
DR OrthoDB; 1385709at2759; -.
DR PhylomeDB; P19973; -.
DR TreeFam; TF336257; -.
DR BioGRID-ORCS; 16985; 0 hits in 72 CRISPR screens.
DR PRO; PR:P19973; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P19973; protein.
DR Bgee; ENSMUSG00000018819; Expressed in granulocyte and 205 other tissues.
DR ExpressionAtlas; P19973; baseline and differential.
DR Genevisible; P19973; MM.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:MGI.
DR GO; GO:0006915; P:apoptotic process; TAS:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR006018; Caldesmon_LSP.
DR InterPro; IPR002211; Lymphspecific.
DR PANTHER; PTHR18949; PTHR18949; 2.
DR Pfam; PF02029; Caldesmon; 1.
DR PRINTS; PR01083; LYMPHSPCIFIC.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..330
FT /note="Lymphocyte-specific protein 1"
FT /id="PRO_0000084504"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33241"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000269|PubMed:17481585,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P33241"
FT VAR_SEQ 1..23
FT /note="MAEAAIDPRCEEQEELHAEDSEG -> MNGPALLRRNASKRGLEKLLR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8417117,
FT ECO:0000303|PubMed:8838798"
FT /id="VSP_004313"
FT MUTAGEN 195
FT /note="S->A: No effect on phosphorylation by PKC, PKA,
FT MAPKAPK2 and CaMK2."
FT /evidence="ECO:0000269|PubMed:17481585"
FT MUTAGEN 243
FT /note="S->A: Complete loss of phosphorylation by MAPKAPK2,
FT partial loss of phosphorylation by PKA, no effect on
FT phosphorylation by PKC and CaMK2."
FT /evidence="ECO:0000269|PubMed:17481585"
FT MUTAGEN 243
FT /note="S->E: Complete loss of phosphorylation by MAPKAPK2,
FT partial loss of phosphorylation by PKA, no effect on
FT phosphorylation by PKC and CaMK2."
FT /evidence="ECO:0000269|PubMed:17481585"
FT CONFLICT 125..127
FT /note="SSH -> RQV (in Ref. 9; BAC27463)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="AE -> PK (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..163
FT /note="Missing (in Ref. 7; AAH03796)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="I -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="S -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> T (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT P19973-2:16
FT /note="L -> Q (in Ref. 8; AAB37543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36714 MW; CCC27150F02859FB CRC64;
MAEAAIDPRC EEQEELHAED SEGLTTQWRE EDEEEAAREQ RQRERERQLQ DQDKDKEDDG
GHSLEQPGQQ TLISLKSSEL DEDEGFGDWS QKPEPRQQFW GNEGTAEGTE PSQSERPEEK
QTEESSHQAK VHLEESNLSY REPDPEDAVG GSGEAEEHLI RHQVRTPSPL ALEDTVELSS
PPLSPTTKLA DRTESLNRSI KKSNSVKKSQ PTLPISTIDE RLQQYTQATE SSGRTPKLSR
QPSIELPSMA VASTKTLWET GEVQSQSASK TPSCQDIVAG DMSKKSLWEQ KGGSKISSTI
KSTPSGKRYK FVATGHGKYE KVLVDEGSAP
