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   02-SEP-2026, entry version 199.
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; DOI=10.4049/jimmunol.141.11.3999;
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; DOI=10.4049/jimmunol.150.1.115;
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,
RC   Spleen, 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_001136071.3. [P19973-1]
DR   RefSeq; NP_001258437.1; NM_001271508.2.
DR   RefSeq; NP_001258439.1; NM_001271510.2. [P19973-1]
DR   RefSeq; NP_062264.1; NM_019391.4. [P19973-2]
DR   AlphaFoldDB; P19973; -.
DR   SMR; P19973; -.
DR   BioGRID; 201211; 5.
DR   FunCoup; P19973; 160.
DR   IntAct; P19973; 2.
DR   MINT; P19973; -.
DR   STRING; 10090.ENSMUSP00000101588; -.
DR   GlyGen; P19973; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P19973; -.
DR   PhosphoSitePlus; P19973; -.
DR   SwissPalm; P19973; -.
DR   CPTAC; non-CPTAC-3471; -.
DR   jPOST; P19973; -.
DR   PaxDb; 10090-ENSMUSP00000101588; -.
DR   PeptideAtlas; P19973; -.
DR   ProteomicsDB; 292121; -. [P19973-1]
DR   ProteomicsDB; 292122; -. [P19973-2]
DR   Pumba; P19973; -.
DR   Antibodypedia; 4493; 669 antibodies from 42 providers.
DR   DNASU; 16985; -.
DR   Ensembl; ENSMUST00000018963.11; ENSMUSP00000018963.5; ENSMUSG00000018819.11. [P19973-1]
DR   Ensembl; ENSMUST00000038946.9; ENSMUSP00000040637.3; ENSMUSG00000018819.11. [P19973-2]
DR   Ensembl; ENSMUST00000105968.8; ENSMUSP00000101588.2; ENSMUSG00000018819.11. [P19973-1]
DR   GeneID; 16985; -.
DR   KEGG; mmu:16985; -.
DR   UCSC; uc009knb.3; mouse. [P19973-1]
DR   UCSC; uc009knf.2; mouse. [P19973-2]
DR   AGR; MGI:96832; -.
DR   CTD; 4046; -.
DR   MGI; MGI:96832; Lsp1.
DR   VEuPathDB; HostDB:ENSMUSG00000018819; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000153901; -.
DR   InParanoid; P19973; -.
DR   OMA; TRIDDKM; -.
DR   OrthoDB; 9947942at2759; -.
DR   PhylomeDB; P19973; -.
DR   BioGRID-ORCS; 16985; 0 hits in 77 CRISPR screens.
DR   PRO; PR:P19973; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P19973; protein.
DR   Bgee; ENSMUSG00000018819; Expressed in granulocyte and 209 other cell types or tissues.
DR   ExpressionAtlas; P19973; baseline and differential.
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; CALDESMON; 1.
DR   PANTHER; PTHR18949:SF1; LYMPHOCYTE-SPECIFIC PROTEIN 1; 1.
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..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..302
FT                   /note="Low complexity"
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
//