LSP1_HUMAN
ID LSP1_HUMAN Reviewed; 339 AA.
AC P33241; B3KPP1; B3KRR6; E9PBV6; E9PFP3; Q16096; Q53H48; Q6FHM3; Q9BUY8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Lymphocyte-specific protein 1;
DE AltName: Full=47 kDa actin-binding protein;
DE AltName: Full=52 kDa phosphoprotein;
DE Short=pp52;
DE AltName: Full=Lymphocyte-specific antigen WP34;
GN Name=LSP1; Synonyms=WP34;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2295815;
RA Jongstra-Bilen J., Young A.J., Chong R., Jongstra J.;
RT "Human and mouse LSP1 genes code for highly conserved phosphoproteins.";
RL J. Immunol. 144:1104-1110(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lymphocyte;
RX PubMed=2174784; DOI=10.1002/eji.1830201109;
RA Kadiyala R.K., McIntyre B.W., Krensky A.M.;
RT "Molecular cloning and characterization of WP34, a phosphorylated human
RT lymphocyte differentiation and activation antigen.";
RL Eur. J. Immunol. 20:2417-2423(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8274738;
RA Howard T., Li Y., Torres M., Guerrero A., Coates T.;
RT "The 47-kD protein increased in neutrophil actin dysfunction with 47- and
RT 89-kD protein abnormalities is lymphocyte-specific protein.";
RL Blood 83:231-241(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP THR-100.
RC TISSUE=Esophagus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-100.
RC TISSUE=Dermoid cancer;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-100.
RC TISSUE=Lymph;
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 [9]
RP PHOSPHORYLATION AT SER-252 BY MAPKAPK2.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-111; SER-188;
RP SER-189; SER-193 AND SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May play a role in mediating neutrophil activation and
CC chemotaxis. {ECO:0000250}.
CC -!- SUBUNIT: Binds actin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P33241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33241-2; Sequence=VSP_045655;
CC Name=3;
CC IsoId=P33241-3; Sequence=VSP_045983;
CC -!- TISSUE SPECIFICITY: Activated T-lymphocytes.
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 (By similarity). {ECO:0000250}.
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DR EMBL; M33552; AAA59534.1; -; mRNA.
DR EMBL; X55188; CAA38971.1; -; mRNA.
DR EMBL; S67783; AAB29545.1; -; mRNA.
DR EMBL; CR541728; CAG46529.1; -; mRNA.
DR EMBL; CR541754; CAG46554.1; -; mRNA.
DR EMBL; AK056576; BAG51753.1; -; mRNA.
DR EMBL; AK092071; BAG52478.1; -; mRNA.
DR EMBL; AK222733; BAD96453.1; -; mRNA.
DR EMBL; AC051649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001785; AAH01785.1; -; mRNA.
DR CCDS; CCDS31334.1; -. [P33241-1]
DR CCDS; CCDS31335.1; -. [P33241-2]
DR CCDS; CCDS58110.1; -. [P33241-3]
DR PIR; A43542; A43542.
DR RefSeq; NP_001013271.1; NM_001013253.1. [P33241-2]
DR RefSeq; NP_001013272.1; NM_001013254.1. [P33241-2]
DR RefSeq; NP_001013273.1; NM_001013255.1. [P33241-2]
DR RefSeq; NP_001229861.1; NM_001242932.1. [P33241-3]
DR RefSeq; NP_001275934.1; NM_001289005.1. [P33241-2]
DR RefSeq; NP_002330.1; NM_002339.2. [P33241-1]
DR PDB; 3BH8; X-ray; 1.65 A; C=249-258.
DR PDB; 4NO0; X-ray; 2.70 A; C=249-260.
DR PDB; 4NO2; X-ray; 2.00 A; C=249-260.
DR PDBsum; 3BH8; -.
DR PDBsum; 4NO0; -.
DR PDBsum; 4NO2; -.
DR AlphaFoldDB; P33241; -.
DR SMR; P33241; -.
DR BioGRID; 110224; 37.
DR IntAct; P33241; 23.
DR MINT; P33241; -.
DR STRING; 9606.ENSP00000371194; -.
DR GlyGen; P33241; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P33241; -.
DR PhosphoSitePlus; P33241; -.
DR BioMuta; LSP1; -.
DR DMDM; 462553; -.
DR SWISS-2DPAGE; P33241; -.
DR EPD; P33241; -.
DR jPOST; P33241; -.
DR MassIVE; P33241; -.
DR MaxQB; P33241; -.
DR PaxDb; P33241; -.
DR PeptideAtlas; P33241; -.
DR PRIDE; P33241; -.
DR ProteomicsDB; 19304; -.
DR ProteomicsDB; 20148; -.
DR ProteomicsDB; 54904; -. [P33241-1]
DR ABCD; P33241; 1 sequenced antibody.
DR Antibodypedia; 4493; 663 antibodies from 40 providers.
DR DNASU; 4046; -.
DR Ensembl; ENST00000311604.8; ENSP00000308383.4; ENSG00000130592.17. [P33241-1]
DR Ensembl; ENST00000381775.5; ENSP00000371194.1; ENSG00000130592.17. [P33241-3]
DR Ensembl; ENST00000405957.6; ENSP00000383932.2; ENSG00000130592.17. [P33241-2]
DR Ensembl; ENST00000406638.6; ENSP00000384022.2; ENSG00000130592.17. [P33241-2]
DR Ensembl; ENST00000612798.4; ENSP00000484140.1; ENSG00000130592.17. [P33241-2]
DR Ensembl; ENST00000672349.1; ENSP00000500618.1; ENSG00000288199.3. [P33241-2]
DR Ensembl; ENST00000672565.3; ENSP00000500350.1; ENSG00000288199.3. [P33241-1]
DR Ensembl; ENST00000673051.1; ENSP00000500060.1; ENSG00000288199.3. [P33241-2]
DR Ensembl; ENST00000673183.1; ENSP00000500923.1; ENSG00000288199.3. [P33241-3]
DR Ensembl; ENST00000673397.1; ENSP00000500330.1; ENSG00000288199.3. [P33241-2]
DR GeneID; 4046; -.
DR KEGG; hsa:4046; -.
DR MANE-Select; ENST00000311604.8; ENSP00000308383.4; NM_002339.3; NP_002330.1.
DR UCSC; uc001lui.3; human. [P33241-1]
DR CTD; 4046; -.
DR DisGeNET; 4046; -.
DR GeneCards; LSP1; -.
DR HGNC; HGNC:6707; LSP1.
DR HPA; ENSG00000130592; Tissue enhanced (adrenal gland, lymphoid tissue).
DR MIM; 153432; gene.
DR neXtProt; NX_P33241; -.
DR OpenTargets; ENSG00000130592; -.
DR PharmGKB; PA30472; -.
DR VEuPathDB; HostDB:ENSG00000130592; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000153901; -.
DR HOGENOM; CLU_055750_0_0_1; -.
DR InParanoid; P33241; -.
DR OMA; RAPQTRW; -.
DR OrthoDB; 1385709at2759; -.
DR PhylomeDB; P33241; -.
DR TreeFam; TF336257; -.
DR PathwayCommons; P33241; -.
DR SignaLink; P33241; -.
DR SIGNOR; P33241; -.
DR BioGRID-ORCS; 4046; 144 hits in 1071 CRISPR screens.
DR ChiTaRS; LSP1; human.
DR EvolutionaryTrace; P33241; -.
DR GeneWiki; LSP1; -.
DR GenomeRNAi; 4046; -.
DR Pharos; P33241; Tbio.
DR PRO; PR:P33241; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P33241; protein.
DR Bgee; ENSG00000130592; Expressed in granulocyte and 101 other tissues.
DR ExpressionAtlas; P33241; baseline and differential.
DR Genevisible; P33241; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..339
FT /note="Lymphocyte-specific protein 1"
FT /id="PRO_0000084503"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19973"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19973"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 252
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000269|PubMed:17481585,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:24275569"
FT MOD_RES 327
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045655"
FT VAR_SEQ 1..18
FT /note="MAEASSDPGAEEREELLG -> MAPIWSPPGRVSGCHLSSGPAPGSAVGPWL
FT GTPHPSLPLPLAPHKPPPPGLPGSAGQTSLPAQRECVFPGDAAVHQELCGLGFEECLGS
FT IPQAHQCYLTNGPKRRKCSPRRRGRAPAWLCGGSPPCHQGLGHEHPSSGPSTNCSPR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045983"
FT VARIANT 100
FT /note="A -> T (in dbSNP:rs621679)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_011867"
FT VARIANT 108
FT /note="Q -> L (in dbSNP:rs11545725)"
FT /id="VAR_061680"
FT VARIANT 229
FT /note="Q -> K (in dbSNP:rs1803928)"
FT /id="VAR_011868"
FT CONFLICT 15
FT /note="Missing (in Ref. 3; AAB29545)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="S -> T (in Ref. 2; CAA38971)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..101
FT /note="Missing (in Ref. 3; AAB29545)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> D (in Ref. 5; BAG52478)"
FT /evidence="ECO:0000305"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:4NO2"
FT CONFLICT P33241-3:31
FT /note="G -> Q (in Ref. 5; BAG52478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37192 MW; F2A18533500611D9 CRC64;
MAEASSDPGA EEREELLGPT AQWSVEDEEE AVHEQCQHER DRQLQAQDEE GGGHVPERPK
QEMLLSLKPS EAPELDEDEG FGDWSQRPEQ RQQHEGAQGA LDSGEPPQCR SPEGEQEDRP
GLHAYEKEDS DEVHLEELSL SKEGPGPEDT VQDNLGAAGA EEEQEEHQKC QQPRTPSPLV
LEGTIEQSSP PLSPTTKLID RTESLNRSIE KSNSVKKSQP DLPISKIDQW LEQYTQAIET
AGRTPKLARQ ASIELPSMAV ASTKSRWETG EVQAQSAAKT PSCKDIVAGD MSKKSLWEQK
GGSKTSSTIK STPSGKRYKF VATGHGKYEK VLVEGGPAP
