ID CD19_MOUSE Reviewed; 547 AA. AC P25918; Q542B2; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 189. DE RecName: Full=B-lymphocyte antigen CD19; DE AltName: Full=Differentiation antigen CD19; DE AltName: CD_antigen=CD19; DE Flags: Precursor; GN Name=Cd19; 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 [GENOMIC DNA]. RC STRAIN=BALB/cJ; TISSUE=Spleen; RX PubMed=1714482; RA Zhou L.J., Ord D.C., Hughes A.L., Tedder T.F.; RT "Structure and domain organization of the CD19 antigen of human, mouse, and RT guinea pig B lymphocytes. Conservation of the extensive cytoplasmic RT domain."; RL J. Immunol. 147:1424-1432(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Spleen; RX PubMed=1370948; DOI=10.1007/bf00189519; RA Zhou L.J., Ord D.C., Omori S.A., Tedder T.F.; RT "Structure of the genes encoding the CD19 antigen of human and mouse B RT lymphocytes."; RL Immunogenetics 35:102-111(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Spleen; 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-547. RC STRAIN=BALB/cJ; TISSUE=Spleen; RX PubMed=2472450; RA Tedder T.F., Isaacs C.M.; RT "Isolation of cDNAs encoding the CD19 antigen of human and mouse B RT lymphocytes. A new member of the immunoglobulin superfamily."; RL J. Immunol. 143:712-717(1989). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. RX PubMed=1375324; DOI=10.1128/mcb.12.6.2662-2672.1992; RA Kozmik Z., Wang S., Doerfler P., Adams B., Busslinger M.; RT "The promoter of the CD19 gene is a target for the B-cell-specific RT transcription factor BSAP."; RL Mol. Cell. Biol. 12:2662-2672(1992). RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=7542548; DOI=10.1016/1074-7613(95)90157-4; RA Engel P., Zhou L.J., Ord D.C., Sato S., Koller B., Tedder T.F.; RT "Abnormal B lymphocyte development, activation, and differentiation in mice RT that lack or overexpress the CD19 signal transduction molecule."; RL Immunity 3:39-50(1995). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE RP SPECIFICITY. RX PubMed=7543183; DOI=10.1038/376352a0; RA Rickert R.C., Rajewsky K., Roes J.; RT "Impairment of T-cell-dependent B-cell responses and B-1 cell development RT in CD19-deficient mice."; RL Nature 376:352-355(1995). RN [9] RP FUNCTION. RX PubMed=9382888; DOI=10.1084/jem.186.11.1897; RA Buhl A.M., Pleiman C.M., Rickert R.C., Cambier J.C.; RT "Qualitative regulation of B cell antigen receptor signaling by CD19: RT selective requirement for PI3-kinase activation, inositol-1,4,5- RT trisphosphate production and Ca2+ mobilization."; RL J. Exp. Med. 186:1897-1910(1997). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9317126; RA Sato S., Miller A.S., Howard M.C., Tedder T.F.; RT "Regulation of B lymphocyte development and activation by the RT CD19/CD21/CD81/Leu 13 complex requires the cytoplasmic domain of CD19."; RL J. Immunol. 159:3278-3287(1997). RN [11] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=12387743; DOI=10.1016/s1074-7613(02)00426-0; RA Wang Y., Brooks S.R., Li X., Anzelon A.N., Rickert R.C., Carter R.H.; RT "The physiologic role of CD19 cytoplasmic tyrosines."; RL Immunity 17:501-514(2002). RN [12] RP PHOSPHORYLATION AT SER-225. RX PubMed=15378723; DOI=10.1002/rcm.1604; RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.; RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity RT purification and linear ion trap mass spectrometry."; RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-402; TYR-493 AND RP TYR-522, AND TISSUE SPECIFICITY. RX PubMed=20101619; DOI=10.1002/eji.200939848; RA Ishiura N., Nakashima H., Watanabe R., Kuwano Y., Adachi T., Takahashi Y., RA Tsubata T., Okochi H., Tamaki K., Tedder T.F., Fujimoto M.; RT "Differential phosphorylation of functional tyrosines in CD19 modulates B- RT lymphocyte activation."; RL Eur. J. Immunol. 40:1192-1204(2010). CC -!- FUNCTION: Functions as a coreceptor for the B-cell antigen receptor CC complex (BCR) on B-lymphocytes. Decreases the threshold for activation CC of downstream signaling pathways and for triggering B-cell responses to CC antigens (By similarity). Activates signaling pathways that lead to the CC activation of phosphatidylinositol 3-kinase and the mobilization of CC intracellular Ca(2+) stores (PubMed:9382888, PubMed:12387743, CC PubMed:20101619). Is not required for early steps during B cell CC differentiation in the blood marrow (PubMed:7542548, PubMed:7543183, CC PubMed:9317126). Required for normal differentiation of B-1 cells CC (PubMed:7542548, PubMed:7543183, PubMed:12387743). Required for normal CC B cell differentiation and proliferation in response to antigen CC challenges (PubMed:7542548, PubMed:9317126, PubMed:12387743). Required CC for normal levels of serum immunoglobulins, and for production of high- CC affinity antibodies in response to antigen challenge (PubMed:7542548, CC PubMed:7543183, PubMed:12387743). {ECO:0000250|UniProtKB:P15391, CC ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:20101619, CC ECO:0000269|PubMed:7542548, ECO:0000269|PubMed:7543183, CC ECO:0000269|PubMed:9317126, ECO:0000269|PubMed:9382888}. CC -!- SUBUNIT: Interacts with CR2/CD21. Part of a complex composed of CD19, CC CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B-cells. CC Interacts directly with CD81 (via the second extracellular domain); CC this interaction is initiated early during biosynthesis in the ER/pre- CC Golgi compartments and is essential for trafficking and CC compartmentalization of CD19 receptor on the cell surface of when CC phosphorylated on Tyr-346 and/or Tyr-376. Interacts with PLCG2 when CC phosphorylated on Tyr-402. Interacts with LYN. Interacts (when tyrosine CC phosphorylated) with the regulatory p85 subunit of phosphatidylinositol CC 3-kinase (PIK3R1 or PIK3R2). {ECO:0000250|UniProtKB:P15391}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12387743, CC ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7543183}; Single-pass CC type I membrane protein {ECO:0000305}. Membrane raft CC {ECO:0000269|PubMed:20101619}; Single-pass type I membrane protein CC {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Detected on B cells in spleen, bone marrow, thymus CC and lymph nodes (PubMed:12387743, PubMed:7542548, PubMed:20101619). CC Detected on peripheral blood lymphocytes (at protein level) CC (PubMed:7543183). {ECO:0000269|PubMed:12387743, CC ECO:0000269|PubMed:20101619, ECO:0000269|PubMed:7542548, CC ECO:0000269|PubMed:7543183}. CC -!- PTM: Phosphorylated on tyrosine following B-cell activation CC (PubMed:20101619). Phosphorylated on tyrosine residues by LYN (By CC similarity). Tyrosine residues are phosphorylated sequentially after CC activation of the B cell receptor. Phosphorylation of Tyr-522 is CC extremely rapid, followed by phosphorylation at Tyr-402. In contrast, CC phosphorylation of Tyr-493 appears more slowly and is more transient, CC returning rapidly to basal levels (PubMed:20101619). CC {ECO:0000250|UniProtKB:P15391, ECO:0000269|PubMed:20101619}. CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian CC ratio, thrive and are fertile (PubMed:7542548). Mutant mice display CC normal differentiation and expansion of pro-B cells, pre-B cells, CC immature B cells and resting mature B cells in bone marrow CC (PubMed:7542548, PubMed:7543183, PubMed:9317126). Number and surface CC phenotype of conventional B cells in spleen, Peyer's patch and lymph CC nodes appear normal (PubMed:7543183). In contrast, the numbers of B-1 CC cells are decreased to 10-20% of the normal values in the peritoneal CC cavity, together with a severe reduction of serum IgM levels CC (PubMed:7542548, PubMed:7543183, PubMed:12387743). Likewise, mutant CC mice display severely reduced serum IgG1 and IgE levels CC (PubMed:7543183). Mutant mice display severely reduced B cell responses CC to antigens, with a strong decrease in the production of serum CC antibodies after an antigenic challenge, and defective production of CC high-affinity antibodies (PubMed:7543183). CC {ECO:0000269|PubMed:12387743, ECO:0000269|PubMed:7542548, CC ECO:0000269|PubMed:7543183, ECO:0000269|PubMed:9317126}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M62542; AAA37388.1; -; Genomic_DNA. DR EMBL; M62553; AAA37390.1; -; Genomic_DNA. DR EMBL; M62551; AAA37390.1; JOINED; Genomic_DNA. DR EMBL; M62552; AAA37390.1; JOINED; Genomic_DNA. DR EMBL; AK089835; BAC40973.1; -; mRNA. DR EMBL; CH466531; EDL17351.1; -; Genomic_DNA. DR EMBL; M28240; AAA74753.1; -; Genomic_DNA. DR EMBL; M84372; AAA37389.1; -; Genomic_DNA. DR CCDS; CCDS21828.1; -. DR PIR; B45808; B45808. DR RefSeq; NP_033974.2; NM_009844.2. DR RefSeq; XP_006507346.1; XM_006507283.2. DR AlphaFoldDB; P25918; -. DR SMR; P25918; -. DR BioGRID; 198576; 1. DR IntAct; P25918; 3. DR STRING; 10090.ENSMUSP00000145803; -. DR GlyCosmos; P25918; 7 sites, No reported glycans. DR GlyGen; P25918; 7 sites. DR iPTMnet; P25918; -. DR PhosphoSitePlus; P25918; -. DR PaxDb; 10090-ENSMUSP00000032968; -. DR PeptideAtlas; P25918; -. DR ProteomicsDB; 281513; -. DR ABCD; P25918; 8 sequenced antibodies. DR Antibodypedia; 4237; 5787 antibodies from 56 providers. DR DNASU; 12478; -. DR Ensembl; ENSMUST00000206325.2; ENSMUSP00000145803.2; ENSMUSG00000030724.8. DR GeneID; 12478; -. DR KEGG; mmu:12478; -. DR UCSC; uc009jrb.1; mouse. DR AGR; MGI:88319; -. DR CTD; 930; -. DR MGI; MGI:88319; Cd19. DR VEuPathDB; HostDB:ENSMUSG00000030724; -. DR eggNOG; ENOG502STG8; Eukaryota. DR GeneTree; ENSGT00390000014991; -. DR HOGENOM; CLU_038774_0_0_1; -. DR InParanoid; P25918; -. DR OMA; ENMENPE; -. DR OrthoDB; 5319613at2759; -. DR TreeFam; TF338293; -. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-977606; Regulation of Complement cascade. DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR BioGRID-ORCS; 12478; 3 hits in 79 CRISPR screens. DR ChiTaRS; Cd19; mouse. DR PRO; PR:P25918; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P25918; Protein. DR Bgee; ENSMUSG00000030724; Expressed in peripheral lymph node and 45 other cell types or tissues. DR ExpressionAtlas; P25918; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0019724; P:B cell mediated immunity; IMP:UniProtKB. DR GO; GO:0002322; P:B cell proliferation involved in immune response; ISS:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI. DR GO; GO:0001923; P:B-1 B cell differentiation; IMP:UniProtKB. DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:UniProtKB. DR GO; GO:0050864; P:regulation of B cell activation; ISS:UniProtKB. DR GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IMP:UniProtKB. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR042341; CD19. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR PANTHER; PTHR16674; B-LYMPHOCYTE ANTIGEN CD19; 1. DR PANTHER; PTHR16674:SF2; B-LYMPHOCYTE ANTIGEN CD19; 1. DR SMART; SM00409; IG; 2. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; P25918; MM. PE 1: Evidence at protein level; KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity; KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..16 FT PROPEP 17..18 FT /evidence="ECO:0000255" FT /id="PRO_0000014649" FT CHAIN 19..547 FT /note="B-lymphocyte antigen CD19" FT /id="PRO_0000014650" FT TOPO_DOM 19..287 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 288..311 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 312..547 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 20..113 FT /note="Ig-like C2-type 1" FT DOMAIN 171..271 FT /note="Ig-like C2-type 2" FT REGION 330..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..461 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 472..491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 505..547 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 397..413 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..431 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 437..453 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..536 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15378723" FT MOD_RES 346 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P15391" FT MOD_RES 376 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P15391" FT MOD_RES 402 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:20101619" FT MOD_RES 432 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P15391" FT MOD_RES 493 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:20101619, FT ECO:0007744|PubMed:21183079" FT MOD_RES 522 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:20101619" FT CARBOHYD 56 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 125 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 38..259 FT /evidence="ECO:0000250|UniProtKB:P15391" FT DISULFID 97..197 FT /evidence="ECO:0000250|UniProtKB:P15391" FT DISULFID 134..169 FT /evidence="ECO:0000250|UniProtKB:P15391" FT CONFLICT 207 FT /note="G -> A (in Ref. 2; AAA37390)" FT /evidence="ECO:0000305" SQ SEQUENCE 547 AA; 60149 MW; DDC34A3E23410C8D CRC64; MPSPLPVSFL LFLTLVGGRP QKSLLVEVEE GGNVVLPCLP DSSPVSSEKL AWYRGNQSTP FLELSPGSPG LGLHVGSLGI LLVIVNVSDH MGGFYLCQKR PPFKDIWQPA WTVNVEDSGE MFRWNASDVR DLDCDLRNRS SGSHRSTSGS QLYVWAKDHP KVWGTKPVCA PRGSSLNQSL INQDLTVAPG STLWLSCGVP PVPVAKGSIS WTHVHPRRPN VSLLSLSLGG EHPVREMWVW GSLLLLPQAT ALDEGTYYCL RGNLTIERHV KVIARSAVWL WLLRTGGWIV PVVTLVYVIF CMVSLVAFLY CQRAFILRRK RKRMTDPARR FFKVTPPSGN GTQNQYGNVL SLPTSTSGQA HAQRWAAGLG SVPGSYGNPR IQVQDTGAQS HETGLEEEGE AYEEPDSEEG SEFYENDSNL GQDQVSQDGS GYENPEDEPM GPEEEDSFSN AESYENADEE LAQPVGRMMD FLSPHGSAWD PSREASSLGS QSYEDMRGIL YAAPQLHSIQ SGPSHEEDAD SYENMDKSDD LEPAWEGEGH MGTWGTT //