ID PLSL_MOUSE Reviewed; 627 AA. AC Q61233; Q3UE24; Q8R1X3; Q9CV77; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JAN-2024, entry version 207. DE RecName: Full=Plastin-2; DE AltName: Full=65 kDa macrophage protein; DE AltName: Full=L-plastin; DE AltName: Full=Lymphocyte cytosolic protein 1; DE Short=LCP-1; DE AltName: Full=pp65; GN Name=Lcp1; Synonyms=Pls2; 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], PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION RP AT SER-5 AND SER-7. RX PubMed=7897227; RA Shinomiya H., Hagi A., Fukuzumi M., Mizobuchi M., Hirata H., Utsumi S.; RT "Complete primary structure and phosphorylation site of the 65-kDa RT macrophage protein phosphorylated by stimulation with bacterial RT lipopolysaccharide."; RL J. Immunol. 154:3471-3478(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Thymus, and Tongue; 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 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 PROTEIN SEQUENCE OF 234-244; 264-272 AND 344-357, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION. RX PubMed=8060349; DOI=10.1006/bbrc.1994.2120; RA Shinomiya H., Hirata H., Saito S., Yagisawa H., Nakano M.; RT "Identification of the 65-kDa phosphoprotein in murine macrophages as a RT novel protein: homology with human L-plastin."; RL Biochem. Biophys. Res. Commun. 202:1631-1638(1994). RN [6] RP SUBCELLULAR LOCATION, AND INTERACTION WITH AIF1. RX PubMed=14756805; DOI=10.1046/j.1471-4159.2003.02213.x; RA Ohsawa K., Imai Y., Sasaki Y., Kohsaka S.; RT "Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances RT its actin-bundling activity."; RL J. Neurochem. 88:844-856(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-30 AND SER-257, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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: Actin-binding protein. Plays a role in the activation of T- CC cells in response to costimulation through TCR/CD3 and CD2 or CD28. CC Modulates the cell surface expression of IL2RA/CD25 and CD69. CC {ECO:0000250|UniProtKB:P13796}. CC -!- SUBUNIT: Monomer (By similarity). Interacts with AIF1 CC (PubMed:14756805). Interacts with actin (By similarity). CC {ECO:0000250|UniProtKB:P13796, ECO:0000269|PubMed:14756805}. CC -!- INTERACTION: CC Q61233; P47811: Mapk14; NbExp=5; IntAct=EBI-309345, EBI-298727; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:14756805}. Cell projection {ECO:0000250}. Cell CC junction {ECO:0000250}. Cell projection, ruffle membrane CC {ECO:0000269|PubMed:14756805}; Peripheral membrane protein CC {ECO:0000269|PubMed:14756805}; Cytoplasmic side CC {ECO:0000269|PubMed:14756805}. Note=Relocalizes to the immunological CC synapse between peripheral blood T-lymphocytes and antibody-presenting CC cells in response to costimulation through TCR/CD3 and CD2 or CD28. CC Relocalizes to actin-rich cell projections upon serine phosphorylation CC (By similarity). Associated with the actin cytoskeleton at membrane CC ruffles. {ECO:0000250|UniProtKB:P13796}. CC -!- PTM: Phosphorylated on a serine residue in response to costimulation CC through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes CC association with the actin cytoskeleton and targeting to peripheral CC cell projections (By similarity). {ECO:0000250}. 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; D37837; BAA07085.1; -; mRNA. DR EMBL; AK009211; BAB26141.1; -; mRNA. DR EMBL; AK030806; BAE20456.1; -; mRNA. DR EMBL; AK030987; BAC27205.1; -; mRNA. DR EMBL; AK030996; BAC27208.1; -; mRNA. DR EMBL; AK088202; BAC40207.1; -; mRNA. DR EMBL; AK149790; BAE29087.1; -; mRNA. DR EMBL; AK151155; BAE30161.1; -; mRNA. DR EMBL; AK152891; BAE31574.1; -; mRNA. DR EMBL; AK153082; BAE31707.1; -; mRNA. DR EMBL; AK153206; BAE31806.1; -; mRNA. DR EMBL; AK169728; BAE41332.1; -; mRNA. DR EMBL; AK169833; BAE41398.1; -; mRNA. DR EMBL; BC022943; AAH22943.1; -; mRNA. DR CCDS; CCDS27276.1; -. DR PIR; I49445; I49445. DR RefSeq; NP_001234913.1; NM_001247984.1. DR RefSeq; NP_032905.2; NM_008879.4. DR RefSeq; XP_006518762.1; XM_006518699.1. DR RefSeq; XP_006518764.1; XM_006518701.3. DR RefSeq; XP_006518765.1; XM_006518702.3. DR RefSeq; XP_006518766.1; XM_006518703.3. DR RefSeq; XP_006518767.1; XM_006518704.1. DR RefSeq; XP_017171409.1; XM_017315920.1. DR AlphaFoldDB; Q61233; -. DR SMR; Q61233; -. DR BioGRID; 202256; 19. DR IntAct; Q61233; 4. DR MINT; Q61233; -. DR STRING; 10090.ENSMUSP00000116271; -. DR CarbonylDB; Q61233; -. DR GlyGen; Q61233; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q61233; -. DR MetOSite; Q61233; -. DR PhosphoSitePlus; Q61233; -. DR SwissPalm; Q61233; -. DR REPRODUCTION-2DPAGE; Q61233; -. DR CPTAC; non-CPTAC-3599; -. DR CPTAC; non-CPTAC-3733; -. DR EPD; Q61233; -. DR jPOST; Q61233; -. DR MaxQB; Q61233; -. DR PaxDb; 10090-ENSMUSP00000116271; -. DR PeptideAtlas; Q61233; -. DR ProteomicsDB; 289456; -. DR Antibodypedia; 9112; 460 antibodies from 34 providers. DR DNASU; 18826; -. DR Ensembl; ENSMUST00000124499.8; ENSMUSP00000121201.2; ENSMUSG00000021998.17. DR Ensembl; ENSMUST00000131802.2; ENSMUSP00000117137.2; ENSMUSG00000021998.17. DR Ensembl; ENSMUST00000145303.8; ENSMUSP00000116271.2; ENSMUSG00000021998.17. DR GeneID; 18826; -. DR KEGG; mmu:18826; -. DR UCSC; uc007uqm.2; mouse. DR AGR; MGI:104808; -. DR CTD; 3936; -. DR MGI; MGI:104808; Lcp1. DR VEuPathDB; HostDB:ENSMUSG00000021998; -. DR eggNOG; KOG0046; Eukaryota. DR GeneTree; ENSGT00950000183097; -. DR HOGENOM; CLU_015284_2_0_1; -. DR InParanoid; Q61233; -. DR OMA; WQLMRKN; -. DR OrthoDB; 5475188at2759; -. DR PhylomeDB; Q61233; -. DR TreeFam; TF300680; -. DR BioGRID-ORCS; 18826; 3 hits in 77 CRISPR screens. DR ChiTaRS; Lcp1; mouse. DR PRO; PR:Q61233; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; Q61233; Protein. DR Bgee; ENSMUSG00000021998; Expressed in granulocyte and 170 other cell types or tissues. DR ExpressionAtlas; Q61233; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI. DR GO; GO:0005884; C:actin filament; IDA:MGI. DR GO; GO:0032432; C:actin filament bundle; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030175; C:filopodium; ISO:MGI. DR GO; GO:0005925; C:focal adhesion; ISO:MGI. DR GO; GO:0097386; C:glial cell projection; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0001891; C:phagocytic cup; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0002102; C:podosome; ISO:MGI. DR GO; GO:0001726; C:ruffle; IDA:MGI. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001725; C:stress fiber; IEA:Ensembl. DR GO; GO:0051015; F:actin filament binding; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051020; F:GTPase binding; ISO:MGI. DR GO; GO:0005178; F:integrin binding; ISO:MGI. DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI. DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0016477; P:cell migration; ISO:MGI. DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI. DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:MGI. DR GO; GO:0010737; P:protein kinase A signaling; ISO:MGI. DR GO; GO:0033157; P:regulation of intracellular protein transport; ISS:UniProtKB. DR GO; GO:0009611; P:response to wounding; ISO:MGI. DR GO; GO:0002286; P:T cell activation involved in immune response; ISS:UniProtKB. DR CDD; cd21327; CH_PLS2_rpt2; 1. DR CDD; cd21333; CH_PLS2_rpt4; 1. DR CDD; cd21292; CH_PLS_rpt1; 1. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 4. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR039959; Fimbrin/Plastin. DR PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1. DR PANTHER; PTHR19961:SF35; PLASTIN-2; 1. DR Pfam; PF00307; CH; 4. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00033; CH; 4. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00019; ACTININ_1; 2. DR PROSITE; PS00020; ACTININ_2; 2. DR PROSITE; PS50021; CH; 4. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. DR COMPLUYEAST-2DPAGE; Q61233; -. DR Genevisible; Q61233; MM. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Calcium; Cell junction; Cell membrane; KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P13796" FT CHAIN 2..627 FT /note="Plastin-2" FT /id="PRO_0000073744" FT DOMAIN 9..44 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 49..84 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 120..236 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 264..375 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 394..503 FT /note="Calponin-homology (CH) 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 515..624 FT /note="Calponin-homology (CH) 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REGION 106..379 FT /note="Actin-binding 1" FT REGION 380..624 FT /note="Actin-binding 2" FT BINDING 22 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 24 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 68 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 73 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:7897227, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:7897227" FT MOD_RES 28 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 76 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 88 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 124 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 291 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 294 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 297 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 472 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 474 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 542 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT MOD_RES 579 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13796" FT CONFLICT 26 FT /note="N -> K (in Ref. 2; BAC27208)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="S -> T (in Ref. 1; BAA07085)" FT /evidence="ECO:0000305" FT CONFLICT 292 FT /note="D -> H (in Ref. 1; BAA07085)" FT /evidence="ECO:0000305" FT CONFLICT 367..369 FT /note="IAN -> ANL (in Ref. 1; BAA07085)" FT /evidence="ECO:0000305" FT CONFLICT 479 FT /note="A -> G (in Ref. 1; BAA07085)" FT /evidence="ECO:0000305" FT CONFLICT 527 FT /note="T -> M (in Ref. 1; BAA07085)" FT /evidence="ECO:0000305" FT CONFLICT 558 FT /note="A -> S (in Ref. 2; BAB26141)" FT /evidence="ECO:0000305" SQ SEQUENCE 627 AA; 70149 MW; F0A1E6CA1C11A8E6 CRC64; MARGSVSDEE MMELREAFAK VDTDGNGYIS CNELNDLFKA ACLPLPGYRV REITENLMAT GDLDQDGKIS FDEFIKVFHG LKSTEVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT DDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCTKITNFS TDIKDSKAYY HLLEQVAPKG DEEGIPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP KLNLAFIANL FNKYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVDLGKNQ AKFSLVGIAG QDLNEGNRTL TLALVWQLMR RYTLNILEDI GGGQKVNDDI IVNWVNTTLK EAQKSSSIAS FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLDDEEKL NNAKYAISMA RKIGARVYAL PEDLVEVNPK MVMTVFACLM GKGMKRV //