PLSL_MOUSE
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 03-AUG-2022, entry version 199.
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, 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: 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; 18.
DR IntAct; Q61233; 4.
DR MINT; Q61233; -.
DR STRING; 10090.ENSMUSP00000116271; -.
DR CarbonylDB; Q61233; -.
DR iPTMnet; Q61233; -.
DR MetOSite; Q61233; -.
DR PhosphoSitePlus; Q61233; -.
DR SwissPalm; Q61233; -.
DR COMPLUYEAST-2DPAGE; 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; Q61233; -.
DR PeptideAtlas; Q61233; -.
DR PRIDE; Q61233; -.
DR ProteomicsDB; 289456; -.
DR Antibodypedia; 9112; 417 antibodies from 34 providers.
DR DNASU; 18826; -.
DR Ensembl; ENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998.
DR Ensembl; ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998.
DR Ensembl; ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
DR GeneID; 18826; -.
DR KEGG; mmu:18826; -.
DR UCSC; uc007uqm.2; mouse.
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; DAEMVRW; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q61233; -.
DR TreeFam; TF300680; -.
DR BioGRID-ORCS; 18826; 2 hits in 72 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 166 other tissues.
DR ExpressionAtlas; Q61233; baseline and differential.
DR Genevisible; Q61233; MM.
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; ISO:MGI.
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; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
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 InterPro; IPR039956; PLS2/3.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR PANTHER; PTHR19961:SF32; PTHR19961:SF32; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 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.
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
