HS150_YEAST
ID HS150_YEAST Reviewed; 413 AA.
AC P32478; B6RI02; B6RI03; B6RI04; D6VW28; P47000; Q03179; Q6VXX4; Q86ZT2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cell wall mannoprotein HSP150;
DE AltName: Full=150 kDa heat shock glycoprotein;
DE AltName: Full=Covalently-linked cell wall protein 7;
DE AltName: Full=Protein with internal repeats 2;
DE Flags: Precursor;
GN Name=HSP150; Synonyms=CCW7, ORE1, PIR2; OrderedLocusNames=YJL159W;
GN ORFNames=J0558;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 19-39; 73-94; 114-132;
RP 243-261; 346-370 AND 390-412.
RX PubMed=1570286; DOI=10.1073/pnas.89.9.3671;
RA Russo P., Kalkkinen N., Sareneva H., Paakkola J., Makarow M.;
RT "A heat shock gene from Saccharomyces cerevisiae encoding a secretory
RT glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3671-3675(1992).
RN [2]
RP ERRATUM OF PUBMED:1570286, AND SEQUENCE REVISION.
RX PubMed=1528903; DOI=10.1073/pnas.89.18.8857;
RA Russo P., Kalkkinen N., Sareneva H., Paakkola J., Makarow M.;
RL Proc. Natl. Acad. Sci. U.S.A. 89:8857-8857(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RAY-3AD;
RX PubMed=8322511; DOI=10.1002/yea.320090504;
RA Toh-e A., Yasunaga S., Nisogi H., Tanaka K., Oguchi T., Matsui Y.;
RT "Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem
RT repeats, are related to each other, and PIR1 and PIR2 are required for
RT tolerance to heat shock.";
RL Yeast 9:481-494(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP PROTEIN SEQUENCE OF 19-29 AND 73-87, CLEAVAGE BY KEX2, GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9301021;
RX DOI=10.1002/(sici)1097-0061(19970930)13:12<1145::aid-yea163>3.0.co;2-y;
RA Mrsa V., Seidl T., Gentzsch M., Tanner W.;
RT "Specific labelling of cell wall proteins by biotinylation. Identification
RT of four covalently linked O-mannosylated proteins of Saccharomyces
RT cerevisiae.";
RL Yeast 13:1145-1154(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-393, PROTEIN SEQUENCE OF 73-84, AND
RP VARIANTS SER-96; 116-ALA--THR-163 DEL ILE-175; ILE-199; 226-ALA--THR-244
RP DEL AND SER-297.
RC STRAIN=B1, TD04/1a, and TD04/1b;
RX PubMed=18657192; DOI=10.1111/j.1567-1364.2008.00413.x;
RA Kovacs M., Stuparevic I., Mrsa V., Maraz A.;
RT "Characterization of Ccw7p cell wall proteins and the encoding genes of
RT Saccharomyces cerevisiae wine yeast strains: relevance for flor
RT formation.";
RL FEMS Yeast Res. 8:1115-1126(2008).
RN [8]
RP PROTEIN SEQUENCE OF 73-82.
RX PubMed=10234784;
RX DOI=10.1002/(sici)1097-0061(199904)15:6<459::aid-yea387>3.0.co;2-l;
RA Pardo M., Monteoliva L., Pla J., Sanchez M., Gil C., Nombela C.;
RT "Two-dimensional analysis of proteins secreted by Saccharomyces cerevisiae
RT regenerating protoplasts: a novel approach to study the cell wall.";
RL Yeast 15:459-472(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-366.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=14734023; DOI=10.1016/s1567-1356(03)00172-7;
RA Marinangeli P., Angelozzi D., Ciani M., Clementi F., Mannazzu I.;
RT "Minisatellites in Saccharomyces cerevisiae genes encoding cell wall
RT proteins: a new way towards wine strain characterisation.";
RL FEMS Yeast Res. 4:427-435(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 267-413.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=11223941;
RX DOI=10.1002/1097-0061(20010315)18:4<323::aid-yea671>3.0.co;2-c;
RA Moukadiri I., Zueco J.;
RT "YJL159w does encode Pir2/Hsp150.";
RL Yeast 18:323-324(2001).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-406.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [12]
RP PROTEIN SEQUENCE OF 318-327 AND 338-345.
RX PubMed=11079560;
RX DOI=10.1002/1522-2683(20001001)21:16<3396::aid-elps3396>3.0.co;2-j;
RA Pardo M., Ward M., Bains S., Molina M., Blackstock W., Gil C., Nombela C.;
RT "A proteomic approach for the study of Saccharomyces cerevisiae cell wall
RT biogenesis.";
RL Electrophoresis 21:3396-3410(2000).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9192695; DOI=10.1073/pnas.94.13.7082;
RA Yun D.-J., Zhao Y., Pardo J.M., Narasimhan M.L., Damsz B., Lee H.,
RA Abad L.R., D'Urzo M.P., Hasegawa P.M., Bressan R.A.;
RT "Stress proteins on the yeast cell surface determine resistance to osmotin,
RT a plant antifungal protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7082-7087(1997).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10209754; DOI=10.1046/j.1365-2958.1999.01320.x;
RA Kapteyn J.C., Van Egmond P., Sievi E., Van Den Ende H., Makarow M.,
RA Klis F.M.;
RT "The contribution of the O-glycosylated protein Pir2p/Hsp150 to the
RT construction of the yeast cell wall in wild-type cells and beta 1,6-glucan-
RT deficient mutants.";
RL Mol. Microbiol. 31:1835-1844(1999).
RN [15]
RP INDUCTION.
RX PubMed=10594829; DOI=10.1046/j.1365-2958.1999.01667.x;
RA Jung U.S., Levin D.E.;
RT "Genome-wide analysis of gene expression regulated by the yeast cell wall
RT integrity signalling pathway.";
RL Mol. Microbiol. 34:1049-1057(1999).
RN [16]
RP FUNCTION.
RX PubMed=10407261;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<813::aid-yea421>3.0.co;2-y;
RA Mrsa V., Tanner W.;
RT "Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p
RT (members of the Pir protein family) in stability of the Saccharomyces
RT cerevisiae cell wall.";
RL Yeast 15:813-820(1999).
RN [17]
RP INDUCTION.
RX PubMed=11309124; DOI=10.1046/j.1365-2958.2001.02388.x;
RA Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.;
RT "Overlapping and distinct roles of the duplicated yeast transcription
RT factors Ace2p and Swi5p.";
RL Mol. Microbiol. 40:422-432(2001).
RN [18]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [19]
RP FUNCTION.
RX PubMed=15470095; DOI=10.1099/mic.0.27296-0;
RA Teparic R., Stuparevic I., Mrsa V.;
RT "Increased mortality of Saccharomyces cerevisiae cell wall protein
RT mutants.";
RL Microbiology 150:3145-3150(2004).
RN [20]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
RN [21]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA de Koster C.G.;
RT "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT identification of proteins covalently attached via
RT glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL J. Biol. Chem. 280:20894-20901(2005).
RN [22]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
RN [23]
RP INDUCTION.
RX PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
RA Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
RT "Mass spectrometric quantitation of covalently bound cell wall proteins in
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:887-896(2007).
CC -!- FUNCTION: Component of the outer cell wall layer. Required for
CC stability of the cell wall and for optimal growth. Required for
CC resistance against several antifungal and cell wall-perturbing agents
CC and for tolerance to heat shock. {ECO:0000269|PubMed:10209754,
CC ECO:0000269|PubMed:10407261, ECO:0000269|PubMed:15470095,
CC ECO:0000269|PubMed:9192695}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10209754,
CC ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9192695,
CC ECO:0000269|PubMed:9301021}. Note=Covalently attached to the cell wall.
CC -!- INDUCTION: Positively regulated by signaling through MPK1 in response
CC to cell wall perturbation. Induced by heat shock and nitrogen
CC starvation. Expression is also regulated by the ACE2 and SWI5
CC transcription factors. {ECO:0000269|PubMed:10594829,
CC ECO:0000269|PubMed:11309124, ECO:0000269|PubMed:15116342,
CC ECO:0000269|PubMed:17617218, ECO:0000269|PubMed:9192695}.
CC -!- DOMAIN: The PIR1/2/3 repeats are required for the covalent linkage to
CC the cell wall (By similarity). Their number varies among different
CC strains of S.cerevisiae. {ECO:0000250}.
CC -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC of glutamic acids, arising from specific glutamines within the PIR1/2/3
CC repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
CC {ECO:0000250}.
CC -!- PTM: The propeptide is cleaved off in the late Golgi. While both
CC peptides are secreted, only a fraction of the mature glycoprotein is
CC incorporated into the cell wall. {ECO:0000269|PubMed:9301021}.
CC -!- PTM: O-glycosylated. Extensively O-mannosylated.
CC {ECO:0000269|PubMed:9301021}.
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89454.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M88698; AAA17683.1; -; Unassigned_DNA.
DR EMBL; S45000; AAB23364.1; -; Genomic_DNA.
DR EMBL; D13741; BAA02886.1; -; Genomic_DNA.
DR EMBL; Z49434; CAA89454.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU220722; ABY67720.1; -; Genomic_DNA.
DR EMBL; EU220723; ABY67721.1; -; Genomic_DNA.
DR EMBL; EU220724; ABY67722.1; -; Genomic_DNA.
DR EMBL; AY321583; AAQ83898.1; -; Genomic_DNA.
DR EMBL; AY260881; AAP21749.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08644.1; -; Genomic_DNA.
DR PIR; A46183; A46183.
DR PIR; S56942; S56942.
DR RefSeq; NP_012376.3; NM_001181592.1.
DR AlphaFoldDB; P32478; -.
DR BioGRID; 33601; 96.
DR DIP; DIP-2035N; -.
DR IntAct; P32478; 1.
DR MINT; P32478; -.
DR STRING; 4932.YJL159W; -.
DR iPTMnet; P32478; -.
DR COMPLUYEAST-2DPAGE; P32478; -.
DR MaxQB; P32478; -.
DR PaxDb; P32478; -.
DR PRIDE; P32478; -.
DR EnsemblFungi; YJL159W_mRNA; YJL159W; YJL159W.
DR GeneID; 853281; -.
DR KEGG; sce:YJL159W; -.
DR SGD; S000003695; HSP150.
DR VEuPathDB; FungiDB:YJL159W; -.
DR eggNOG; ENOG502QQD8; Eukaryota.
DR GeneTree; ENSGT00940000176350; -.
DR HOGENOM; CLU_039662_0_0_1; -.
DR InParanoid; P32478; -.
DR OMA; IQHQTTV; -.
DR BioCyc; YEAST:G3O-31599-MON; -.
DR PRO; PR:P32478; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32478; protein.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR InterPro; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 11.
DR PROSITE; PS00929; PIR_REPEAT_1; 11.
DR PROSITE; PS50256; PIR_REPEAT_2; 11.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1570286,
FT ECO:0000269|PubMed:9301021"
FT PROPEP 19..72
FT /evidence="ECO:0000269|PubMed:10234784,
FT ECO:0000269|PubMed:1570286, ECO:0000269|PubMed:18657192,
FT ECO:0000269|PubMed:9301021"
FT /id="PRO_0000033260"
FT CHAIN 73..413
FT /note="Cell wall mannoprotein HSP150"
FT /id="PRO_0000033261"
FT REPEAT 73..89
FT /note="PIR1/2/3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 97..115
FT /note="PIR1/2/3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 116..134
FT /note="PIR1/2/3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 140..158
FT /note="PIR1/2/3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 164..182
FT /note="PIR1/2/3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 188..206
FT /note="PIR1/2/3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 207..225
FT /note="PIR1/2/3 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 226..244
FT /note="PIR1/2/3 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 245..263
FT /note="PIR1/2/3 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 264..282
FT /note="PIR1/2/3 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 283..300
FT /note="PIR1/2/3 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT SITE 72..73
FT /note="Cleavage; by KEX2"
FT SITE 81
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 107
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 217
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 236
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 255
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 274
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 292
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT VARIANT 96
FT /note="T -> S (in strain: B1, TD04/1a and TD04/1b)"
FT /evidence="ECO:0000269|PubMed:18657192"
FT VARIANT 116..163
FT /note="Missing (in strain: B1, TD04/1a and TD04/1b)"
FT VARIANT 175
FT /note="V -> I (in strain: TD04/1a and TD04/1b)"
FT /evidence="ECO:0000269|PubMed:18657192"
FT VARIANT 176
FT /note="Q -> QAATTTASVSTKSSAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQ
FT (in strain: TD04/1b)"
FT VARIANT 199
FT /note="V -> I (in strain: B1, TD04/1a and TD04/1b)"
FT /evidence="ECO:0000269|PubMed:18657192"
FT VARIANT 226..244
FT /note="Missing (in strain: B1, TD04/1a and TD04/1b)"
FT /evidence="ECO:0000269|PubMed:18657192"
FT VARIANT 297
FT /note="T -> S (in strain: B1, TD04/1a and TD04/1b)"
FT /evidence="ECO:0000269|PubMed:18657192"
FT CONFLICT 47
FT /note="G -> A (in Ref. 3; BAA02886)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..123
FT /note="QIG -> R (in Ref. 4; CAA89454)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..175
FT /note="Missing (in Ref. 4; CAA89454)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> F (in Ref. 1; AAA17683 and 2; AAB23364)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="Q -> L (in Ref. 1; AAA17683 and 2; AAB23364)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> R (in Ref. 1; AAA17683 and 2; AAB23364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 41059 MW; 5EAF10136E25132A CRC64;
MQYKKTLVAS ALAATTLAAY APSEPWSTLT PTATYSGGVT DYASTFGIAV QPISTTSSAS
SAATTASSKA KRAASQIGDG QVQAATTTAS VSTKSTAAAV SQIGDGQIQA TTKTTAAAVS
QIGDGQIQAT TKTTSAKTTA AAVSQISDGQ IQATTTTLAP KSTAAAVSQI GDGQVQATTT
TLAPKSTAAA VSQIGDGQVQ ATTKTTAAAV SQIGDGQVQA TTKTTAAAVS QIGDGQVQAT
TKTTAAAVSQ IGDGQVQATT KTTAAAVSQI TDGQVQATTK TTQAASQVSD GQVQATTATS
ASAAATSTDP VDAVSCKTSG TLEMNLKGGI LTDGKGRIGS IVANRQFQFD GPPPQAGAIY
AAGWSITPDG NLAIGDNDVF YQCLSGTFYN LYDEHIGSQC TPVHLEAIDL IDC
