GenomeNet

Database: UniProt
Entry: P98064
LinkDB: P98064
Original site: P98064 
ID   MASP1_MOUSE             Reviewed;         704 AA.
AC   P98064; A2RRH8; A2RRH9; Q8CD27; Q8CIR8; Q920S0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   10-APR-2019, entry version 163.
DE   RecName: Full=Mannan-binding lectin serine protease 1;
DE            EC=3.4.21.-;
DE   AltName: Full=Complement factor MASP-3;
DE   AltName: Full=Complement-activating component of Ra-reactive factor;
DE   AltName: Full=Mannose-binding lectin-associated serine protease 1;
DE            Short=MASP-1;
DE   AltName: Full=Mannose-binding protein-associated serine protease;
DE   AltName: Full=Ra-reactive factor serine protease p100;
DE            Short=RaRF;
DE   AltName: Full=Serine protease 5;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 1 light chain;
DE   Flags: Precursor;
GN   Name=Masp1; Synonyms=Crarf, Masp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=8133044;
RA   Takayama Y., Takada F., Takahashi A., Kawakami M.;
RT   "A 100-kDa protein in the C4-activating component of Ra-reactive
RT   factor is a new serine protease having module organization similar to
RT   C1r and C1s.";
RL   J. Immunol. 152:2308-2316(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
RP   SPLICING (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=12847554; DOI=10.1038/sj.gene.6363970;
RA   Stover C.M., Lynch N.J., Dahl M.R., Hanson S., Takahashi M.,
RA   Frankenberger M., Ziegler-Heitbrock L., Eperon I., Thiel S.,
RA   Schwaeble W.J.;
RT   "Murine serine proteases MASP-1 and MASP-3, components of the lectin
RT   pathway activation complex of complement, are encoded by a single
RT   structural gene.";
RL   Genes Immun. 4:374-384(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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 [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 465-704 (ISOFORM 1), AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=8439319; DOI=10.1006/bbrc.1993.1103;
RA   Takahashi A., Takayama Y., Hatsuse H., Kawakami M.;
RT   "Presence of a serine protease in the complement-activating component
RT   of the complement-dependent bactericidal factor, RaRF, in mouse
RT   serum.";
RL   Biochem. Biophys. Res. Commun. 190:681-687(1993).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18424734; DOI=10.4049/jimmunol.180.9.6132;
RA   Takahashi M., Iwaki D., Kanno K., Ishida Y., Xiong J., Matsushita M.,
RA   Endo Y., Miura S., Ishii N., Sugamura K., Fujita T.;
RT   "Mannose-binding lectin (MBL)-associated serine protease (MASP)-1
RT   contributes to activation of the lectin complement pathway.";
RL   J. Immunol. 180:6132-6138(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Functions in the lectin pathway of complement, which
CC       performs a key role in innate immunity by recognizing pathogens
CC       through patterns of sugar moieties and neutralizing them. The
CC       lectin pathway is triggered upon binding of mannan-binding lectin
CC       (MBL) and ficolins to sugar moieties which leads to activation of
CC       the associated proteases MASP1 and MASP2. Functions as an
CC       endopeptidase and may activate MASP2 or C2 or directly activate C3
CC       the key component of complement reaction. Isoform 2 may have an
CC       inhibitory effect on the activation of the lectin pathway of
CC       complement or may cleave IGFBP5. Also plays a role in development.
CC       {ECO:0000250|UniProtKB:P48740, ECO:0000269|PubMed:18424734}.
CC   -!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2,
CC       FCN2 and FCN3; triggers the lectin pathway of complement through
CC       activation of C3. Interacts with SERPING1. Interacts with COLEC11;
CC       probably triggers the lectin pathway of complement.
CC       {ECO:0000250|UniProtKB:P48740}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8133044}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=MASP-1;
CC         IsoId=P98064-1; Sequence=Displayed;
CC       Name=2; Synonyms=MASP-3;
CC         IsoId=P98064-2; Sequence=VSP_036814, VSP_036815;
CC         Note=Contains a N-linked (GlcNAc...) asparagine at position 538
CC         Contains a N-linked (GlcNAc...) asparagine at position 604.
CC         {ECO:0000250|UniProtKB:P48740};
CC   -!- TISSUE SPECIFICITY: Protein of the plasma which is primarily
CC       expressed by liver. {ECO:0000269|PubMed:18424734,
CC       ECO:0000269|PubMed:8133044}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Autoproteolytic processing of the proenzyme produces the
CC       active enzyme composed on the heavy and the light chain held
CC       together by a disulfide bond. Isoform 1 but not isoform 2 is
CC       activated through autoproteolytic processing (By similarity).
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are smaller and more vulnerable
CC       indicating developmental and growth defects. Mice serum has low C4
CC       and C3 cleavage activity together with low MASP2 activation.
CC       {ECO:0000269|PubMed:18424734}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; D16492; BAA03944.1; -; mRNA.
DR   EMBL; AB049755; BAB69688.1; -; mRNA.
DR   EMBL; AY135527; AAN39850.1; -; Genomic_DNA.
DR   EMBL; AY135525; AAN39850.1; JOINED; Genomic_DNA.
DR   EMBL; AK031598; BAC27469.1; -; mRNA.
DR   EMBL; CH466521; EDK97670.1; -; Genomic_DNA.
DR   EMBL; CH466521; EDK97671.1; -; Genomic_DNA.
DR   EMBL; BC131637; AAI31638.1; -; mRNA.
DR   EMBL; BC131638; AAI31639.1; -; mRNA.
DR   CCDS; CCDS37303.1; -. [P98064-1]
DR   PIR; PC1235; PC1235.
DR   RefSeq; NP_032581.2; NM_008555.2. [P98064-1]
DR   RefSeq; XP_006521891.1; XM_006521828.3.
DR   UniGene; Mm.1213; -.
DR   ProteinModelPortal; P98064; -.
DR   SMR; P98064; -.
DR   STRING; 10090.ENSMUSP00000087327; -.
DR   MEROPS; S01.132; -.
DR   iPTMnet; P98064; -.
DR   PhosphoSitePlus; P98064; -.
DR   MaxQB; P98064; -.
DR   PaxDb; P98064; -.
DR   PeptideAtlas; P98064; -.
DR   PRIDE; P98064; -.
DR   Ensembl; ENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
DR   Ensembl; ENSMUST00000229619; ENSMUSP00000155665; ENSMUSG00000022887. [P98064-2]
DR   GeneID; 17174; -.
DR   KEGG; mmu:17174; -.
DR   UCSC; uc007ytr.1; mouse. [P98064-1]
DR   UCSC; uc007yts.1; mouse. [P98064-2]
DR   CTD; 5648; -.
DR   MGI; MGI:88492; Masp1.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00950000183084; -.
DR   HOGENOM; HOG000237311; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; P98064; -.
DR   KO; K03992; -.
DR   OMA; DLSQRWV; -.
DR   OrthoDB; 156878at2759; -.
DR   PhylomeDB; P98064; -.
DR   TreeFam; TF330373; -.
DR   BRENDA; 3.4.21.B7; 3474.
DR   PRO; PR:P98064; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022887; Expressed in 18 organ(s), highest expression level in liver.
DR   ExpressionAtlas; P98064; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autocatalytic cleavage; Calcium;
KW   Complement activation lectin pathway; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW   Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Sushi.
FT   SIGNAL        1     24
FT   CHAIN        25    704       Mannan-binding lectin serine protease 1.
FT                                /FTId=PRO_0000027595.
FT   CHAIN        25    453       Mannan-binding lectin serine protease 1
FT                                heavy chain.
FT                                /FTId=PRO_0000027596.
FT   CHAIN       454    704       Mannan-binding lectin serine protease 1
FT                                light chain.
FT                                /FTId=PRO_0000027597.
FT   DOMAIN       25    143       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      144    187       EGF-like; calcium-binding. {ECO:0000250}.
FT   DOMAIN      190    302       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      304    369       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      370    439       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      454    701       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION       25    305       Interaction with MBL1. {ECO:0000250}.
FT   REGION       25    283       Interaction with FCN2. {ECO:0000250}.
FT   REGION       25    189       Homodimerization. {ECO:0000250}.
FT   REGION       25    189       Interaction with MBL2. {ECO:0000250}.
FT   ACT_SITE    495    495       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    557    557       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    651    651       Charge relay system. {ECO:0000250}.
FT   METAL        73     73       Calcium 1. {ECO:0000250}.
FT   METAL        81     81       Calcium 1. {ECO:0000250}.
FT   METAL       126    126       Calcium 1. {ECO:0000250}.
FT   METAL       128    128       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       144    144       Calcium 2. {ECO:0000250}.
FT   METAL       145    145       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       147    147       Calcium 2. {ECO:0000250}.
FT   METAL       164    164       Calcium 2. {ECO:0000250}.
FT   METAL       165    165       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       168    168       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       240    240       Calcium 3. {ECO:0000250}.
FT   METAL       250    250       Calcium 3. {ECO:0000250}.
FT   METAL       287    287       Calcium 3. {ECO:0000250}.
FT   METAL       289    289       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   SITE        453    454       Cleavage; by autolysis. {ECO:0000250}.
FT   MOD_RES     164    164       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    183    183       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    390    390       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    412    412       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     78     96       {ECO:0000250}.
FT   DISULFID    148    162       {ECO:0000250}.
FT   DISULFID    158    171       {ECO:0000250}.
FT   DISULFID    173    186       {ECO:0000250}.
FT   DISULFID    190    217       {ECO:0000250}.
FT   DISULFID    247    265       {ECO:0000250}.
FT   DISULFID    306    354       {ECO:0000250}.
FT   DISULFID    334    367       {ECO:0000250}.
FT   DISULFID    372    419       {ECO:0000250}.
FT   DISULFID    402    437       {ECO:0000250}.
FT   DISULFID    441    577       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DISULFID    480    496       {ECO:0000250}.
FT   DISULFID    619    636       {ECO:0000250}.
FT   DISULFID    647    677       {ECO:0000250}.
FT   VAR_SEQ     443    443       V -> QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTS
FT                                RVPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKE
FT                                HVTVYLGLHDVRDKSGAVNSSAARVILHPDFNIQNYNHDIA
FT                                LVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGIS
FT                                NPNVTVDEIILSGTRTLSDVLQYVKLPVVSHAECKASYESR
FT                                SGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQHW
FT                                VAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPR
FT                                AVRDLQVER (in isoform 2).
FT                                {ECO:0000303|PubMed:12847554,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_036814.
FT   VAR_SEQ     444    704       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12847554,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_036815.
FT   CONFLICT    257    257       G -> A (in Ref. 5; AAI31638).
FT                                {ECO:0000305}.
FT   CONFLICT    345    345       E -> G (in Ref. 1; BAA03944 and 2;
FT                                BAB69688). {ECO:0000305}.
FT   CONFLICT    428    428       E -> K (in Ref. 1; BAA03944).
FT                                {ECO:0000305}.
FT   CONFLICT    465    465       M -> T (in Ref. 2; AAN39850).
FT                                {ECO:0000305}.
SQ   SEQUENCE   704 AA;  79968 MW;  4CF0B17916C10961 CRC64;
     MRFLSFWRLL LYHALCLALP EVSAHTVELN EMFGQIQSPG YPDSYPSDSE VTWNITVPEG
     FRIKLYFMHF NLESSYLCEY DYVKVETEDQ VLATFCGRET TDTEQTPGQE VVLSPGTFMS
     VTFRSDFSNE ERFTGFDAHY MAVDVDECKE REDEELSCDH YCHNYIGGYY CSCRFGYILH
     TDNRTCRVEC SGNLFTQRTG TITSPDYPNP YPKSSECSYT IDLEEGFMVS LQFEDIFDIE
     DHPEVPCPYD YIKIKAGSKV WGPFCGEKSP EPISTQTHSV QILFRSDNSG ENRGWRLSYR
     AAGNECPKLQ PPVYGKIEPS QAVYSFKDQV LVSCDTGYKV LKDNEVMDTF QIECLKDGAW
     SNKIPTCKIV DCGAPAGLKH GLVTFSTRNN LTTYKSEIRY SCQQPYYKML HNTTGVYTCS
     AHGTWTNEVL KRSLPTCLPV CGVPKFSRKQ ISRIFNGRPA QKGTMPWIAM LSHLNGQPFC
     GGSLLGSNWV LTAAHCLHQS LDPEEPTLHS SYLLSPSDFK IIMGKHWRRR SDEDEQHLHV
     KRTTLHPLYN PSTFENDLGL VELSESPRLN DFVMPVCLPE QPSTEGTMVI VSGWGKQFLQ
     RFPENLMEIE IPIVNSDTCQ EAYTPLKKKV TKDMICAGEK EGGKDACAGD SGGPMVTKDA
     ERDQWYLVGV VSWGEDCGKK DRYGVYSYIY PNKDWIQRIT GVRN
//
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