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Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]

 MASP1_MOUSE             Reviewed;         704 AA.
P98064; A2RRH8; A2RRH9; Q8CD27; Q8CIR8; Q920S0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 2.
29-SEP-2021, entry version 175.
RecName: Full=Mannan-binding lectin serine protease 1;
EC=3.4.21.-;
AltName: Full=Complement factor MASP-3;
AltName: Full=Complement-activating component of Ra-reactive factor;
AltName: Full=Mannose-binding lectin-associated serine protease 1;
Short=MASP-1;
AltName: Full=Mannose-binding protein-associated serine protease;
AltName: Full=Ra-reactive factor serine protease p100;
Short=RaRF;
AltName: Full=Serine protease 5;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 light chain;
Flags: Precursor;
Name=Masp1; Synonyms=Crarf, Masp3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8133044;
Takayama Y., Takada F., Takahashi A., Kawakami M.;
"A 100-kDa protein in the C4-activating component of Ra-reactive factor is
a new serine protease having module organization similar to C1r and C1s.";
J. Immunol. 152:2308-2316(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
SPLICING (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=12847554; DOI=10.1038/sj.gene.6363970;
Stover C.M., Lynch N.J., Dahl M.R., Hanson S., Takahashi M.,
Frankenberger M., Ziegler-Heitbrock L., Eperon I., Thiel S.,
Schwaeble W.J.;
"Murine serine proteases MASP-1 and MASP-3, components of the lectin
pathway activation complex of complement, are encoded by a single
structural gene.";
Genes Immun. 4:374-384(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 465-704 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8439319; DOI=10.1006/bbrc.1993.1103;
Takahashi A., Takayama Y., Hatsuse H., Kawakami M.;
"Presence of a serine protease in the complement-activating component of
the complement-dependent bactericidal factor, RaRF, in mouse serum.";
Biochem. Biophys. Res. Commun. 190:681-687(1993).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18424734; DOI=10.4049/jimmunol.180.9.6132;
Takahashi M., Iwaki D., Kanno K., Ishida Y., Xiong J., Matsushita M.,
Endo Y., Miura S., Ishii N., Sugamura K., Fujita T.;
"Mannose-binding lectin (MBL)-associated serine protease (MASP)-1
contributes to activation of the lectin complement pathway.";
J. Immunol. 180:6132-6138(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Functions in the lectin pathway of complement, which performs
a key role in innate immunity by recognizing pathogens through patterns
of sugar moieties and neutralizing them. The lectin pathway is
triggered upon binding of mannan-binding lectin (MBL) and ficolins to
sugar moieties which leads to activation of the associated proteases
MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2
or C2 or directly activate C3 the key component of complement reaction.
Isoform 2 may have an inhibitory effect on the activation of the lectin
pathway of complement or may cleave IGFBP5. Also plays a role in
development. {ECO:0000250|UniProtKB:P48740,
ECO:0000269|PubMed:18424734}.
-!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2, FCN2
and FCN3; triggers the lectin pathway of complement through activation
of C3. Interacts with SERPING1. Interacts with COLEC11; probably
triggers the lectin pathway of complement.
{ECO:0000250|UniProtKB:P48740}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8133044}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MASP-1;
IsoId=P98064-1; Sequence=Displayed;
Name=2; Synonyms=MASP-3;
IsoId=P98064-2; Sequence=VSP_036814, VSP_036815;
-!- TISSUE SPECIFICITY: Protein of the plasma which is primarily expressed
by liver. {ECO:0000269|PubMed:18424734, ECO:0000269|PubMed:8133044}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
-!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type (By
similarity). {ECO:0000250}.
-!- PTM: Autoproteolytic processing of the proenzyme produces the active
enzyme composed on the heavy and the light chain held together by a
disulfide bond. Isoform 1 but not isoform 2 is activated through
autoproteolytic processing (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are smaller and more vulnerable indicating
developmental and growth defects. Mice serum has low C4 and C3 cleavage
activity together with low MASP2 activation.
{ECO:0000269|PubMed:18424734}.
-!- MISCELLANEOUS: [Isoform 2]: Contains a N-linked (GlcNAc...) asparagine
at position 538 Contains a N-linked (GlcNAc...) asparagine at position
604. {ECO:0000250|UniProtKB:P48740}.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
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EMBL; D16492; BAA03944.1; -; mRNA.
EMBL; AB049755; BAB69688.1; -; mRNA.
EMBL; AY135527; AAN39850.1; -; Genomic_DNA.
EMBL; AY135525; AAN39850.1; JOINED; Genomic_DNA.
EMBL; AK031598; BAC27469.1; -; mRNA.
EMBL; CH466521; EDK97670.1; -; Genomic_DNA.
EMBL; CH466521; EDK97671.1; -; Genomic_DNA.
EMBL; BC131637; AAI31638.1; -; mRNA.
EMBL; BC131638; AAI31639.1; -; mRNA.
CCDS; CCDS37303.1; -. [P98064-1]
CCDS; CCDS88904.1; -. [P98064-2]
PIR; PC1235; PC1235.
RefSeq; NP_032581.2; NM_008555.2. [P98064-1]
RefSeq; XP_006521891.1; XM_006521828.3.
SMR; P98064; -.
BioGRID; 201316; 1.
STRING; 10090.ENSMUSP00000087327; -.
MEROPS; S01.198; -.
GlyGen; P98064; 4 sites.
iPTMnet; P98064; -.
PhosphoSitePlus; P98064; -.
CPTAC; non-CPTAC-3723; -.
MaxQB; P98064; -.
PaxDb; P98064; -.
PeptideAtlas; P98064; -.
PRIDE; P98064; -.
ProteomicsDB; 292089; -. [P98064-1]
ProteomicsDB; 292090; -. [P98064-2]
Antibodypedia; 889; 358 antibodies.
DNASU; 17174; -.
Ensembl; ENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
Ensembl; ENSMUST00000229619; ENSMUSP00000155665; ENSMUSG00000022887. [P98064-2]
GeneID; 17174; -.
KEGG; mmu:17174; -.
UCSC; uc007ytr.1; mouse. [P98064-1]
UCSC; uc007yts.1; mouse. [P98064-2]
CTD; 5648; -.
MGI; MGI:88492; Masp1.
VEuPathDB; HostDB:ENSMUSG00000022887; -.
eggNOG; KOG3627; Eukaryota.
GeneTree; ENSGT00950000183084; -.
HOGENOM; CLU_006842_14_1_1; -.
InParanoid; P98064; -.
OMA; WGGPEDC; -.
OrthoDB; 156878at2759; -.
PhylomeDB; P98064; -.
TreeFam; TF330373; -.
BRENDA; 3.4.21.B7; 3474.
Reactome; R-MMU-166662; Lectin pathway of complement activation.
Reactome; R-MMU-166663; Initial triggering of complement.
Reactome; R-MMU-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
BioGRID-ORCS; 17174; 3 hits in 63 CRISPR screens.
ChiTaRS; Masp1; mouse.
PRO; PR:P98064; -.
Proteomes; UP000000589; Chromosome 16.
RNAct; P98064; protein.
Bgee; ENSMUSG00000022887; Expressed in multi-cellular organism and 66 other tissues.
ExpressionAtlas; P98064; baseline and differential.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
CDD; cd00033; CCP; 2.
CDD; cd00041; CUB; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 1.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00431; CUB; 2.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 2.
SMART; SM00042; CUB; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Calcium;
Complement activation lectin pathway; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation;
Immunity; Innate immunity; Metal-binding; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Sushi.
SIGNAL 1..24
CHAIN 25..704
/note="Mannan-binding lectin serine protease 1"
/id="PRO_0000027595"
CHAIN 25..453
/note="Mannan-binding lectin serine protease 1 heavy chain"
/id="PRO_0000027596"
CHAIN 454..704
/note="Mannan-binding lectin serine protease 1 light chain"
/id="PRO_0000027597"
DOMAIN 25..143
/note="CUB 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
DOMAIN 144..187
/note="EGF-like; calcium-binding"
/evidence="ECO:0000250"
DOMAIN 190..302
/note="CUB 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
DOMAIN 304..369
/note="Sushi 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
DOMAIN 370..439
/note="Sushi 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
DOMAIN 454..701
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 25..305
/note="Interaction with MBL1"
/evidence="ECO:0000250"
REGION 25..283
/note="Interaction with FCN2"
/evidence="ECO:0000250"
REGION 25..189
/note="Homodimerization"
/evidence="ECO:0000250"
REGION 25..189
/note="Interaction with MBL2"
/evidence="ECO:0000250"
ACT_SITE 495
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 557
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 651
/note="Charge relay system"
/evidence="ECO:0000250"
METAL 73
/note="Calcium 1"
/evidence="ECO:0000250"
METAL 81
/note="Calcium 1"
/evidence="ECO:0000250"
METAL 126
/note="Calcium 1"
/evidence="ECO:0000250"
METAL 128
/note="Calcium 1; via carbonyl oxygen"
/evidence="ECO:0000250"
METAL 144
/note="Calcium 2"
/evidence="ECO:0000250"
METAL 145
/note="Calcium 2; via carbonyl oxygen"
/evidence="ECO:0000250"
METAL 147
/note="Calcium 2"
/evidence="ECO:0000250"
METAL 164
/note="Calcium 2"
/evidence="ECO:0000250"
METAL 165
/note="Calcium 2; via carbonyl oxygen"
/evidence="ECO:0000250"
METAL 168
/note="Calcium 2; via carbonyl oxygen"
/evidence="ECO:0000250"
METAL 240
/note="Calcium 3"
/evidence="ECO:0000250"
METAL 250
/note="Calcium 3"
/evidence="ECO:0000250"
METAL 287
/note="Calcium 3"
/evidence="ECO:0000250"
METAL 289
/note="Calcium 3; via carbonyl oxygen"
/evidence="ECO:0000250"
SITE 453..454
/note="Cleavage; by autolysis"
/evidence="ECO:0000250"
MOD_RES 164
/note="(3R)-3-hydroxyasparagine"
/evidence="ECO:0000255"
CARBOHYD 54
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 183
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 390
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 412
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 78..96
/evidence="ECO:0000250"
DISULFID 148..162
/evidence="ECO:0000250"
DISULFID 158..171
/evidence="ECO:0000250"
DISULFID 173..186
/evidence="ECO:0000250"
DISULFID 190..217
/evidence="ECO:0000250"
DISULFID 247..265
/evidence="ECO:0000250"
DISULFID 306..354
/evidence="ECO:0000250"
DISULFID 334..367
/evidence="ECO:0000250"
DISULFID 372..419
/evidence="ECO:0000250"
DISULFID 402..437
/evidence="ECO:0000250"
DISULFID 441..577
/note="Interchain (between heavy and light chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302"
DISULFID 480..496
/evidence="ECO:0000250"
DISULFID 619..636
/evidence="ECO:0000250"
DISULFID 647..677
/evidence="ECO:0000250"
VAR_SEQ 443
/note="V -> QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRVPNDKWFGSG
ALLSESWILTAAHVLRSQRRDNTVIPVSKEHVTVYLGLHDVRDKSGAVNSSAARVILHP
DFNIQNYNHDIALVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTV
DEIILSGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCL
GDSGGAFVIFDEMSQHWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPRA
VRDLQVER (in isoform 2)"
/evidence="ECO:0000303|PubMed:12847554,
ECO:0000303|PubMed:16141072"
/id="VSP_036814"
VAR_SEQ 444..704
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:12847554,
ECO:0000303|PubMed:16141072"
/id="VSP_036815"
CONFLICT 257
/note="G -> A (in Ref. 5; AAI31638)"
/evidence="ECO:0000305"
CONFLICT 345
/note="E -> G (in Ref. 1; BAA03944 and 2; BAB69688)"
/evidence="ECO:0000305"
CONFLICT 428
/note="E -> K (in Ref. 1; BAA03944)"
/evidence="ECO:0000305"
CONFLICT 465
/note="M -> T (in Ref. 2; AAN39850)"
/evidence="ECO:0000305"
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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U1895r CLIA kit Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-bindi 96T
E1895r ELISA kit Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-bind 96T
E1895m ELISA kit Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-bind 96T
U1895m CLIA kit Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-bindi 96T
E1895m ELISA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-binding p 96T
U1895r CLIA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-binding pr 96T
E1895r ELISA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-binding p 96T
U1895m CLIA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,Crarf,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine protease 1,Mannose-binding pr 96T
E1895h ELISA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,CRARF,CRARF1,Homo sapiens,Human,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine pr 96T
U1895h CLIA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,CRARF,CRARF1,Homo sapiens,Human,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine pro 96T
U2234h CLIA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus
E2234r Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus
Pathways :
WP2199: Seed Development
WP1659: Glycine, serine and threonine metabolism
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP218: Serine and Glycine biosynthesis
WP390: Serine-isocitrate lyase pathway
WP459: Serine Biosynthesis
WP2185: Purine metabolism
WP470: Proteasome Degradation
WP731: Sterol regulatory element binding protein related
WP2292: Chemokine signaling pathway
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP590: Cardiovascular Signaling
WP1825: GPCR ligand binding
WP1654: gamma-Hexachlorocyclohexane degradation
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1665: Limonene and pinene degradation
WP2148: Brain derived neurotrophic factor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1502: Mitochondrial biogenesis

Related Genes :
[MASP1 CRARF CRARF1 PRSS5] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[MASP2] Mannan-binding lectin serine protease 2 (EC 3.4.21.104) (MBL-associated serine protease 2) (Mannose-binding protein-associated serine protease 2) (MASP-2) [Cleaved into: Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain]
[Mbl1] Mannose-binding protein A (MBP-A) (Mannan-binding protein) (Ra-reactive factor polysaccharide-binding component p28B) (RaRF p28B)
[Mbl2] Mannose-binding protein C (MBP-C) (Mannan-binding protein) (Ra-reactive factor polysaccharide-binding component p28A) (RaRF p28A)
[MBL2 COLEC1 MBL] Mannose-binding protein C (MBP-C) (Collectin-1) (MBP1) (Mannan-binding protein) (Mannose-binding lectin)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[PPAF1 PPAF-I] Phenoloxidase-activating factor 1 (EC 3.4.21.-) (Prophenoloxidase-activating factor I) (Serine protease PPAF-1) [Cleaved into: Phenoloxidase-activating factor 1 light chain; Phenoloxidase-activating factor 1 heavy chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[C1S] Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]
[] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[GP1 MZ11_60484gpGP1 MZ11_60553gpGP1] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease/Helicase NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Mbl2] Mannose-binding protein C (MBP-C) (Mannan-binding protein) (RA-reactive factor P28A subunit) (RARF/P28A)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[MBL1 MBL-A] Mannose-binding protein A (MBP-A) (28 kDa mannan-binding protein monomeric subunit) (pMBP-28) (Mannan-binding lectin A) (MBL-A) (Mannose-binding lectin A)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)] (Fragment)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :
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