MASP2_MOUSE
ID MASP2_MOUSE Reviewed; 685 AA.
AC Q91WP0; B1ARY2; B1ARY3; Q9QXA4; Q9QXD2; Q9QXD5; Q9Z338;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mannan-binding lectin serine protease 2;
DE EC=3.4.21.104;
DE AltName: Full=MBL-associated serine protease 2;
DE AltName: Full=Mannose-binding protein-associated serine protease 2;
DE Short=MASP-2;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 2 A chain;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 2 B chain;
DE Flags: Precursor;
GN Name=Masp2;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9794427;
RA Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M.,
RA Nonaka M., Fujita T.;
RT "Two lineages of mannose-binding lectin-associated serine protease (MASP)
RT in vertebrates.";
RL J. Immunol. 161:4924-4930(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-362 (ISOFORM 1).
RC STRAIN=C57BL/6J X CBA/J;
RX PubMed=10586086;
RA Stover C.M., Thiel S., Lynch N.J., Schwaeble W.J.;
RT "The rat and mouse homologues of MASP-2 and MAp19, components of the
RT mannan-binding lectin activation pathway of complement.";
RL J. Immunol. 163:6848-6859(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15672593; DOI=10.1007/s00335-004-3006-8;
RA Stover C.M., Lynch N.J., Hanson S.J., Windbichler M., Gregory S.G.,
RA Schwaeble W.J.;
RT "Organization of the MASP2 locus and its expression profile in mouse and
RT rat.";
RL Mamm. Genome 15:887-900(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-641.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
CC -!- FUNCTION: Serum protease that plays an important role in the activation
CC of the complement system via mannose-binding lectin. After activation
CC by auto-catalytic cleavage it cleaves C2 and C4, leading to their
CC activation and to the formation of C3 convertase (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage after Arg-223 in complement component C2 (-
CC Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement
CC component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104;
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to
CC MASP1. Binds SERPING1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WP0-1; Sequence=Displayed;
CC Name=2; Synonyms=MAp19;
CC IsoId=Q91WP0-2; Sequence=VSP_014636, VSP_014637;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- MISCELLANEOUS: Dimerization and MBL2 binding requires calcium ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB009459; BAA34674.1; -; mRNA.
DR EMBL; AJ250369; CAB63701.1; -; mRNA.
DR EMBL; Y19160; CAB65247.1; -; mRNA.
DR EMBL; Y19163; CAB65250.1; -; mRNA.
DR EMBL; AK050052; BAC34052.1; -; mRNA.
DR EMBL; AL606969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013893; AAH13893.1; -; mRNA.
DR CCDS; CCDS18941.1; -. [Q91WP0-1]
DR CCDS; CCDS18942.1; -. [Q91WP0-2]
DR RefSeq; NP_001003893.1; NM_001003893.2. [Q91WP0-1]
DR RefSeq; NP_034897.1; NM_010767.3. [Q91WP0-2]
DR AlphaFoldDB; Q91WP0; -.
DR SMR; Q91WP0; -.
DR BioGRID; 201317; 1.
DR STRING; 10090.ENSMUSP00000049729; -.
DR MEROPS; S01.229; -.
DR GlyGen; Q91WP0; 5 sites.
DR iPTMnet; Q91WP0; -.
DR PhosphoSitePlus; Q91WP0; -.
DR CPTAC; non-CPTAC-3430; -.
DR CPTAC; non-CPTAC-3722; -.
DR MaxQB; Q91WP0; -.
DR PaxDb; Q91WP0; -.
DR PeptideAtlas; Q91WP0; -.
DR PRIDE; Q91WP0; -.
DR ProteomicsDB; 252736; -. [Q91WP0-1]
DR ProteomicsDB; 252737; -. [Q91WP0-2]
DR Antibodypedia; 27998; 375 antibodies from 27 providers.
DR DNASU; 17175; -.
DR Ensembl; ENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979. [Q91WP0-1]
DR Ensembl; ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979. [Q91WP0-2]
DR GeneID; 17175; -.
DR KEGG; mmu:17175; -.
DR UCSC; uc008vux.1; mouse. [Q91WP0-2]
DR UCSC; uc008vuy.1; mouse. [Q91WP0-1]
DR CTD; 10747; -.
DR MGI; MGI:1330832; Masp2.
DR VEuPathDB; HostDB:ENSMUSG00000028979; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_103588_3_0_1; -.
DR InParanoid; Q91WP0; -.
DR OMA; YTCAHDG; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q91WP0; -.
DR TreeFam; TF330373; -.
DR BRENDA; 3.4.21.104; 3474.
DR Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR BioGRID-ORCS; 17175; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Masp2; mouse.
DR PRO; PR:Q91WP0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91WP0; protein.
DR Bgee; ENSMUSG00000028979; Expressed in left lobe of liver and 65 other tissues.
DR Genevisible; Q91WP0; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0001855; F:complement component C4b binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:MGI.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR037571; MASP2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255:SF10; PTHR24255:SF10; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF07645; EGF_CA; 1.
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; SM00181; EGF; 1.
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; 2.
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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Calcium; Complement pathway;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation;
KW Immunity; Innate immunity; Metal-binding; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..685
FT /note="Mannan-binding lectin serine protease 2"
FT /id="PRO_0000027601"
FT CHAIN 20..443
FT /note="Mannan-binding lectin serine protease 2 A chain"
FT /id="PRO_0000027602"
FT CHAIN 444..685
FT /note="Mannan-binding lectin serine protease 2 B chain"
FT /id="PRO_0000027603"
FT DOMAIN 20..137
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 138..181
FT /note="EGF-like; calcium-binding"
FT DOMAIN 184..296
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 298..363
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 364..431
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 444..683
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 483
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 532
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 632
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 443..444
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT DISULFID 72..90
FT /evidence="ECO:0000250"
FT DISULFID 142..156
FT /evidence="ECO:0000250"
FT DISULFID 152..165
FT /evidence="ECO:0000250"
FT DISULFID 167..180
FT /evidence="ECO:0000250"
FT DISULFID 184..211
FT /evidence="ECO:0000250"
FT DISULFID 241..259
FT /evidence="ECO:0000250"
FT DISULFID 300..348
FT /evidence="ECO:0000250"
FT DISULFID 328..361
FT /evidence="ECO:0000250"
FT DISULFID 366..411
FT /evidence="ECO:0000250"
FT DISULFID 396..429
FT /evidence="ECO:0000250"
FT DISULFID 433..552
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 598..617
FT /evidence="ECO:0000250"
FT DISULFID 628..659
FT /evidence="ECO:0000250"
FT VAR_SEQ 182..185
FT /note="ALCS -> EQSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10586086"
FT /id="VSP_014636"
FT VAR_SEQ 186..685
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10586086"
FT /id="VSP_014637"
FT CONFLICT 1..2
FT /note="MR -> MSLPCPQ (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="V -> I (in Ref. 1; BAA34674 and 2; CAB65247)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> K (in Ref. 2; CAB65250)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="I -> T (in Ref. 1; BAA34674)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> Y (in Ref. 2; CAB65250)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> Q (in Ref. 1; BAA34674)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="A -> T (in Ref. 1; BAA34674)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="D -> G (in Ref. 1; BAA34674)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="I -> N (in Ref. 1; BAA34674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 75517 MW; F56A6D522BC7099D CRC64;
MRLLIFLGLL WSLVATLLGS KWPEPVFGRL VSPGFPEKYA DHQDRSWTLT APPGYRLRLY
FTHFDLELSY RCEYDFVKLS SGTKVLATLC GQESTDTEQA PGNDTFYSLG PSLKVTFHSD
YSNEKPFTGF EAFYAAEDVD ECRVSLGDSV PCDHYCHNYL GGYYCSCRAG YVLHQNKHTC
SALCSGQVFT GRSGYLSSPE YPQPYPKLSS CTYSIRLEDG FSVILDFVES FDVETHPEAQ
CPYDSLKIQT DKGEHGPFCG KTLPPRIETD SHKVTITFAT DESGNHTGWK IHYTSTARPC
PDPTAPPNGS ISPVQAIYVL KDRFSVFCKT GFELLQGSVP LKSFTAVCQK DGSWDRPMPE
CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF YTMSSNGKYV CEADGFWTSS
KGEKLPPVCE PVCGLSTHTI GGRIVGGQPA KPGDFPWQVL LLGQTTAAAG ALIHDNWVLT
AAHAVYEKRM AASSLNIRMG ILKRLSPHYT QAWPEEIFIH EGYTHGAGFD NDIALIKLKN
KVTINGSIMP VCLPRKEAAS LMRTDFTGTV AGWGLTQKGL LARNLMFVDI PIADHQKCTA
VYEKLYPGVR VSANMLCAGL ETGGKDSCRG DSGGALVFLD NETQRWFVGG IVSWGSINCG
AADQYGVYTK VINYIPWIEN IISNF
