CO2_MOUSE
ID CO2_MOUSE Reviewed; 760 AA.
AC P21180; O70350;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Complement C2;
DE EC=3.4.21.43;
DE AltName: Full=C3/C5 convertase;
DE Contains:
DE RecName: Full=Complement C2b fragment;
DE Contains:
DE RecName: Full=Complement C2a fragment;
DE Flags: Precursor;
GN Name=C2;
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 [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=2229060; DOI=10.1016/s0021-9258(17)30621-x;
RA Ishikawa N., Nonaka M., Wetsel R.A., Colten H.R.;
RT "Murine complement C2 and factor B genomic and cDNA cloning reveals
RT different mechanisms for multiple transcripts of C2 and B.";
RL J. Biol. Chem. 265:19040-19046(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component C2 which is part of the classical pathway of the
CC complement system is cleaved by activated factor C1 into two fragments:
CC C2b and C2a. C2a, a serine protease, then combines with complement
CC factor C4b to generate the C3 or C5 convertase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ser bond in complement component
CC C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement
CC component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P21180-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P21180-2; Sequence=VSP_005385;
CC -!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal
CC cations. {ECO:0000250}.
CC -!- MISCELLANEOUS: C2 is a major histocompatibility complex class-III
CC protein.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M57891; AAA63294.1; -; mRNA.
DR EMBL; M60579; AAA37380.1; -; Genomic_DNA.
DR EMBL; M60563; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60564; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60565; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60566; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60567; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60568; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60569; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60570; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60571; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60572; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60573; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60574; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60575; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60605; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60576; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60577; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60578; AAA37380.1; JOINED; Genomic_DNA.
DR EMBL; M60579; AAA37381.1; -; Genomic_DNA.
DR EMBL; M60563; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60564; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60565; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60566; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60567; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60568; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60569; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60570; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60571; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60572; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60573; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60574; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60575; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60605; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60576; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60577; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; M60578; AAA37381.1; JOINED; Genomic_DNA.
DR EMBL; AK146812; BAE27452.1; -; mRNA.
DR EMBL; AF109906; AAC84162.1; -; Genomic_DNA.
DR EMBL; CT025759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466666; EDL26734.1; -; Genomic_DNA.
DR EMBL; BC011086; AAH11086.1; -; mRNA.
DR CCDS; CCDS28664.1; -. [P21180-1]
DR PIR; A38876; C2MS.
DR RefSeq; NP_038512.2; NM_013484.2. [P21180-1]
DR AlphaFoldDB; P21180; -.
DR SMR; P21180; -.
DR ComplexPortal; CPX-6198; Classical and lectin pathway C3 convertase complex C4b2a-B.
DR IntAct; P21180; 1.
DR MINT; P21180; -.
DR STRING; 10090.ENSMUSP00000025230; -.
DR MEROPS; S01.194; -.
DR GlyGen; P21180; 8 sites.
DR iPTMnet; P21180; -.
DR PhosphoSitePlus; P21180; -.
DR CPTAC; non-CPTAC-3777; -.
DR CPTAC; non-CPTAC-5589; -.
DR MaxQB; P21180; -.
DR PaxDb; P21180; -.
DR PeptideAtlas; P21180; -.
DR PRIDE; P21180; -.
DR ProteomicsDB; 283593; -. [P21180-1]
DR ProteomicsDB; 283594; -. [P21180-2]
DR Antibodypedia; 7528; 509 antibodies from 32 providers.
DR DNASU; 12263; -.
DR Ensembl; ENSMUST00000025230; ENSMUSP00000025230; ENSMUSG00000024371. [P21180-1]
DR GeneID; 12263; -.
DR KEGG; mmu:12263; -.
DR UCSC; uc008cdz.2; mouse. [P21180-1]
DR CTD; 717; -.
DR MGI; MGI:88226; C2.
DR VEuPathDB; HostDB:ENSMUSG00000024371; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162934; -.
DR HOGENOM; CLU_022004_1_0_1; -.
DR InParanoid; P21180; -.
DR OMA; PRSILWI; -.
DR OrthoDB; 172139at2759; -.
DR PhylomeDB; P21180; -.
DR TreeFam; TF330194; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-174577; Activation of C3 and C5.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12263; 1 hit in 78 CRISPR screens.
DR ChiTaRS; C2; mouse.
DR PRO; PR:P21180; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P21180; protein.
DR Bgee; ENSMUSG00000024371; Expressed in iris and 159 other tissues.
DR ExpressionAtlas; P21180; baseline and differential.
DR Genevisible; P21180; MM.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006956; P:complement activation; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISO:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:1903028; P:positive regulation of opsonization; IC:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR037568; Complement_C2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
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 InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR46393; PTHR46393; 1.
DR PANTHER; PTHR46393:SF2; PTHR46393:SF2; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF001154; Compl_C2_B; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57535; SSF57535; 3.
DR PROSITE; PS50923; SUSHI; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complement pathway; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunity; Innate immunity; Metal-binding; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..18
FT CHAIN 19..760
FT /note="Complement C2"
FT /id="PRO_0000027613"
FT CHAIN 19..250
FT /note="Complement C2b fragment"
FT /id="PRO_0000027614"
FT CHAIN 251..760
FT /note="Complement C2a fragment"
FT /id="PRO_0000027615"
FT DOMAIN 20..90
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 92..151
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 154..212
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 261..459
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 471..752
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 267..271
FT /note="MIDAS-like motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 514
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 570
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 689
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..62
FT /evidence="ECO:0000250"
FT DISULFID 49..89
FT /evidence="ECO:0000250"
FT DISULFID 94..136
FT /evidence="ECO:0000250"
FT DISULFID 122..149
FT /evidence="ECO:0000250"
FT DISULFID 156..197
FT /evidence="ECO:0000250"
FT DISULFID 182..210
FT /evidence="ECO:0000250"
FT DISULFID 499..515
FT /evidence="ECO:0000250"
FT DISULFID 685..715
FT /evidence="ECO:0000250"
FT VAR_SEQ 606..612
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:2229060"
FT /id="VSP_005385"
FT CONFLICT 123..124
FT /note="EQ -> DE (in Ref. 1; AAA37380/AAA37381/AAA63294)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> T (in Ref. 1; AAA37380/AAA37381/AAA63294)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="T -> A (in Ref. 1; AAA37380/AAA37381/AAA63294)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> T (in Ref. 1; AAA37380/AAA37381/AAA63294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 84741 MW; 91C896A3EDC7D448 CRC64;
MAPLLALFYL LQLGPGLAAL FCNQNVNITG GNFTLSHGWA PGSLLIYSCP LGRYPSPAWR
KCQSNGQWLT PRSSSHHTLR SSRMVKAVCK PVRCLAPSSF ENGIYFPRLV SYPVGSNVSF
ECEQDFTLRG SPVRYCRPNG LWDGETAVCD NGASHCPNPG ISVGTARTGL NFDLGDKVRY
RCSSSNMVLT GSAERECQSN GVWSGSEPIC RQPYSYDFPE DVASALDTSL TNLLGATNPT
QNLLTKSLGR KIIIQRSGHL NLYLLLDASQ SVTEKDFDIF KKSAELMVER IFSFEVNVSV
AIITFASQPK TIMSILSERS QDVTEVITSL DSASYKDHEN ATGTNTYEVL IRVYSMMQSQ
MDRLGMETSA WKEIRHTIIL LTDGKSNMGD SPKKAVTRIR ELLSIEQNRD DYLDIYAIGV
GKLDVDWKEL NELGSKKDGE RHAFILQDAK ALQQIFEHML DVSKLTDTIC GVGNMSANAS
DQERTPWQVT FKPKSKETCQ GSLISDQWVL TAAHCFHDIQ MEDHHLWRVN VGDPTSQHGK
EFLVEDVIIA PGFNVHAKRK QGISEFYADD IALLKLSRKV KMSTHARPIC LPCTVGANMA
LRRSPGSTCK DHETELLSQQ KVPAHFVALN GNRLNINLRT GPEWTRCIQA VSQNKNIFPS
LTNVSEVVTD QFLCSGMEEE DDNPCKGESG GAVFLGRRYR FFQVGLVSWG LFDPCHGSSN
KNLRKKPPRG VLPRDFHISL FRLQPWLRQH LDGVLDFLPL
