CO3A1_MOUSE
ID CO3A1_MOUSE Reviewed; 1464 AA.
AC P08121; Q61429; Q9CRN7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 4.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Collagen alpha-1(III) chain;
DE Flags: Precursor;
GN Name=Col3a1;
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].
RC STRAIN=C57BL/6 X DBA; TISSUE=Embryo;
RX PubMed=7926795; DOI=10.1016/0378-1119(94)90061-2;
RA Toman D., de Crombrugghe B.;
RT "The mouse type-III procollagen-encoding gene: genomic cloning and complete
RT DNA sequence.";
RL Gene 147:161-168(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-488.
RX PubMed=3443309; DOI=10.1016/0378-1119(87)90117-x;
RA Wood L., Theriault N., Vogeli G.;
RT "Complete nucleotide sequence of the N-terminal domains of the murine
RT alpha-1 type-III collagen chain.";
RL Gene 61:225-230(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=3972847; DOI=10.1016/s0021-9258(19)83690-6;
RA Liau G., Mudryj M., de Crombrugghe B.;
RT "Identification of the promoter and first exon of the mouse alpha 1 (III)
RT collagen gene.";
RL J. Biol. Chem. 260:3773-3777(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 810-1464.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 [6]
RP NUCLEOTIDE SEQUENCE OF 1442-1464.
RC STRAIN=C57BL/6J;
RX PubMed=2054384; DOI=10.1016/0167-4781(91)90014-d;
RA Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
RT "Specific hybridization probes for mouse type I, II, III and IX collagen
RT mRNAs.";
RL Biochim. Biophys. Acta 1089:241-243(1991).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Pancreas;
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).
RN [8]
RP FUNCTION, RECEPTOR-BINDING, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21768377; DOI=10.1073/pnas.1104821108;
RA Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.;
RT "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair,
RT regulates cortical development and lamination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011).
CC -!- FUNCTION: Collagen type III occurs in most soft connective tissues
CC along with type I collagen. Involved in regulation of cortical
CC development. Is the major ligand of ADGRG1 in the developing brain and
CC binding to ADGRG1 inhibits neuronal migration and activates the RhoA
CC pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
CC {ECO:0000269|PubMed:21768377}.
CC -!- SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are
CC linked to each other by interchain disulfide bonds. Trimers are also
CC cross-linked via hydroxylysines. Interacts with ADGRG1 (By similarity).
CC {ECO:0000250|UniProtKB:P02461}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic brain, specifically in the
CC meninges, pial basement membrane and blood vessels (at protein level).
CC {ECO:0000269|PubMed:21768377}.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: Proline residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the
CC oxygen atom of a post-translationally added hydroxyl group.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Neuronal ectopias and abnormal cortical
CC lamination. {ECO:0000269|PubMed:21768377}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; X52046; CAA36279.1; -; Genomic_DNA.
DR EMBL; BC043089; AAH43089.1; -; mRNA.
DR EMBL; BC058724; AAH58724.1; -; mRNA.
DR EMBL; M18933; AAA37338.1; -; mRNA.
DR EMBL; K03037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK019448; BAB31724.1; -; mRNA.
DR EMBL; X57983; CAA41048.1; -; Genomic_DNA.
DR CCDS; CCDS35554.1; -.
DR PIR; A27353; A27353.
DR PIR; S59856; S59856.
DR RefSeq; NP_034060.2; NM_009930.2.
DR AlphaFoldDB; P08121; -.
DR SMR; P08121; -.
DR BioGRID; 198815; 11.
DR ComplexPortal; CPX-2958; Collagen type III trimer.
DR IntAct; P08121; 2.
DR STRING; 10090.ENSMUSP00000085192; -.
DR GlyGen; P08121; 1 site.
DR iPTMnet; P08121; -.
DR PhosphoSitePlus; P08121; -.
DR CPTAC; non-CPTAC-3364; -.
DR jPOST; P08121; -.
DR PaxDb; P08121; -.
DR PeptideAtlas; P08121; -.
DR PRIDE; P08121; -.
DR ProteomicsDB; 283595; -.
DR Antibodypedia; 3392; 805 antibodies from 38 providers.
DR DNASU; 12825; -.
DR Ensembl; ENSMUST00000087883; ENSMUSP00000085192; ENSMUSG00000026043.
DR GeneID; 12825; -.
DR KEGG; mmu:12825; -.
DR UCSC; uc007awq.2; mouse.
DR CTD; 1281; -.
DR MGI; MGI:88453; Col3a1.
DR VEuPathDB; HostDB:ENSMUSG00000026043; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161229; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P08121; -.
DR OMA; PQFESYD; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; P08121; -.
DR TreeFam; TF344135; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12825; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Col3a1; mouse.
DR PRO; PR:P08121; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P08121; protein.
DR Bgee; ENSMUSG00000026043; Expressed in efferent duct and 273 other tissues.
DR ExpressionAtlas; P08121; baseline and differential.
DR Genevisible; P08121; MM.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005586; C:collagen type III trimer; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0048251; P:elastic fiber assembly; IMP:MGI.
DR GO; GO:0060350; P:endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR GO; GO:0036022; P:limb joint morphogenesis; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0050777; P:negative regulation of immune response; ISO:MGI.
DR GO; GO:2001223; P:negative regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:1990776; P:response to angiotensin; IMP:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; ISO:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0032905; P:transforming growth factor beta1 production; IMP:MGI.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT PROPEP 24..154
FT /note="N-terminal propeptide"
FT /id="PRO_0000005743"
FT CHAIN 155..1219
FT /note="Collagen alpha-1(III) chain"
FT /id="PRO_0000005744"
FT PROPEP 1220..1464
FT /note="C-terminal propeptide"
FT /id="PRO_0000005745"
FT DOMAIN 31..90
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1230..1464
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 97..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..169
FT /note="Nonhelical region (N-terminal)"
FT REGION 170..1195
FT /note="Triple-helical region"
FT COMPBIAS 97..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 283
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 859
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 976
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1093
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1105
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 262
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 1195
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1196
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1260..1292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1266
FT /note="Interchain (with C-1283)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1283
FT /note="Interchain (with C-1266)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1300..1462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1370..1415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
SQ SEQUENCE 1464 AA; 138943 MW; 2104EC27A886090B CRC64;
MMSFVQSGTW FLLTLLHPTL ILAQQSNVDE LGCSHLGQSY ESRDVWKPEP CQICVCDSGS
VLCDDIICDE EPLDCPNPEI PFGECCAICP QPSTPAPVLP DGHGPQGPKG DPGPPGIPGR
NGDPGLPGQP GLPGPPGSPG ICESCPTGGQ NYSPQFDSYD VKSGVGGMGG YPGPAGPPGP
PGPPGSSGHP GSPGSPGYQG PPGEPGQAGP AGPPGPPGAL GPAGPAGKDG ESGRPGRPGE
RGLPGPPGIK GPAGMPGFPG MKGHRGFDGR NGEKGETGAP GLKGENGLPG DNGAPGPMGP
RGAPGERGRP GLPGAAGARG NDGARGSDGQ PGPPGPPGTA GFPGSPGAKG EVGPAGSPGS
NGSPGQRGEP GPQGHAGAQG PPGPPGNNGS PGGKGEMGPA GIPGAPGLIG ARGPPGPAGT
NGIPGTRGPS GEPGKNGAKG EPGARGERGE AGSPGIPGPK GEDGKDGSPG EPGANGLPGA
AGERGPSGFR GPAGPNGIPG EKGPPGERGG PGPAGPRGVA GEPGRDGTPG GPGIRGMPGS
PGGPGNDGKP GPPGSQGESG RPGPPGPSGP RGQPGVMGFP GPKGNDGAPG KNGERGGPGG
PGLPGPAGKN GETGPQGPPG PTGPAGDKGD SGPPGPQGLQ GIPGTGGPPG ENGKPGEPGP
KGEVGAPGAP GGKGDSGAPG ERGPPGTAGI PGARGGAGPP GPEGGKGPAG PPGPPGASGS
PGLQGMPGER GGPGSPGPKG EKGEPGGAGA DGVPGKDGPR GPAGPIGPPG PAGQPGDKGE
GGSPGLPGIA GPRGGPGERG EHGPPGPAGF PGAPGQNGEP GAKGERGAPG EKGEGGPPGP
AGPTGSSGPA GPPGPQGVKG ERGSPGGPGT AGFPGGRGLP GPPGNNGNPG PPGPSGAPGK
DGPPGPAGNS GSPGNPGIAG PKGDAGQPGE KGPPGAQGPP GSPGPLGIAG LTGARGLAGP
PGMPGPRGSP GPQGIKGESG KPGASGHNGE RGPPGPQGLP GQPGTAGEPG RDGNPGSDGQ
PGRDGSPGGK GDRGENGSPG APGAPGHPGP PGPVGPSGKS GDRGETGPAG PSGAPGPAGA
RGAPGPQGPR GDKGETGERG SNGIKGHRGF PGNPGPPGSP GAAGHQGAIG SPGPAGPRGP
VGPHGPPGKD GTSGHPGPIG PPGPRGNRGE RGSEGSPGHP GQPGPPGPPG APGPCCGGGA
AAIAGVGGEK SGGFSPYYGD DPMDFKINTE EIMSSLKSVN GQIESLISPD GSRKNPARNC
RDLKFCHPEL KSGEYWVDPN QGCKMDAIKV FCNMETGETC INASPMTVPR KHWWTDSGAE
KKHVWFGESM NGGFQFSYGP PDLPEDVVDV QLAFLRLLSS RASQNITYHC KNSIAYMDQA
SGNVKKSLKL MGSNEGEFKA EGNSKFTYTV LEDGCTKHTG EWSKTVFEYQ TRKAMRLPII
DIAPYDIGGP DQEFGVDIGP VCFL
