CO5A2_MOUSE
ID CO5A2_MOUSE Reviewed; 1497 AA.
AC Q3U962; Q3TVR2; Q3UHK7; Q3UTT4; Q3V1J6; Q61431; Q7TMS0; Q80VS8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Collagen alpha-2(V) chain;
DE Flags: Precursor;
GN Name=Col5a2 {ECO:0000312|MGI:MGI:88458};
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] {ECO:0000305, ECO:0000312|EMBL:AAA37440.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAA37440.1};
RX PubMed=1297453; DOI=10.1002/aja.1001950205;
RA Andrikopoulos K., Suzuki H.R., Solursh M., Ramirez F.;
RT "Localization of pro-alpha 2(V) collagen transcripts in the tissues of the
RT developing mouse embryo.";
RL Dev. Dyn. 195:113-120(1992).
RN [2] {ECO:0000312|EMBL:BAE30805.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE30805.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE30805.1},
RC Cerebellum {ECO:0000312|EMBL:BAE23896.1},
RC Embryo {ECO:0000312|EMBL:BAE27775.1},
RC Placenta {ECO:0000312|EMBL:BAE27850.1}, and
RC Skin {ECO:0000312|EMBL:BAE21154.1};
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] {ECO:0000312|EMBL:AAH55077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He {ECO:0000312|EMBL:AAH55077.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH43696.1}, and
RC Mesenchymal stem cell {ECO:0000312|EMBL:AAH55077.1};
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=7704020; DOI=10.1038/ng0195-31;
RA Andrikopoulos K., Liu X., Keene D.R., Jaenisch R., Ramirez F.;
RT "Targeted mutation in the col5a2 gene reveals a regulatory role for type V
RT collagen during matrix assembly.";
RL Nat. Genet. 9:31-36(1995).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9642685; DOI=10.1007/bf03401742;
RA Phelps R.G., Murai C., Saito S., Hatakeyama A., Andrikopoulos K.,
RA Kasturi K.N., Bona C.A.;
RT "Effect of targeted mutation in collagen V alpha 2 gene on development of
RT cutaneous hyperplasia in tight skin mice.";
RL Mol. Med. 4:356-360(1998).
RN [6] {ECO:0000305}
RP SUBUNIT.
RX PubMed=15199158; DOI=10.1128/mcb.24.13.6049-6057.2004;
RA Chanut-Delalande H., Bonod-Bidaud C., Cogne S., Malbouyres M., Ramirez F.,
RA Fichard A., Ruggiero F.;
RT "Development of a functional skin matrix requires deposition of collagen V
RT heterotrimers.";
RL Mol. Cell. Biol. 24:6049-6057(2004).
CC -!- FUNCTION: Type V collagen is a member of group I collagen (fibrillar
CC forming collagen). It is a minor connective tissue component of nearly
CC ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate,
CC thrombospondin, heparin, and insulin. Type V collagen is a key
CC determinant in the assembly of tissue-specific matrices.
CC {ECO:0000250|UniProtKB:P05997, ECO:0000269|PubMed:1297453,
CC ECO:0000269|PubMed:7704020, ECO:0000269|PubMed:9642685}.
CC -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains expressed
CC in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one
CC alpha 3(V) chains with a more limited distribution of expression.
CC {ECO:0000250|UniProtKB:P05997, ECO:0000269|PubMed:15199158}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos from 9 days of gestation
CC onward. In 12.5 dpc embryos, low and diffuse level of expression was
CC observed in the peritoneal membranes and intestinal and craniofacial
CC mesenchymes. By 16.5 dpc, expression is higher and exhibits a more
CC restricted accumulation in primary ossified regions, perichondrium,
CC joints, tendon, atrioventricular valve of heart, and in selected
CC portions of the head. {ECO:0000269|PubMed:1297453}.
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: Prolines at the third position of the tripeptide repeating unit
CC (G-X-P) are hydroxylated in some or all of the chains. Probably 3-
CC hydroxylated on prolines by LEPREL1.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mice homozygous for the targeted deletion of the N-
CC terminal telopeptide segment of the COL5A2 chain show poor survival
CC rates, possibly because of complications from spinal deformities, and
CC exhibit skin and eye abnormalities caused by disorganized type I
CC collagen fibrils. {ECO:0000269|PubMed:15199158,
CC ECO:0000269|PubMed:7704020, ECO:0000269|PubMed:9642685}.
CC -!- MISCELLANEOUS: The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer makes
CC a critical contribution to fibrillogenesis, basement membrane
CC organization, and cell viability, and may play a possible role in the
CC development of a functional skin matrix. {ECO:0000269|PubMed:15199158}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE23896.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L02918; AAA37440.1; -; mRNA.
DR EMBL; AK132413; BAE21154.1; -; mRNA.
DR EMBL; AK139130; BAE23896.1; ALT_INIT; mRNA.
DR EMBL; AK147220; BAE27775.1; -; mRNA.
DR EMBL; AK147328; BAE27850.1; -; mRNA.
DR EMBL; AK151929; BAE30805.1; -; mRNA.
DR EMBL; AK160008; BAE35556.1; -; mRNA.
DR EMBL; BC043696; AAH43696.1; -; mRNA.
DR EMBL; BC055077; AAH55077.1; -; mRNA.
DR CCDS; CCDS35555.1; -.
DR PIR; I49607; I49607.
DR RefSeq; NP_031763.2; NM_007737.2.
DR AlphaFoldDB; Q3U962; -.
DR SMR; Q3U962; -.
DR BioGRID; 198822; 8.
DR ComplexPortal; CPX-2962; Collagen type V trimer variant 1.
DR ComplexPortal; CPX-2963; Collagen type V trimer variant 2.
DR ComplexPortal; CPX-2976; Collagen type XI trimer variant 2.
DR ComplexPortal; CPX-2977; Collagen type XI trimer variant 3.
DR STRING; 10090.ENSMUSP00000083620; -.
DR GlyGen; Q3U962; 2 sites.
DR iPTMnet; Q3U962; -.
DR PhosphoSitePlus; Q3U962; -.
DR CPTAC; non-CPTAC-4024; -.
DR MaxQB; Q3U962; -.
DR PaxDb; Q3U962; -.
DR PeptideAtlas; Q3U962; -.
DR PRIDE; Q3U962; -.
DR ProteomicsDB; 283544; -.
DR Antibodypedia; 34019; 169 antibodies from 28 providers.
DR DNASU; 12832; -.
DR Ensembl; ENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
DR GeneID; 12832; -.
DR KEGG; mmu:12832; -.
DR UCSC; uc007awr.1; mouse.
DR CTD; 1290; -.
DR MGI; MGI:88458; Col5a2.
DR VEuPathDB; HostDB:ENSMUSG00000026042; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155675; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; Q3U962; -.
DR OMA; MANWAEA; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; Q3U962; -.
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-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; 12832; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Col5a2; mouse.
DR PRO; PR:Q3U962; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U962; protein.
DR Bgee; ENSMUSG00000026042; Expressed in vault of skull and 255 other tissues.
DR Genevisible; Q3U962; MM.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005588; C:collagen type V trimer; ISO:MGI.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048592; P:eye morphogenesis; ISO:MGI.
DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; ISO:MGI.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1227
FT /note="Collagen alpha-2(V) chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283768"
FT PROPEP 1228..1497
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283769"
FT DOMAIN 38..96
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1264..1497
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 103..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 141..143
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 504..506
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 942..944
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1065..1067
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1068..1070
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1125..1127
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1134..1136
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 166..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 288
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 291
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 294
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 609
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 615
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 1260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1294..1326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1334..1495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1403..1448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 20
FT /note="Y -> D (in Ref. 2; BAE23896)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> P (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> R (in Ref. 2; BAE27850)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="V -> M (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="Q -> V (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="V -> A (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="A -> R (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="T -> H (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> R (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="P -> A (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="L -> V (in Ref. 1; AAA37440 and 3; AAH55077)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="Q -> A (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 809..813
FT /note="PTGEK -> LLGAP (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="P -> S (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001..1002
FT /note="ER -> VT (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="T -> A (in Ref. 3; AAH55077)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="G -> V (in Ref. 2; BAE21154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="P -> S (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
FT CONFLICT 1337
FT /note="A -> T (in Ref. 3; AAH55077)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="L -> F (in Ref. 1; AAA37440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1497 AA; 145018 MW; CAAE15514984DB41 CRC64;
MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR DIWKPSPCQI
CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG GDTSFGRGRK GQKGEPGLVP
VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP
GPDGMSRPFS AQMAGLDEKS GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP
GEPGPMGPIG SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR
GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA PGKRGAHGMP
GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG QRGETGPPGP AGSQGLPGAV
GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK
GEPGPHGIQG PIGPPGEEGK RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ
GERGPVGSSG PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP
GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP SGPVGPPGLA
GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG AVGPLGPRGE RGNPGERGEP
GITGLPGEKG MAGGHGPDGP KGNPGPTGTI GDTGPPGLQG MPGERGIAGT PGPKGDRGGI
GEKGAEGTAG NDGARGLPGP LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT
GAVGFAGPQG PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ
GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR VGDRGPAGPP
GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG ERGMPGLPGP AGTPGKVGPT
GATGDKGPPG PVGPPGSNGP VGEPGPEGPA GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ
GAPGTPGPVG APGDAGQRGE PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK
GHRGFTGLQG LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR
GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT EDQAAPDDTN
KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC HPTKQSGEYW IDPNQGSAED
AIKVYCNMET GETCISANPA SVPRKTWWAS KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT
AITQMTFLRL LSKEASQNLT YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR
YTVLQDTCSK RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM
