COGA1_HUMAN
ID COGA1_HUMAN Reviewed; 1604 AA.
AC Q07092; Q16593; Q59F89; Q71RG9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Collagen alpha-1(XVI) chain;
DE Flags: Precursor;
GN Name=COL16A1; ORFNames=FP1572;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-62.
RC TISSUE=Fibroblast;
RX PubMed=1631157; DOI=10.1073/pnas.89.14.6565;
RA Pan T.-C., Zhang R.-Z., Mattei M.-G., Timpl R., Chu M.-L.;
RT "Cloning and chromosomal location of human alpha 1(XVI) collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6565-6569(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP PROTEIN SEQUENCE OF 22-33, SUBUNIT, AND GLYCOSYLATION.
RX PubMed=7882999; DOI=10.1111/j.1432-1033.1995.tb20245.x;
RA Tillet E., Mann K., Nischt R., Pan T.-C., Chu M.-L., Timpl R.;
RT "Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for
RT processing of the N-terminal globular domain.";
RL Eur. J. Biochem. 228:160-168(1995).
RN [4]
RP PROTEIN SEQUENCE OF 22-30; 257-265 AND 941-950, SUBUNIT, INTERACTION WITH
RP FBN1 AND FN1, AND GLYCOSYLATION.
RX PubMed=15165854; DOI=10.1016/j.jmb.2004.03.042;
RA Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M.,
RA Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S.;
RT "Molecular structure and interaction of recombinant human type XVI
RT collagen.";
RL J. Mol. Biol. 339:835-853(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-1604 (ISOFORM 2).
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 403-849.
RC TISSUE=Placenta;
RA Kimura S.;
RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 418-1604 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1284248; DOI=10.1093/oxfordjournals.jbchem.a123989;
RA Yamaguchi N., Kimura S., McBride O.W., Hori H., Yamada Y., Kanamori T.,
RA Yamakoshi H., Nagai Y.;
RT "Molecular cloning and partial characterization of a novel collagen chain,
RT alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-
RT containing non-collagenous segments.";
RL J. Biochem. 112:856-863(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1387-1604.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9022684; DOI=10.1111/j.1432-1033.1996.0576r.x;
RA Grassel S., Timpl R., Tan E.M.L., Chu M.-L.;
RT "Biosynthesis and processing of type XVI collagen in human fibroblasts and
RT smooth muscle cells.";
RL Eur. J. Biochem. 242:576-584(1996).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12782140; DOI=10.1016/s0945-053x(03)00008-8;
RA Kassner A., Hansen U., Miosge N., Reinhardt D.P., Aigner T.,
RA Bruckner-Tuderman L., Bruckner P., Grassel S.;
RT "Discrete integration of collagen XVI into tissue-specific collagen fibrils
RT or beaded microfibrils.";
RL Matrix Biol. 22:131-143(2003).
RN [11]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH INTEGRIN ALPHA-1/BETA-1 AND
RP INTEGRIN ALPHA-2/BETA-1.
RX PubMed=16754661; DOI=10.1074/jbc.m509942200;
RA Eble J.A., Kassner A., Niland S., Morgelin M., Grifka J., Grassel S.;
RT "Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-
RT terminal domains.";
RL J. Biol. Chem. 281:25745-25756(2006).
CC -!- FUNCTION: Involved in mediating cell attachment and inducing integrin-
CC mediated cellular reactions, such as cell spreading and alterations in
CC cell morphology. {ECO:0000269|PubMed:16754661}.
CC -!- SUBUNIT: Homotrimer. Interacts with FBN1, fibronectin and integrins
CC ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique
CC site within COL16A1 located close to its C-terminal end between
CC collagenous domains COL1-COL3. {ECO:0000269|PubMed:15165854,
CC ECO:0000269|PubMed:16754661, ECO:0000269|PubMed:7882999,
CC ECO:0000269|PubMed:9022684}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:9022684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07092-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07092-2; Sequence=VSP_024259, VSP_024260;
CC -!- TISSUE SPECIFICITY: In papillary dermis, is a component of specialized
CC fibrillin-1-containing microfibrils, whereas in territorial cartilage
CC matrix, it is localized to a discrete population of thin, weakly banded
CC collagen fibrils in association with other collagens (at protein
CC level). In the placenta, where it is found in the amnion, a membranous
CC tissue lining the amniotic cavity. Within the amnion, it is found in an
CC acellular, relatively dense layer of a complex network of reticular
CC fibers. Also located to a fibroblast layer beneath this dense layer.
CC Exists in tissues in association with other types of collagen.
CC {ECO:0000269|PubMed:12782140}.
CC -!- DEVELOPMENTAL STAGE: Transiently elevated expression during gestation,
CC and decrease at term.
CC -!- DOMAIN: This sequence defines eighteen different domains, nine triple-
CC helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10
CC to NC1). The numerous interruptions in the triple helix may make this
CC molecule either elastic or flexible.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15165854,
CC ECO:0000269|PubMed:7882999}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/COL16A1ID44542ch1p35.html";
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DR EMBL; M92642; AAA58427.1; -; mRNA.
DR EMBL; AC114488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209571; BAD92808.1; -; mRNA.
DR EMBL; X14963; CAA33085.1; -; mRNA.
DR EMBL; X15038; CAA33142.1; -; mRNA.
DR EMBL; S57132; AAB25797.1; -; mRNA.
DR EMBL; AF370368; AAQ15204.1; -; mRNA.
DR CCDS; CCDS41297.1; -. [Q07092-1]
DR PIR; S23810; S23810.
DR RefSeq; NP_001847.3; NM_001856.3. [Q07092-1]
DR AlphaFoldDB; Q07092; -.
DR BioGRID; 107703; 18.
DR ComplexPortal; CPX-1757; Collagen type XVI trimer.
DR IntAct; Q07092; 5.
DR MINT; Q07092; -.
DR STRING; 9606.ENSP00000362776; -.
DR GlyConnect; 1133; 1 N-Linked glycan (1 site).
DR GlyGen; Q07092; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q07092; -.
DR PhosphoSitePlus; Q07092; -.
DR BioMuta; COL16A1; -.
DR DMDM; 143811380; -.
DR EPD; Q07092; -.
DR jPOST; Q07092; -.
DR MassIVE; Q07092; -.
DR MaxQB; Q07092; -.
DR PaxDb; Q07092; -.
DR PeptideAtlas; Q07092; -.
DR PRIDE; Q07092; -.
DR ProteomicsDB; 58503; -. [Q07092-1]
DR ProteomicsDB; 58504; -. [Q07092-2]
DR Antibodypedia; 8436; 65 antibodies from 19 providers.
DR DNASU; 1307; -.
DR Ensembl; ENST00000373672.8; ENSP00000362776.3; ENSG00000084636.18. [Q07092-1]
DR GeneID; 1307; -.
DR KEGG; hsa:1307; -.
DR MANE-Select; ENST00000373672.8; ENSP00000362776.3; NM_001856.4; NP_001847.3.
DR UCSC; uc001btk.2; human. [Q07092-1]
DR CTD; 1307; -.
DR DisGeNET; 1307; -.
DR GeneCards; COL16A1; -.
DR HGNC; HGNC:2193; COL16A1.
DR HPA; ENSG00000084636; Low tissue specificity.
DR MIM; 120326; gene.
DR neXtProt; NX_Q07092; -.
DR OpenTargets; ENSG00000084636; -.
DR PharmGKB; PA26709; -.
DR VEuPathDB; HostDB:ENSG00000084636; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161782; -.
DR HOGENOM; CLU_001074_2_2_1; -.
DR InParanoid; Q07092; -.
DR OMA; MGNSWQP; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; Q07092; -.
DR TreeFam; TF332900; -.
DR PathwayCommons; Q07092; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q07092; -.
DR BioGRID-ORCS; 1307; 6 hits in 1061 CRISPR screens.
DR ChiTaRS; COL16A1; human.
DR GeneWiki; Collagen,_type_XVI,_alpha_1; -.
DR GenomeRNAi; 1307; -.
DR Pharos; Q07092; Tbio.
DR PRO; PR:Q07092; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q07092; protein.
DR Bgee; ENSG00000084636; Expressed in tibia and 196 other tissues.
DR ExpressionAtlas; Q07092; baseline and differential.
DR Genevisible; Q07092; HS.
DR GO; GO:0005588; C:collagen type V trimer; IBA:GO_Central.
DR GO; GO:0005597; C:collagen type XVI trimer; TAS:ProtInc.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:CACAO.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0033622; P:integrin activation; IDA:CACAO.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:CACAO.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 6.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15165854,
FT ECO:0000269|PubMed:7882999"
FT CHAIN 22..1604
FT /note="Collagen alpha-1(XVI) chain"
FT /id="PRO_0000005792"
FT DOMAIN 50..231
FT /note="Laminin G-like"
FT DOMAIN 375..423
FT /note="Collagen-like 1"
FT DOMAIN 573..633
FT /note="Collagen-like 2"
FT DOMAIN 667..721
FT /note="Collagen-like 3"
FT DOMAIN 788..840
FT /note="Collagen-like 4"
FT DOMAIN 888..938
FT /note="Collagen-like 5"
FT DOMAIN 1018..1075
FT /note="Collagen-like 6"
FT DOMAIN 1472..1524
FT /note="Collagen-like 7"
FT DOMAIN 1528..1576
FT /note="Collagen-like 8"
FT REGION 232..374
FT /note="Nonhelical region 10 (NC10)"
FT REGION 301..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..506
FT /note="Triple-helical region 9 (COL9) with 3 imperfections"
FT REGION 507..521
FT /note="Nonhelical region 9 (NC9)"
FT REGION 522..555
FT /note="Triple-helical region 8 (COL8) with 1 imperfection"
FT REGION 556..572
FT /note="Nonhelical region 8 (NC8)"
FT REGION 573..631
FT /note="Triple-helical region 7 (COL7) with 1 imperfection"
FT REGION 604..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..652
FT /note="Nonhelical region 7 (NC7)"
FT REGION 653..723
FT /note="Triple-helical region 6 (COL6) with 1 imperfection"
FT REGION 724..738
FT /note="Nonhelical region 6 (NC6)"
FT REGION 739..876
FT /note="Triple-helical region 5 (COL5) with 3 imperfections"
FT REGION 877..887
FT /note="Nonhelical region 5 (NC5)"
FT REGION 888..939
FT /note="Triple-helical region 4 (COL4) with 2 imperfections"
FT REGION 940..973
FT /note="Nonhelical region 4 (NC4)"
FT REGION 974..988
FT /note="Triple-helical region 3 (COL3)"
FT REGION 989..1011
FT /note="Nonhelical region 3 (NC3)"
FT REGION 1001..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1433
FT /note="Triple-helical region 2 (COL2) with 2 imperfections"
FT REGION 1434..1472
FT /note="Nonhelical region 2 (NC2)"
FT REGION 1468..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1578
FT /note="Triple-helical region 1 (COL1) with 2 imperfections"
FT REGION 1579..1604
FT /note="Nonhelical region 1 (NC1)"
FT MOTIF 540..542
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1006..1008
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1227..1229
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 448..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1052
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_024259"
FT VAR_SEQ 1161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_024260"
FT VARIANT 62
FT /note="T -> K (in dbSNP:rs2228552)"
FT /evidence="ECO:0000269|PubMed:1631157"
FT /id="VAR_031440"
FT VARIANT 418
FT /note="R -> Q (in dbSNP:rs6699645)"
FT /id="VAR_048778"
FT VARIANT 745
FT /note="G -> S (in dbSNP:rs34770879)"
FT /id="VAR_048779"
FT CONFLICT 419
FT /note="D -> G (in Ref. 7; AAB25797)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..421
FT /note="GR -> A (in Ref. 1; AAA58427)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="P -> R (in Ref. 1; AAA58427)"
FT /evidence="ECO:0000305"
FT CONFLICT 848..849
FT /note="RD -> VM (in Ref. 6; CAA33142/CAA33085)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="P -> T (in Ref. 1; AAA58427)"
FT /evidence="ECO:0000305"
FT CONFLICT 1164
FT /note="P -> T (in Ref. 1; AAA58427)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166
FT /note="P -> S (in Ref. 1; AAA58427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1604 AA; 157751 MW; 5FAA1950DFC6CA3C CRC64;
MWVSWAPGLW LLGLWATFGH GANTGAQCPP SQQEGLKLEH SSSLPANVTG FNLIHRLSLM
KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF ALVLTLLLKK HTHQKTWYLF
QVTDANGYPQ ISLEVNSQER SLELRAQGQD GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA
SVHVDCSSAS SQPLGPRRPM RPVGHVFLGL DAEQGKPVSF DLQQVHIYCD PELVLEEGCC
EILPAGCPPE TSKARRDTQS NELIEINPQS EGKVYTRCFC LEEPQNSEVD AQLTGRISQK
AERGAKVHQE TAADECPPCV HGARDSNVTL APSGPKGGKG ERGLPGPPGS KGEKGARGND
CVRISPDAPL QCAEGPKGEK GESGALGPSG LPGSTGEKGQ KGEKGDGGIK GVPGKPGRDG
RPGEICVIGP KGQKGDPGFV GPEGLAGEPG PPGLPGPPGI GLPGTPGDPG GPPGPKGDKG
SSGIPGKEGP GGKPGKPGVK GEKGDPCEVC PTLPEGFQNF VGLPGKPGPK GEPGDPVPAR
GDPGIQGIKG EKGEPCLSCS SVVGAQHLVS STGASGDVGS PGFGLPGLPG RAGVPGLKGE
KGNFGEAGPA GSPGPPGPVG PAGIKGAKGE PCEPCPALSN LQDGDVRVVA LPGPSGEKGE
PGPPGFGLPG KQGKAGERGL KGQKGDAGNP GDPGTPGTTG RPGLSGEPGV QGPAGPKGEK
GDGCTACPSL QGTVTDMAGR PGQPGPKGEQ GPEGVGRPGK PGQPGLPGVQ GPPGLKGVQG
EPGPPGRGVQ GPQGEPGAPG LPGIQGLPGP RGPPGPTGEK GAQGSPGVKG ATGPVGPPGA
SVSGPPGRDG QQGQTGLRGT PGEKGPRGEK GEPGECSCPS QGDLIFSGMP GAPGLWMGSS
WQPGPQGPPG IPGPPGPPGV PGLQGVPGNN GLPGQPGLTA ELGSLPIEQH LLKSICGDCV
QGQRAHPGYL VEKGEKGDQG IPGVPGLDNC AQCFLSLERP RAEEARGDNS EGDPGCVGSP
GLPGPPGLPG QRGEEGPPGM RGSPGPPGPI GPPGFPGAVG SPGLPGLQGE RGLTGLTGDK
GEPGPPGQPG YPGATGPPGL PGIKGERGYT GSAGEKGEPG PPGSEGLPGP PGPAGPRGER
GPQGNSGEKG DQGFQGQPGF PGPPGPPGFP GKVGSPGPPG PQAEKGSEGI RGPSGLPGSP
GPPGPPGIQG PAGLDGLDGK DGKPGLRGDP GPAGPPGLMG PPGFKGKTGH PGLPGPKGDC
GKPGPPGSTG RPGAEGEPGA MGPQGRPGPP GHVGPPGPPG QPGPAGISAV GLKGDRGATG
ERGLAGLPGQ PGPPGHPGPP GEPGTDGAAG KEGPPGKQGF YGPPGPKGDP GAAGQKGQAG
EKGRAGMPGG PGKSGSMGPV GPPGPAGERG HPGAPGPSGS PGLPGVPGSM GDMVNYDEIK
RFIRQEIIKM FDERMAYYTS RMQFPMEMAA APGRPGPPGK DGAPGRPGAP GSPGLPGQIG
REGRQGLPGV RGLPGTKGEK GDIGIGIAGE NGLPGPPGPQ GPPGYGKMGA TGPMGQQGIP
GIPGPPGPMG QPGKAGHCNP SDCFGAMPME QQYPPMKTMK GPFG
