ID   CO6A5_HUMAN             Reviewed;        2615 AA.
AC   A8TX70; A9J6L2; A9J6L4; A9J6L6; A9J6L7; A9J6M0; A9J6M1; A9J6M2;
AC   B5MEA7; Q6ZW26; Q8NA36;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Collagen alpha-5(VI) chain;
DE   AltName: Full=Collagen alpha-1(XXIX) chain;
DE   AltName: Full=von Willebrand factor A domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=COL6A5; Synonyms=COL29A1, VWA4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   POSSIBLE INVOLVEMENT IN ATOPIC DERMATITIS.
RC   TISSUE=Skin;
RX   PubMed=17850181; DOI=10.1371/journal.pbio.0050242;
RA   Soederhaell C., Marenholz I., Kerscher T., Rueschendorf F.,
RA   Esparza-Gordillo J., Worm M., Gruber C., Mayr G., Albrecht M.,
RA   Rohde K., Schulz H., Wahn U., Hubner N., Lee Y.-A.;
RT   "Variants in a novel epidermal collagen gene (COL29A1) are associated
RT   with atopic dermatitis.";
RL   PLoS Biol. 5:1952-1961(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-455;
RP   PRO-1280; ARG-2188 AND ASP-2205.
RX   PubMed=18276594; DOI=10.1074/jbc.M709540200;
RA   Gara S.K., Grumati P., Urciuolo A., Bonaldo P., Kobbe B., Koch M.,
RA   Paulsson M., Wagener R.;
RT   "Three novel collagen VI chains with high homology to the alpha 3
RT   chain.";
RL   J. Biol. Chem. 283:10658-10670(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1900-2615 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2096-2615 (ISOFORM 1), AND
RP   VARIANTS ARG-2188 AND ASP-2205.
RC   TISSUE=Lung, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Trimers composed of three different chains: alpha-1(VI),
CC       alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}. Note=Deposed in the extracellular matrix of
CC       skeletal muscle. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A8TX70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A8TX70-2; Sequence=VSP_033912, VSP_033913;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in skin, followed by lung, small
CC       intestine, colon and testis. In skin, it is expressed in the
CC       epidermis with strongest staining in suprabasal viable layers. In
CC       ATOD patients, it is absent in the most differentiated upper
CC       spinous and granular layers (at protein level).
CC       {ECO:0000269|PubMed:17850181}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains.
CC       {ECO:0000250}.
CC   -!- DISEASE: Note=Patients affected by atopic dermatitis display an
CC       abnormal distribution of COL29A1 mRNA and protein in skin
CC       suggesting that COL29A1 may be involved in the pathogenesis of the
CC       disease.
CC   -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC04092.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAC04092.1; Type=Frameshift; Positions=2591; Evidence={ECO:0000305};
CC       Sequence=BAC85681.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EU085556; ABW81241.1; -; mRNA.
DR   EMBL; AM906078; CAP19997.1; -; mRNA.
DR   EMBL; AM906079; CAP19998.1; -; mRNA.
DR   EMBL; AM906080; CAP19999.1; -; mRNA.
DR   EMBL; AM906081; CAP20000.1; -; mRNA.
DR   EMBL; AM906082; CAP20001.1; -; mRNA.
DR   EMBL; AM906083; CAP20002.1; -; mRNA.
DR   EMBL; AM906084; CAP20003.1; -; mRNA.
DR   EMBL; AC093004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK093199; BAC04092.1; ALT_SEQ; mRNA.
DR   EMBL; AK123718; BAC85681.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001265227.1; NM_001278298.1.
DR   RefSeq; NP_694996.5; NM_153264.6. [A8TX70-2]
DR   UniGene; Hs.205403; -.
DR   ProteinModelPortal; A8TX70; -.
DR   SMR; A8TX70; -.
DR   BioGrid; 129134; 1.
DR   STRING; 9606.ENSP00000265379; -.
DR   ChEMBL; CHEMBL2364188; -.
DR   iPTMnet; A8TX70; -.
DR   PhosphoSitePlus; A8TX70; -.
DR   BioMuta; COL6A5; -.
DR   EPD; A8TX70; -.
DR   jPOST; A8TX70; -.
DR   PaxDb; A8TX70; -.
DR   PRIDE; A8TX70; -.
DR   ProteomicsDB; 2486; -.
DR   ProteomicsDB; 2487; -. [A8TX70-2]
DR   DNASU; 256076; -.
DR   Ensembl; ENST00000312481; ENSP00000309762; ENSG00000172752. [A8TX70-1]
DR   GeneID; 256076; -.
DR   KEGG; hsa:256076; -.
DR   UCSC; uc062ntw.1; human. [A8TX70-1]
DR   CTD; 256076; -.
DR   DisGeNET; 256076; -.
DR   EuPathDB; HostDB:ENSG00000172752.14; -.
DR   GeneCards; COL6A5; -.
DR   H-InvDB; HIX0003678; -.
DR   HGNC; HGNC:26674; COL6A5.
DR   HPA; HPA043138; -.
DR   MIM; 611916; gene.
DR   neXtProt; NX_A8TX70; -.
DR   OpenTargets; ENSG00000172752; -.
DR   PharmGKB; PA165696956; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   eggNOG; ENOG410XNMM; LUCA.
DR   GeneTree; ENSGT00940000162990; -.
DR   HOVERGEN; HBG107743; -.
DR   InParanoid; A8TX70; -.
DR   KO; K06238; -.
DR   OMA; KCFPNAC; -.
DR   OrthoDB; 1049829at2759; -.
DR   PhylomeDB; A8TX70; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-419037; NCAM1 interactions.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   GenomeRNAi; 256076; -.
DR   PRO; PR:A8TX70; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000172752; Expressed in 38 organ(s), highest expression level in upper lobe of left lung.
DR   ExpressionAtlas; A8TX70; baseline and differential.
DR   Genevisible; A8TX70; HS.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; -; 9.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF00092; VWA; 9.
DR   SMART; SM00327; VWA; 9.
DR   SUPFAM; SSF53300; SSF53300; 10.
DR   PROSITE; PS50234; VWFA; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Collagen; Complete proteome;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   2615       Collagen alpha-5(VI) chain.
FT                                /FTId=PRO_5000294475.
FT   DOMAIN       30    209       VWFA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      236    413       VWFA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      442    612       VWFA 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      628    797       VWFA 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      814    987       VWFA 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1005   1178       VWFA 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1194   1376       VWFA 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1395   1446       Collagen-like 1. {ECO:0000255}.
FT   DOMAIN     1434   1490       Collagen-like 2. {ECO:0000255}.
FT   DOMAIN     1464   1520       Collagen-like 3. {ECO:0000255}.
FT   DOMAIN     1524   1580       Collagen-like 4. {ECO:0000255}.
FT   DOMAIN     1579   1629       Collagen-like 5. {ECO:0000255}.
FT   DOMAIN     1674   1729       Collagen-like 6. {ECO:0000255}.
FT   DOMAIN     1758   1965       VWFA 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1963   2154       VWFA 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     2291   2487       VWFA 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   REGION       19   1394       Nonhelical region.
FT   REGION     1395   1728       Triple-helical region.
FT   REGION     1729   2615       Nonhelical region.
FT   MOTIF      1430   1432       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    201    201       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    260    260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    835    835       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2509   2509       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ    2526   2526       L -> W (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_033912.
FT   VAR_SEQ    2527   2615       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_033913.
FT   VARIANT     455    455       E -> K (in dbSNP:rs1453241).
FT                                {ECO:0000269|PubMed:18276594}.
FT                                /FTId=VAR_059234.
FT   VARIANT     641    641       N -> H (in dbSNP:rs9882852).
FT                                /FTId=VAR_059235.
FT   VARIANT     805    805       H -> R (in dbSNP:rs16827168).
FT                                /FTId=VAR_059236.
FT   VARIANT     982    982       D -> G (in dbSNP:rs11917356).
FT                                /FTId=VAR_059237.
FT   VARIANT    1114   1114       I -> M (in dbSNP:rs1353613).
FT                                /FTId=VAR_059238.
FT   VARIANT    1280   1280       T -> P (in dbSNP:rs12488457).
FT                                {ECO:0000269|PubMed:18276594}.
FT                                /FTId=VAR_059239.
FT   VARIANT    1477   1477       C -> S (in dbSNP:rs1497312).
FT                                /FTId=VAR_059240.
FT   VARIANT    1589   1589       S -> P (in dbSNP:rs16827497).
FT                                /FTId=VAR_059241.
FT   VARIANT    2175   2175       D -> N (in dbSNP:rs60021408).
FT                                /FTId=VAR_061119.
FT   VARIANT    2188   2188       Q -> R (in dbSNP:rs9883988).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:18276594}.
FT                                /FTId=VAR_043607.
FT   VARIANT    2205   2205       G -> D (in dbSNP:rs819085).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:18276594}.
FT                                /FTId=VAR_043608.
FT   CONFLICT   2482   2482       K -> R (in Ref. 4; BAC04092).
FT                                {ECO:0000305}.
FT   CONFLICT   2512   2512       S -> P (in Ref. 4; BAC04092).
FT                                {ECO:0000305}.
FT   CONFLICT   2560   2560       S -> N (in Ref. 2; CAP20002/CAP20003 and
FT                                4; BAC04092). {ECO:0000305}.
SQ   SEQUENCE   2615 AA;  289926 MW;  745874018AC47EAF CRC64;
     MKILLIIFVL IIWTETLADQ SPGPGPVYAD VVFLVDSSDH LGPKSFPFVK TFINKMINSL
     PIEANKYRVA LAQYSDEFHS EFHLSTFKGR SPMLNHLKKN FQFIGGSLQI GKALQEAHRT
     YFSAPINGRD RKQFPPILVV LASAESEDEV EEASKALQKD GVKIISVGVQ KASEENLKAM
     ATSHFHFNLR TIRDLSTFSQ NMTQIIKDVT KYKEGAVDAD MQVHFPISCQ KDSLADLVFL
     VDESLGTGGN LRHLQTFLEN ITSSMDVKEN CMRLGLMSYS NSAKTISFLK SSTTQSEFQQ
     QIKNLSIQVG KSNTGAAIDQ MRRDGFSESY GSRRAQGVPQ IAVLVTHRPS DDEVHDAALN
     LRLEDVNVFA LSIQGANNTQ LEEIVSYPPE QTISTLKSYA DLETYSTKFL KKLQNEIWSQ
     ISTYAEQRNL DKTGCVDTKE ADIHFLIDGS SSIQEKQFEQ IKRFMLEVTE MFSIGPDKVR
     VGVVQYSDDT EVEFYITDYS NDIDLRKAIF NIKQLTGGTY TGKALDYILQ IIKNGMKDRM
     SKVPCYLIVL TDGMSTDRVV EPAKRLRAEQ ITVHAVGIGA ANKIELQEIA GKEERVSFGQ
     NFDALKSIKN EVVREICAEK GCEDMKADIM FLVDSSWSIG NENFRKMKIF MKNLLTKIQI
     GADKTQIGVV QFSDKTKEEF QLNRYFTQQE ISDAIDRMSL INEGTLTGKA LNFVGQYFTH
     SKGARLGAKK FLILITDGVA QDDVRDPARI LRGKDVTIFS VGVYNANRSQ LEEISGDSSL
     VFHVENFDHL KALERKLIFR VCALHDCKRI TLLDVVFVLD HSGSIKKQYQ DHMINLTIHL
     VKKADVGRDR VQFGALKYSD QPNILFYLNT YSNRSAIIEN LRKRRDTGGN TYTAKALKHA
     NALFTEEHGS RIKQNVKQML IVITDGESHD HDQLNDTALE LRNKGITIFA VGVGKANQKE
     LEGMAGNKNN TIYVDNFDKL KDVFTLVQER MCTEAPEVCH LQEADVIFLC DGSDRVSNSD
     FVTMTTFLSD LIDNFDIQSQ RMKIGMAQFG SNYQSIIELK NSLTKTQWKT QIQNVSKSGG
     FPRIDFALKK VSNMFNLHAG GRRNAGVPQT LVVITSGDPR YDVADAVKTL KDLGICVLVL
     GIGDVYKEHL LPITGNSEKI ITFQDFDKLK NVDVKKRIIR EICQSCGKTN CFMDIVVGFD
     ISTHVQGQPL FQGHPQLESY LPGILEDISS IKGVSCGAGT EAQVSLAFKV NSDQGFPAKF
     QIYQKAVFDS LLQVNVSGPT HLNAQFLRSL WDTFKDKSAS RGQVLLIFSD GLQSESNIML
     ENQSDRLREA GLDALLVVSL NTTAHHEFSS FEFGKRFDYR THLTIGMREL GKKLSQYLGN
     IAERTCCCTF CKCPGIPGPH GTRGLQAMKG SQGLKGSRGH RGEDGNPGVR GDTGPQGDKG
     IAGCPGAWGQ KGLKGFSGPK GGHGDDGIDG LDGEEGCHGF PGIKGEKGDP GSQGSPGSRG
     APGQYGEKGF PGDPGNPGQN NNIKGQKGSK GEQGRQGRSG QKGVQGSPSS RGSRGREGQR
     GLRGVSGEPG NPGPTGTLGA EGLQGPQGSQ GNPGRKGEKG SQGQKGPQGS PGLMGAKGST
     GRPGLLGKKG EPGLPGDLGP VGQTGQRGRQ GDSGIPGYGQ MGRKGVKGPR GFPGDAGQKG
     DIGNPGIPGG PGPKGFRGLA LTVGLKGEEG SRGLPGPPGQ RGIKGMAGQP VYSQCDLIRF
     LREHSPCWKE KCPAYPTELV FALDNSYDVT EESFNKTRDI ITSIVNDLNI RENNCPVGAR
     VAMVSYNSGT SYLIRWSDYN RKKQLLQQLS QIKYQDTTEP RDVGNAMRFV TRNVFKRTYA
     GANVRRVAVF FSNGQTASRS SIITATMEFS ALDISPTVFA FDERVFLEAF GFDNTGTFQV
     IPVPPNGENQ TLERLRRCAL CYDKCFPNAC IREAFLPEDS YMDVVFLIDN SRNIAKDEFK
     AVKALVSSVI DNFNIASDPL ISDSGDRIAL LSYSPWESSR RKMGTVKTEF DFITYDNQLL
     MKNHIQTSFQ QLNGEATIGR ALLWTTENLF PETPYLRKHK VIFVVSAGEN YERKEFVKMM
     ALRAKCQGYV IFVISLGSTR KDDMEELASY PLDQHLIQLG RIHKPDLNYI AKFLKPFLYS
     VRRGFNQYPP PMLEDACRLI NLGGENIQND GFQFVTELQE DFLGGNGFIG QELNSGRESP
     FVKTEDNGSD YLVYLPSQMF EPQKLMINYE KDQKSAEIAS LTSGHENYGR KEEPDHTYEP
     GDVSLQEYYM DVAFLIDASQ RVGSDEFKEV KAFITSVLDY FHIAPTPLTS TLGDRVAVLS
     YSPPGYMPNT EECPVYLEFD LVTYNSIHQM KHHLQDSQQL NGDVFIGHAL QWTIDNVFVG
     TPNLRKNKVI FVISAGETNS LDKDVLRNVS LRAKCQGYSI FVFSFGPKHN DKELEELASH
     PLDHHLVQLG RTHKPDWNYI IKFVKPFVHL IRRAINKYPT EDMKATCVNM TSPNPENGGT
     ENTVLLLPGI YEIKTENGDL FDEFDSQAQH LLVLGNNHSS GSETATDLMQ KLYLLFSTEK
     LAMKDKEKAH LEEISALVVD KQQEKEDKEM EATDI
//