ID CO6A5_HUMAN Reviewed; 2615 AA.
AC A8TX70; A9J6L2; A9J6L4; A9J6L6; A9J6L7; A9J6M0; A9J6M1; A9J6M2; B5MEA7;
AC Q6ZW26; Q8NA36;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 127.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND POSSIBLE
RP 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., Rohde K.,
RA Schulz H., Wahn U., Hubner N., Lee Y.-A.;
RT "Variants in a novel epidermal collagen gene (COL29A1) are associated with
RT atopic dermatitis.";
RL PLoS Biol. 5:1952-1961(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-455; PRO-1280;
RP 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 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2096-2615 (ISOFORM 1), AND VARIANTS ARG-2188
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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. {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 -!- TISSUE SPECIFICITY: Expressed in skin, followed by lung, small
CC intestine, colon and testis. In skin, it is expressed in the epidermis
CC with strongest staining in suprabasal viable layers. In ATOD patients,
CC it is absent in the most differentiated upper spinous and granular
CC layers (at protein level). {ECO:0000269|PubMed:17850181}.
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. {ECO:0000250}.
CC -!- DISEASE: Note=Patients affected by atopic dermatitis display an
CC abnormal distribution of COL29A1 mRNA and protein in skin suggesting
CC that COL29A1 may be involved in the pathogenesis of the disease.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04092.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04092.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC85681.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 CCDS; CCDS93385.1; -. [A8TX70-2]
DR RefSeq; NP_001265227.1; NM_001278298.1.
DR RefSeq; NP_694996.5; NM_153264.6. [A8TX70-2]
DR AlphaFoldDB; A8TX70; -.
DR SMR; A8TX70; -.
DR BioGRID; 129134; 3.
DR STRING; 9606.ENSP00000265379; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyCosmos; A8TX70; 4 sites, No reported glycans.
DR GlyGen; A8TX70; 4 sites.
DR iPTMnet; A8TX70; -.
DR PhosphoSitePlus; A8TX70; -.
DR BioMuta; COL6A5; -.
DR EPD; A8TX70; -.
DR jPOST; A8TX70; -.
DR MassIVE; A8TX70; -.
DR PaxDb; 9606-ENSP00000265379; -.
DR PeptideAtlas; A8TX70; -.
DR ProteomicsDB; 2486; -. [A8TX70-1]
DR ProteomicsDB; 2487; -. [A8TX70-2]
DR Pumba; A8TX70; -.
DR DNASU; 256076; -.
DR Ensembl; ENST00000312481.11; ENSP00000309762.7; ENSG00000172752.16. [A8TX70-1]
DR Ensembl; ENST00000512836.6; ENSP00000422898.2; ENSG00000172752.16. [A8TX70-2]
DR GeneID; 256076; -.
DR KEGG; hsa:256076; -.
DR UCSC; uc062ntw.1; human. [A8TX70-1]
DR AGR; HGNC:26674; -.
DR CTD; 256076; -.
DR DisGeNET; 256076; -.
DR GeneCards; COL6A5; -.
DR HGNC; HGNC:26674; COL6A5.
DR MIM; 611916; gene.
DR neXtProt; NX_A8TX70; -.
DR OpenTargets; ENSG00000172752; -.
DR PharmGKB; PA165696956; -.
DR VEuPathDB; HostDB:ENSG00000172752; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000162990; -.
DR HOGENOM; CLU_000182_1_0_1; -.
DR InParanoid; A8TX70; -.
DR OMA; PCWKEKC; -.
DR OrthoDB; 5359724at2759; -.
DR PhylomeDB; A8TX70; -.
DR PathwayCommons; 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 BioGRID-ORCS; 256076; 7 hits in 315 CRISPR screens.
DR GenomeRNAi; 256076; -.
DR Pharos; A8TX70; Tbio.
DR PRO; PR:A8TX70; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; A8TX70; Protein.
DR Bgee; ENSG00000172752; Expressed in upper leg skin and 42 other cell types or tissues.
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 CDD; cd01472; vWA_collagen; 2.
DR CDD; cd01450; vWFA_subfamily_ECM; 5.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 9.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR22588:SF4; COLLAGEN ALPHA-5(VI) CHAIN; 1.
DR PANTHER; PTHR22588; UNCHARACTERIZED; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00092; VWA; 9.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF53300; vWA-like; 10.
DR PROSITE; PS50234; VWFA; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2615
FT /note="Collagen alpha-5(VI) chain"
FT /id="PRO_5000294475"
FT DOMAIN 30..209
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 236..413
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 442..612
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 628..797
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 814..987
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1005..1178
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1194..1376
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1395..1446
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1434..1490
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1464..1520
FT /note="Collagen-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 1524..1580
FT /note="Collagen-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 1579..1629
FT /note="Collagen-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 1674..1729
FT /note="Collagen-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1758..1965
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1963..2154
FT /note="VWFA 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2291..2487
FT /note="VWFA 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 19..1394
FT /note="Nonhelical region"
FT REGION 1395..1728
FT /note="Triple-helical region"
FT REGION 1404..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..2615
FT /note="Nonhelical region"
FT MOTIF 1430..1432
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1515..1554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2526
FT /note="L -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033912"
FT VAR_SEQ 2527..2615
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033913"
FT VARIANT 455
FT /note="E -> K (in dbSNP:rs1453241)"
FT /evidence="ECO:0000269|PubMed:18276594"
FT /id="VAR_059234"
FT VARIANT 641
FT /note="N -> H (in dbSNP:rs9882852)"
FT /id="VAR_059235"
FT VARIANT 805
FT /note="H -> R (in dbSNP:rs16827168)"
FT /id="VAR_059236"
FT VARIANT 982
FT /note="D -> G (in dbSNP:rs11917356)"
FT /id="VAR_059237"
FT VARIANT 1114
FT /note="I -> M (in dbSNP:rs1353613)"
FT /id="VAR_059238"
FT VARIANT 1280
FT /note="T -> P (in dbSNP:rs12488457)"
FT /evidence="ECO:0000269|PubMed:18276594"
FT /id="VAR_059239"
FT VARIANT 1477
FT /note="C -> S (in dbSNP:rs1497312)"
FT /id="VAR_059240"
FT VARIANT 1589
FT /note="S -> P (in dbSNP:rs16827497)"
FT /id="VAR_059241"
FT VARIANT 2175
FT /note="D -> N (in dbSNP:rs60021408)"
FT /id="VAR_061119"
FT VARIANT 2188
FT /note="Q -> R (in dbSNP:rs9883988)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:18276594"
FT /id="VAR_043607"
FT VARIANT 2205
FT /note="G -> D (in dbSNP:rs819085)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:18276594"
FT /id="VAR_043608"
FT CONFLICT 2482
FT /note="K -> R (in Ref. 4; BAC04092)"
FT /evidence="ECO:0000305"
FT CONFLICT 2512
FT /note="S -> P (in Ref. 4; BAC04092)"
FT /evidence="ECO:0000305"
FT CONFLICT 2560
FT /note="S -> N (in Ref. 2; CAP20002/CAP20003 and 4;
FT BAC04092)"
FT /evidence="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
//
