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CO6A5_HUMAN
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   03-AUG-2022, entry version 120.
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};
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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   AlphaFoldDB; A8TX70; -.
DR   SMR; A8TX70; -.
DR   BioGRID; 129134; 2.
DR   STRING; 9606.ENSP00000265379; -.
DR   ChEMBL; CHEMBL2364188; -.
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; A8TX70; -.
DR   PeptideAtlas; A8TX70; -.
DR   PRIDE; A8TX70; -.
DR   ProteomicsDB; 2486; -. [A8TX70-1]
DR   ProteomicsDB; 2487; -. [A8TX70-2]
DR   DNASU; 256076; -.
DR   Ensembl; ENST00000312481.11; ENSP00000309762.7; ENSG00000172752.15. [A8TX70-1]
DR   GeneID; 256076; -.
DR   KEGG; hsa:256076; -.
DR   UCSC; uc062ntw.1; human. [A8TX70-1]
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; ESMCTEA; -.
DR   OrthoDB; 1049829at2759; -.
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 261 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 41 other 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   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 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
 
 
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