ID MATN2_HUMAN Reviewed; 956 AA. AC O00339; A8K106; E7EW74; E9PD48; E9PGL2; Q6UWA5; Q7Z5X1; Q8NDE6; AC Q96FT5; Q9NSZ1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 13-FEB-2019, entry version 184. DE RecName: Full=Matrilin-2; DE Flags: Precursor; GN Name=MATN2; ORFNames=UNQ193/PRO219; 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] (ISOFORMS 1 AND 2). RX PubMed=11124542; RA Muratoglu S., Krysan K., Balazs M., Sheng H., Zakany R., Modis L., RA Kiss I., Deak F.; RT "Primary structure of human matrilin-2, chromosome location of the RT MATN2 gene and conservation of an AT-AC intron in matrilin genes."; RL Cytogenet. Cell Genet. 90:323-327(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP MET-187. RC TISSUE=Brain; 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). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT RP GLU-356. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 242-956 (ISOFORM 1), AND VARIANT RP GLU-356. RC TISSUE=Brain, and Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 644-956. RX PubMed=9083061; DOI=10.1074/jbc.272.14.9268; RA Deak F., Piecha D., Bachrati C., Paulsson M., Kiss I.; RT "Primary structure and expression of matrilin-2, the closest relative RT of cartilage matrix protein within the von Willebrand factor type A- RT like module superfamily."; RL J. Biol. Chem. 272:9268-9274(1997). CC -!- FUNCTION: Involved in matrix assembly. {ECO:0000250}. CC -!- INTERACTION: CC O15265:ATXN7; NbExp=2; IntAct=EBI-949020, EBI-708350; CC O00555:CACNA1A; NbExp=2; IntAct=EBI-949020, EBI-766279; CC O68704:yopK (xeno); NbExp=2; IntAct=EBI-949020, EBI-20592411; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long; CC IsoId=O00339-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=O00339-2; Sequence=VSP_001399; CC Name=3; CC IsoId=O00339-3; Sequence=VSP_013284; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O00339-4; Sequence=VSP_014540; CC Note=No experimental confirmation available.; CC -!- SEQUENCE CAUTION: CC Sequence=CAD38787.1; 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; U69263; AAC51260.2; -; mRNA. DR EMBL; AY358895; AAQ89254.1; -; mRNA. DR EMBL; AL137638; CAB70853.2; -; mRNA. DR EMBL; AK289721; BAF82410.1; -; mRNA. DR EMBL; AL833931; CAD38787.1; ALT_INIT; mRNA. DR EMBL; AP002906; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003352; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010444; AAH10444.1; -; mRNA. DR EMBL; BC016394; AAH16394.1; -; mRNA. DR CCDS; CCDS55264.1; -. [O00339-1] DR CCDS; CCDS55265.1; -. [O00339-2] DR CCDS; CCDS83309.1; -. [O00339-3] DR RefSeq; NP_001304677.1; NM_001317748.1. [O00339-3] DR RefSeq; NP_002371.3; NM_002380.4. [O00339-1] DR RefSeq; NP_085072.2; NM_030583.3. [O00339-2] DR UniGene; Hs.189445; -. DR UniGene; Hs.737531; -. DR ProteinModelPortal; O00339; -. DR BioGrid; 110317; 57. DR DIP; DIP-47267N; -. DR IntAct; O00339; 7. DR MINT; O00339; -. DR STRING; 9606.ENSP00000430487; -. DR iPTMnet; O00339; -. DR PhosphoSitePlus; O00339; -. DR BioMuta; MATN2; -. DR jPOST; O00339; -. DR MaxQB; O00339; -. DR PaxDb; O00339; -. DR PeptideAtlas; O00339; -. DR PRIDE; O00339; -. DR ProteomicsDB; 47856; -. DR ProteomicsDB; 47857; -. [O00339-2] DR ProteomicsDB; 47858; -. [O00339-3] DR ProteomicsDB; 47859; -. [O00339-4] DR Ensembl; ENST00000254898; ENSP00000254898; ENSG00000132561. [O00339-1] DR Ensembl; ENST00000520016; ENSP00000430487; ENSG00000132561. [O00339-1] DR Ensembl; ENST00000521689; ENSP00000429977; ENSG00000132561. [O00339-2] DR Ensembl; ENST00000522025; ENSP00000429010; ENSG00000132561. [O00339-4] DR Ensembl; ENST00000524308; ENSP00000430221; ENSG00000132561. [O00339-3] DR GeneID; 4147; -. DR KEGG; hsa:4147; -. DR UCSC; uc003yic.4; human. [O00339-1] DR CTD; 4147; -. DR DisGeNET; 4147; -. DR EuPathDB; HostDB:ENSG00000132561.13; -. DR GeneCards; MATN2; -. DR HGNC; HGNC:6908; MATN2. DR HPA; CAB033879; -. DR MIM; 602108; gene. DR neXtProt; NX_O00339; -. DR OpenTargets; ENSG00000132561; -. DR PharmGKB; PA30651; -. DR eggNOG; ENOG410IR7H; Eukaryota. DR eggNOG; ENOG410XSTY; LUCA. DR GeneTree; ENSGT00940000158008; -. DR HOVERGEN; HBG056906; -. DR InParanoid; O00339; -. DR OMA; KDVCQAV; -. DR OrthoDB; 1174178at2759; -. DR TreeFam; TF330078; -. DR ChiTaRS; MATN2; human. DR GeneWiki; MATN2; -. DR GenomeRNAi; 4147; -. DR PRO; PR:O00339; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000132561; Expressed in 229 organ(s), highest expression level in tibia. DR ExpressionAtlas; O00339; baseline and differential. DR Genevisible; O00339; HS. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL. DR GO; GO:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0031104; P:dendrite regeneration; IEA:Ensembl. DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl. DR GO; GO:0003429; P:growth plate cartilage chondrocyte morphogenesis; IBA:GO_Central. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR Gene3D; 1.20.5.30; -; 1. DR Gene3D; 3.40.50.410; -; 2. DR InterPro; IPR026823; cEGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR030747; Matrilin-2. DR InterPro; IPR036337; Matrilin_cc_sf. DR InterPro; IPR019466; Matrilin_coiled-coil_trimer. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR44734:SF1; PTHR44734:SF1; 1. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF07645; EGF_CA; 2. DR Pfam; PF10393; Matrilin_ccoil; 1. DR Pfam; PF00092; VWA; 2. DR SMART; SM00181; EGF; 10. DR SMART; SM00179; EGF_CA; 10. DR SMART; SM01279; Matrilin_ccoil; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF53300; SSF53300; 2. DR SUPFAM; SSF57184; SSF57184; 3. DR SUPFAM; SSF58002; SSF58002; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 9. DR PROSITE; PS01186; EGF_2; 9. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS50234; VWFA; 2. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Disulfide bond; KW EGF-like domain; Glycoprotein; Polymorphism; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 956 Matrilin-2. FT /FTId=PRO_0000007655. FT DOMAIN 57 232 VWFA 1. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT DOMAIN 238 278 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 279 319 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 320 360 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 361 401 EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 402 442 EGF-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 443 483 EGF-like 6. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 484 524 EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 525 565 EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 566 606 EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 607 647 EGF-like 10. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 655 830 VWFA 2. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT COILED 917 955 {ECO:0000255}. FT CARBOHYD 221 221 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 242 253 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 249 262 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 264 277 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 283 294 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 290 303 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 305 318 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 324 335 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 331 344 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 346 359 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 365 376 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 372 385 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 387 400 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 406 417 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 413 426 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 428 441 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 447 458 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 454 467 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 469 482 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 488 499 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 495 508 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 510 523 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 529 540 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 536 549 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 551 564 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 570 581 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 577 590 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 592 605 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 611 622 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 618 631 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 633 646 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT VAR_SEQ 1 284 Missing (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_014540. FT VAR_SEQ 361 401 Missing (in isoform 3). FT {ECO:0000303|PubMed:12975309}. FT /FTId=VSP_013284. FT VAR_SEQ 861 879 Missing (in isoform 2). FT {ECO:0000303|PubMed:11124542, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_001399. FT VARIANT 14 14 G -> A (in dbSNP:rs35804177). FT /FTId=VAR_055753. FT VARIANT 187 187 T -> M (in dbSNP:rs2290472). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_055754. FT VARIANT 356 356 K -> E (in dbSNP:rs1869609). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005}. FT /FTId=VAR_021568. FT VARIANT 599 599 A -> T (in dbSNP:rs35120814). FT /FTId=VAR_055755. FT VARIANT 855 855 T -> M (in dbSNP:rs2255317). FT /FTId=VAR_055756. FT VARIANT 932 932 V -> I (in dbSNP:rs17831160). FT /FTId=VAR_055757. FT CONFLICT 58 58 L -> P (in Ref. 3; BAF82410). FT {ECO:0000305}. FT CONFLICT 594 594 E -> V (in Ref. 1; AAC51260). FT {ECO:0000305}. FT CONFLICT 644 644 R -> G (in Ref. 7; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 755 755 L -> F (in Ref. 1; AAC51260). FT {ECO:0000305}. FT CONFLICT 890 890 N -> D (in Ref. 3; BAF82410). FT {ECO:0000305}. FT CONFLICT 935 935 L -> F (in Ref. 7; no nucleotide entry). FT {ECO:0000305}. SQ SEQUENCE 956 AA; 106837 MW; D0868FBF62744EF2 CRC64; MEKMLAGCFL LILGQIVLLP AEARERSRGR SISRGRHART HPQTALLESS CENKRADLVF IIDSSRSVNT HDYAKVKEFI VDILQFLDIG PDVTRVGLLQ YGSTVKNEFS LKTFKRKSEV ERAVKRMRHL STGTMTGLAI QYALNIAFSE AEGARPLREN VPRVIMIVTD GRPQDSVAEV AAKARDTGIL IFAIGVGQVD FNTLKSIGSE PHEDHVFLVA NFSQIETLTS VFQKKLCTAH MCSTLEHNCA HFCINIPGSY VCRCKQGYIL NSDQTTCRIQ DLCAMEDHNC EQLCVNVPGS FVCQCYSGYA LAEDGKRCVA VDYCASENHG CEHECVNADG SYLCQCHEGF ALNPDKKTCT KIDYCASSNH GCQHECVNTD DSYSCHCLKG FTLNPDKKTC RRINYCALNK PGCEHECVNM EESYYCRCHR GYTLDPNGKT CSRVDHCAQQ DHGCEQLCLN TEDSFVCQCS EGFLINEDLK TCSRVDYCLL SDHGCEYSCV NMDRSFACQC PEGHVLRSDG KTCAKLDSCA LGDHGCEHSC VSSEDSFVCQ CFEGYILRED GKTCRRKDVC QAIDHGCEHI CVNSDDSYTC ECLEGFRLAE DGKRCRRKDV CKSTHHGCEH ICVNNGNSYI CKCSEGFVLA EDGRRCKKCT EGPIDLVFVI DGSKSLGEEN FEVVKQFVTG IIDSLTISPK AARVGLLQYS TQVHTEFTLR NFNSAKDMKK AVAHMKYMGK GSMTGLALKH MFERSFTQGE GARPLSTRVP RAAIVFTDGR AQDDVSEWAS KAKANGITMY AVGVGKAIEE ELQEIASEPT NKHLFYAEDF STMDEISEKL KKGICEALED SDGRQDSPAG ELPKTVQQPT ESEPVTINIQ DLLSCSNFAV QHRYLFEEDN LLRSTQKLSH STKPSGSPLE EKHDQCKCEN LIMFQNLANE EVRKLTQRLE EMTQRMEALE NRLRYR //