THS7A_DANRE
ID THS7A_DANRE Reviewed; 1686 AA.
AC A7MBS7; E3VW06; F1QPE6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7A;
DE Flags: Precursor;
GN Name=thsd7aa {ECO:0000312|ZFIN:ZDB-GENE-060503-709};
GN Synonyms=thsd7a {ECO:0000303|PubMed:21520329};
GN ORFNames=si:dkey-12h3.1 {ECO:0000312|EMBL:AAI51898.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAI51898.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAI51898.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva {ECO:0000312|EMBL:AAI51898.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:ADO87037.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-297, FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=21520329; DOI=10.1002/dvdy.22641;
RA Wang C.H., Chen I.H., Kuo M.W., Su P.T., Lai Z.Y., Wang C.H., Huang W.C.,
RA Hoffman J., Kuo C.J., You M.S., Chuang Y.J.;
RT "Zebrafish Thsd7a is a neural protein required for angiogenic patterning
RT during development.";
RL Dev. Dyn. 240:1412-1421(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=27484901; DOI=10.1186/s12929-016-0277-9;
RA Liu L.Y., Lin M.H., Lai Z.Y., Jiang J.P., Huang Y.C., Jao L.E.,
RA Chuang Y.J.;
RT "Motor neuron-derived Thsd7a is essential for zebrafish vascular
RT development via the Notch-dll4 signaling pathway.";
RL J. Biomed. Sci. 23:59-59(2016).
RN [5]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=28814510; DOI=10.1681/asn.2017010030;
RA Tomas N.M., Meyer-Schwesinger C., von Spiegel H., Kotb A.M., Zahner G.,
RA Hoxha E., Helmchen U., Endlich N., Koch-Nolte F., Stahl R.A.K.;
RT "A Heterologous Model of Thrombospondin Type 1 Domain-Containing 7A-
RT Associated Membranous Nephropathy.";
RL J. Am. Soc. Nephrol. 28:3262-3277(2017).
CC -!- FUNCTION: Required for normal sprouting angiogenesis and normal
CC embryonic development of intersegmental vessels (ISV) (PubMed:21520329,
CC PubMed:27484901). Required for normal function of the glomerular
CC filtration barrier (PubMed:28814510). Required for normal axon
CC outgrowth on embryonic motor neurons at the level of the horizontal
CC myoseptum. Required for normal expression of notch1b, suggesting that
CC its functions in angiogenesis and neuron outgrowth are due to decreased
CC expression of notch1b (PubMed:27484901). Plays a role in actin
CC cytoskeleton rearrangement (By similarity).
CC {ECO:0000250|UniProtKB:Q69ZU6, ECO:0000269|PubMed:21520329,
CC ECO:0000269|PubMed:27484901, ECO:0000269|PubMed:28814510}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q69ZU6};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q69ZU6}.
CC Cell projection {ECO:0000250|UniProtKB:Q69ZU6}. Note=Detected on
CC podocyte foot processes. {ECO:0000250|UniProtKB:Q69ZU6}.
CC -!- DEVELOPMENTAL STAGE: Detected in larvae (at protein level)
CC (PubMed:28814510). First detected in the dorsal region of the embryo at
CC 15 hpf. Detected along the ventral edge of the neural tube from 22 to
CC 32 hpf. Highly expressed in retina, cranial ganglia, pectoral fin,
CC brain and spinal cord at 48 hpf (PubMed:21520329). Detected in primary
CC motor neurons along the ventral edge of the neuron tube at 24 hpf
CC (PubMed:27484901). {ECO:0000269|PubMed:21520329,
CC ECO:0000269|PubMed:27484901, ECO:0000269|PubMed:28814510}.
CC -!- DOMAIN: Sequence analysis combined with the expression of constructs
CC corresponding each to two or three adjacent TSP type-1 domains suggests
CC the presence of 21 TSP type-1 domains; not all of these are detected by
CC standard bioinformatic tools. {ECO:0000250|UniProtKB:Q9UPZ6}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q69ZU6}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein impairs
CC normal embryonic development of intersegmental vessels (ISV)
CC (PubMed:21520329, PubMed:27484901). Morpholino knockdown of the protein
CC causes malformation of the glomerular tufts and a reduction in the
CC number of podocytes per glomerular tuft, and causes pericardial edema
CC in many cases, probably due to impaired function of the glomerular
CC filtration barrier (PubMed:28814510). Morpholino knockdown of the
CC protein causes loss of the parachordal chain in the developing
CC vasculature and absence of laterally projecting motor axons at the
CC level of the horizontal myoseptum (PubMed:27484901).
CC {ECO:0000269|PubMed:21520329, ECO:0000269|PubMed:27484901,
CC ECO:0000269|PubMed:28814510}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADO87037.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; CR381594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR735126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR627498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151897; AAI51898.1; -; mRNA.
DR EMBL; HQ267705; ADO87037.1; ALT_TERM; mRNA.
DR AlphaFoldDB; A7MBS7; -.
DR STRING; 7955.ENSDARP00000082128; -.
DR ZFIN; ZDB-GENE-060503-709; thsd7aa.
DR HOGENOM; CLU_004819_0_0_1; -.
DR TreeFam; TF329791; -.
DR Reactome; R-DRE-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:A7MBS7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0048675; P:axon extension; IMP:ZFIN.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:ZFIN.
DR GO; GO:0003094; P:glomerular filtration; IMP:ZFIN.
DR GO; GO:0032835; P:glomerulus development; IMP:ZFIN.
DR GO; GO:0072015; P:podocyte development; IMP:ZFIN.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:ZFIN.
DR Gene3D; 2.20.100.10; -; 10.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF19028; TSP1_spondin; 3.
DR Pfam; PF00090; TSP_1; 4.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF82895; SSF82895; 8.
DR PROSITE; PS50092; TSP1; 11.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Cell projection; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..1686
FT /note="Thrombospondin type-1 domain-containing protein 7A"
FT /id="PRO_5002713241"
FT TOPO_DOM 37..1635
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1636..1656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1657..1686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 44..103
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 107..181
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 183..236
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 385..441
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 448..535
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 537..596
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 656..717
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 718..797
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 799..859
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 860..932
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 934..985
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 988..1061
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1063..1123
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1124..1191
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1193..1247
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1248..1311
FT /note="TSP type-1 16"
FT /evidence="ECO:0000255"
FT DOMAIN 1313..1368
FT /note="TSP type-1 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1369..1439
FT /note="TSP type-1 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1441..1502
FT /note="TSP type-1 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 257..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 460..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 480..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 491..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 657..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 668..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 711..716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 729..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 756..796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 767..780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 800..842
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 811..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 852..858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1000..1056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1022..1060
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1033..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1064..1101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1075..1079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1118..1122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1240..1246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1259..1306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1267..1310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1278..1291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1314..1352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1325..1329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1362..1367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1378..1434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1385..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1396..1415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1442..1486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1453..1457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1496..1501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 1686 AA; 187338 MW; 39385A2502445C5B CRC64;
MGLASRAPGK GGTSAGALAS LFRVALLFFG LWDVQTQTVA NTRPTYIWQT GPWGRCMGSE
CGPGGSQSRA VWCAHSEGWT TLHTNCQQSE RPSNQQSCFR VCDWHKELYD WQLGAWNQCV
PVSMRNAGVP RPAVCTRGEE GIQTREVGCV HKSDGVPAED AICEYFEPKP RLEQACLIPC
PRDCVVSEFS PWTSCSKSCG MGLQNRLRSV LAPPLFGGSA CPNLTEFRTC QPGKCEGVES
LHSLRVGPWG QCMASPIRQA RDTGEARVPK AERKAKRDRQ ARQERQGKRR KNKEKKELRE
SKGERVRERV KEKKRMRDPE TRELIKKKRT RNRQNRQGLK FWDLQVGYQT REVTCVHRSG
STASISQCTQ QTLPVTYQAC VISKDCEVSE WSDWSVCSKE CYDLNGRKGQ RTRTRQVQQF
PVGGGAECPE LEESEPCSPQ GEGIPPCVVY NWRSTEWSDC RVDVLLSQQD RRRSNQTGLC
GGGVQTREVY CVQAPSETSS NLGSLKSKDA LRPVNSDLCL GVPHNTTQLC HIPCPVECEV
SAWSAWGPCT FENCQDQSTK KGFKLRKRKI MNEPTGGTGN CPHLTEAIPC EEPSCYDWLL
VKLEECVPDN DKVCGPGTQN PQVQCINSDG EFVDRQLCRD AILPMPVLCE VSCPKDCVLS
PWTSWSLCSN TCSGKNSEGK QTRARSILAY NAGDGGVQCP NSSALQEVRS CNDHPCTVYH
WQTGPWGQCI EDTSVPSANS SISRAVPGTA VNDAFCSVGM QTRKVICVRV NVGQVPPKKC
PESLRPETVR PCLLPCKRDC VVTPYSDWTP CPSICQTGGS VKKKQSRKRI IIQLPANGGQ
DCPEVLFQEK DCDASSVCPG YRWKTHKWRR CQLVPWSIRQ DSPGAQETCG PGLQARAVSC
KKLDSGPADV AACLKFAGPM PQLTQSCQLP CQDDCQLTAW SKFSTCAADC VGVRTRKRTL
VGKSKKREQC KNTQMYPLSE TQYCPCNKYN AQPVGNWSDC ILPEGRVEGL LGMKVQGDIK
ECGQGYRYQA MVCYDQDNRL VETSRCNSHG YIEEACIIPC PSDCKLSEWS NWSRCSKSCG
SGVKVRSKWL REKPYNGGRP CPKLDHVNQA QVYEVVPCLS DCSQYVWVAE PWSVWKVSNV
DLKENCGEGV QTRKVRCMQN TVDGPSDPVE DYLCDPEEMP LGARESKLPC PEDCVLTDWG
SWSRCPLPCN VNSTRQRSAS PIRQPSERKQ CPSTTEKEIC TLNSNCFHYS YNITDWSTCQ
LSERAVCGVG FKTRMLDCVR SDSKSVDLKF CEELGLEKKW QMNASCVVEC PVNCQLSDWS
SWSECSHTCG LAGKLWRRRT VIQASQGDGR PCSSQLEQWK PCPVKPCFSW RYSVWSPCKS
EGARCGEGLR FRNVSCFVSD GSGKDAGSMV DEELCGDLEQ TVDGDKQIIL QESCTVPCPG
ECYLTDWTMW SPCQLSCIGG DDLGFGSVQV RSRAVLAQEP ENLLQCPEQE WEARPCTEGQ
CYDYKWMTGA WRGSSRQVWC QRSDGLNVTG GCQSTTEPVS DRSCDPACDK PRSICTEAGI
CGCEEGYTEV MTSDGVLDQC TVIPVLEIPT AGDSKADVKT IRALNPTEPT ANMPGRAGRT
WFLQPFGPDG KLKTWVYGVA AGAFVLLVFI VSMTYLACKK PKKPQRRQMN NRLKPLTLAY
DGDADM
